NO328377B1 - Humanisert, monoklonalt antistoff som binder ErbB2/HER2, farmasoytisk formulering, immunkonjugat, isolert nukleinsyre, vektor, vertscelle og fremgangsmate for fremstilling av antistoff. - Google Patents

Humanisert, monoklonalt antistoff som binder ErbB2/HER2, farmasoytisk formulering, immunkonjugat, isolert nukleinsyre, vektor, vertscelle og fremgangsmate for fremstilling av antistoff. Download PDF

Info

Publication number: NO328377B1
Authority: NO; Norway
Prior art keywords: antibody; erbb2; cells; antibodies; cancer
Prior art date: 1999-06-25

Application number

NO20016329A

Other languages

English (en)

Norwegian (no)

Other versions

NO20016329L (no

NO20016329D0 (no

Inventor

Leonard G Presta

Camellia W Adams

Mark Sliwkowski

Original Assignee

Genentech Inc

Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)

1999-06-25

Filing date

2001-12-21

Publication date

2010-02-08

Family has litigation

First worldwide family litigation filed litigation Critical https://patents.darts-ip.com/?family=22495168&utm_source=google_patent&utm_medium=platform_link&utm_campaign=public_patent_search&patent=NO328377(B1) "Global patent litigation dataset” by Darts-ip is licensed under a Creative Commons Attribution 4.0 International License.

2001-12-21 Application filed by Genentech Inc filed Critical Genentech Inc

2001-12-21 Publication of NO20016329D0 publication Critical patent/NO20016329D0/no

2002-02-25 Publication of NO20016329L publication Critical patent/NO20016329L/no

2010-02-08 Publication of NO328377B1 publication Critical patent/NO328377B1/no

Links

150000007523 nucleic acids Chemical class 0.000 title claims description 50
108020004707 nucleic acids Proteins 0.000 title claims description 48
102000039446 nucleic acids Human genes 0.000 title claims description 48
239000013598 vector Substances 0.000 title claims description 34
102100030086 Receptor tyrosine-protein kinase erbB-2 Human genes 0.000 title claims description 23
229940127121 immunoconjugate Drugs 0.000 title claims description 20
101001012157 Homo sapiens Receptor tyrosine-protein kinase erbB-2 Proteins 0.000 title claims description 8
239000008194 pharmaceutical composition Substances 0.000 title claims description 7
238000003452 antibody preparation method Methods 0.000 title 1
210000004027 cell Anatomy 0.000 claims description 325
238000000034 method Methods 0.000 claims description 89
125000003275 alpha amino acid group Chemical group 0.000 claims description 43
229940127089 cytotoxic agent Drugs 0.000 claims description 37
102000008394 Immunoglobulin Fragments Human genes 0.000 claims description 30
108010021625 Immunoglobulin Fragments Proteins 0.000 claims description 30
238000004519 manufacturing process Methods 0.000 claims description 19
239000002254 cytotoxic agent Substances 0.000 claims description 17
108010054477 Immunoglobulin Fab Fragments Proteins 0.000 claims description 16
102000001706 Immunoglobulin Fab Fragments Human genes 0.000 claims description 16
231100000599 cytotoxic agent Toxicity 0.000 claims description 16
238000004113 cell culture Methods 0.000 claims description 13
241000699802 Cricetulus griseus Species 0.000 claims description 5
239000003937 drug carrier Substances 0.000 claims description 5
210000004962 mammalian cell Anatomy 0.000 claims description 5
210000001672 ovary Anatomy 0.000 claims description 5
239000000546 pharmaceutical excipient Substances 0.000 claims description 4
239000003381 stabilizer Substances 0.000 claims description 4
239000007864 aqueous solution Substances 0.000 claims description 2
239000006143 cell culture medium Substances 0.000 claims description 2
238000002156 mixing Methods 0.000 claims description 2
238000000605 extraction Methods 0.000 claims 1
206010028980 Neoplasm Diseases 0.000 description 140
102000001301 EGF receptor Human genes 0.000 description 134
108060006698 EGF receptor Proteins 0.000 description 134
201000011510 cancer Diseases 0.000 description 98
230000027455 binding Effects 0.000 description 95
241000282414 Homo sapiens Species 0.000 description 89
108090000623 proteins and genes Proteins 0.000 description 86
239000003446 ligand Substances 0.000 description 72
230000004913 activation Effects 0.000 description 69
102400000058 Neuregulin-1 Human genes 0.000 description 62
108090000556 Neuregulin-1 Proteins 0.000 description 56
239000003814 drug Substances 0.000 description 54
102000004169 proteins and genes Human genes 0.000 description 54
239000000427 antigen Substances 0.000 description 53
235000018102 proteins Nutrition 0.000 description 53
238000002360 preparation method Methods 0.000 description 52
229940079593 drug Drugs 0.000 description 51
108091007433 antigens Proteins 0.000 description 49
102000036639 antigens Human genes 0.000 description 49
238000003556 assay Methods 0.000 description 44
108090000765 processed proteins & peptides Proteins 0.000 description 44
238000011282 treatment Methods 0.000 description 44
239000012634 fragment Substances 0.000 description 41
102000004196 processed proteins & peptides Human genes 0.000 description 39
229920001184 polypeptide Polymers 0.000 description 38
230000014509 gene expression Effects 0.000 description 34
230000012010 growth Effects 0.000 description 28
206010006187 Breast cancer Diseases 0.000 description 27
208000026310 Breast neoplasm Diseases 0.000 description 26
108020004414 DNA Proteins 0.000 description 26
OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 26
239000003795 chemical substances by application Substances 0.000 description 26
201000010099 disease Diseases 0.000 description 26
208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 26
239000002609 medium Substances 0.000 description 26
102000005962 receptors Human genes 0.000 description 26
108020003175 receptors Proteins 0.000 description 26
238000011160 research Methods 0.000 description 26
102000004190 Enzymes Human genes 0.000 description 25
108090000790 Enzymes Proteins 0.000 description 25
229940088598 enzyme Drugs 0.000 description 25
230000002018 overexpression Effects 0.000 description 25
OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 25
241001529936 Murinae Species 0.000 description 24
239000002246 antineoplastic agent Substances 0.000 description 24
230000000694 effects Effects 0.000 description 24
230000005764 inhibitory process Effects 0.000 description 24
238000006467 substitution reaction Methods 0.000 description 24
108060003951 Immunoglobulin Proteins 0.000 description 23
238000004458 analytical method Methods 0.000 description 23
102000018358 immunoglobulin Human genes 0.000 description 23
239000000047 product Substances 0.000 description 23
-1 benzodopa Chemical class 0.000 description 22
230000004044 response Effects 0.000 description 22
241001465754 Metazoa Species 0.000 description 21
230000026731 phosphorylation Effects 0.000 description 21
238000006366 phosphorylation reaction Methods 0.000 description 21
108010076504 Protein Sorting Signals Proteins 0.000 description 20
240000004808 Saccharomyces cerevisiae Species 0.000 description 20
235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 20
229940002612 prodrug Drugs 0.000 description 20
239000000651 prodrug Substances 0.000 description 20
101800004564 Transforming growth factor alpha Proteins 0.000 description 19
230000004071 biological effect Effects 0.000 description 19
108700020796 Oncogene Proteins 0.000 description 18
102400001320 Transforming growth factor alpha Human genes 0.000 description 18
230000010056 antibody-dependent cellular cytotoxicity Effects 0.000 description 18
229940088597 hormone Drugs 0.000 description 18
239000005556 hormone Substances 0.000 description 18
230000002401 inhibitory effect Effects 0.000 description 18
101710100968 Receptor tyrosine-protein kinase erbB-2 Proteins 0.000 description 17
230000001965 increasing effect Effects 0.000 description 17
239000012528 membrane Substances 0.000 description 17
210000004379 membrane Anatomy 0.000 description 17
VBEQCZHXXJYVRD-GACYYNSASA-N uroanthelone Chemical compound C([C@@H](C(=O)N[C@H](C(=O)N[C@@H](CS)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CS)C(=O)N[C@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)NCC(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O)C(C)C)[C@@H](C)O)NC(=O)[C@H](CO)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CO)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@@H](NC(=O)[C@H](CC=1NC=NC=1)NC(=O)[C@H](CCSC)NC(=O)[C@H](CS)NC(=O)[C@@H](NC(=O)CNC(=O)CNC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CS)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)CNC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CO)NC(=O)[C@H](CO)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CS)NC(=O)CNC(=O)[C@H]1N(CCC1)C(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CO)NC(=O)[C@@H](N)CC(N)=O)C(C)C)[C@@H](C)CC)C1=CC=C(O)C=C1 VBEQCZHXXJYVRD-GACYYNSASA-N 0.000 description 17
235000001014 amino acid Nutrition 0.000 description 16
150000001875 compounds Chemical class 0.000 description 16
210000004408 hybridoma Anatomy 0.000 description 16
206010009944 Colon cancer Diseases 0.000 description 15
101800003838 Epidermal growth factor Proteins 0.000 description 15
102400001368 Epidermal growth factor Human genes 0.000 description 15
239000003623 enhancer Substances 0.000 description 15
229940116977 epidermal growth factor Drugs 0.000 description 15
238000000338 in vitro Methods 0.000 description 15
210000002966 serum Anatomy 0.000 description 15
230000006907 apoptotic process Effects 0.000 description 14
239000003550 marker Substances 0.000 description 14
239000000203 mixture Substances 0.000 description 14
230000004048 modification Effects 0.000 description 14
238000012986 modification Methods 0.000 description 14
239000000758 substrate Substances 0.000 description 14
210000001519 tissue Anatomy 0.000 description 14
206010061818 Disease progression Diseases 0.000 description 13
241000699666 Mus <mouse, genus> Species 0.000 description 13
108091007491 NSP3 Papain-like protease domains Proteins 0.000 description 13
102100024952 Protein CBFA2T1 Human genes 0.000 description 13
230000001419 dependent effect Effects 0.000 description 13
230000005750 disease progression Effects 0.000 description 13
239000002502 liposome Substances 0.000 description 13
230000001404 mediated effect Effects 0.000 description 13
230000010076 replication Effects 0.000 description 13
230000003442 weekly effect Effects 0.000 description 13
102000004127 Cytokines Human genes 0.000 description 12
108090000695 Cytokines Proteins 0.000 description 12
AOJJSUZBOXZQNB-TZSSRYMLSA-N Doxorubicin Chemical compound O([C@H]1C[C@@](O)(CC=2C(O)=C3C(=O)C=4C=CC=C(C=4C(=O)C3=C(O)C=21)OC)C(=O)CO)[C@H]1C[C@H](N)[C@H](O)[C@H](C)O1 AOJJSUZBOXZQNB-TZSSRYMLSA-N 0.000 description 12
108091054455 MAP kinase family Proteins 0.000 description 12
102000043136 MAP kinase family Human genes 0.000 description 12
238000006243 chemical reaction Methods 0.000 description 12
230000000295 complement effect Effects 0.000 description 12
LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 12
238000001727 in vivo Methods 0.000 description 12
230000001939 inductive effect Effects 0.000 description 12
239000002953 phosphate buffered saline Substances 0.000 description 12
230000001225 therapeutic effect Effects 0.000 description 12
210000004881 tumor cell Anatomy 0.000 description 12
108091003079 Bovine Serum Albumin Proteins 0.000 description 11
WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 11
241000699670 Mus sp. Species 0.000 description 11
206010060862 Prostate cancer Diseases 0.000 description 11
208000000236 Prostatic Neoplasms Diseases 0.000 description 11
229940024606 amino acid Drugs 0.000 description 11
150000001413 amino acids Chemical class 0.000 description 11
230000015572 biosynthetic process Effects 0.000 description 11
230000035772 mutation Effects 0.000 description 11
239000002243 precursor Substances 0.000 description 11
230000004083 survival effect Effects 0.000 description 11
238000002560 therapeutic procedure Methods 0.000 description 11
241000588724 Escherichia coli Species 0.000 description 10
241000829100 Macaca mulatta polyomavirus 1 Species 0.000 description 10
230000008859 change Effects 0.000 description 10
238000010367 cloning Methods 0.000 description 10
239000012636 effector Substances 0.000 description 10
238000005755 formation reaction Methods 0.000 description 10
230000006870 function Effects 0.000 description 10
230000004927 fusion Effects 0.000 description 10
238000011534 incubation Methods 0.000 description 10
201000009030 Carcinoma Diseases 0.000 description 9
108091026890 Coding region Proteins 0.000 description 9
208000001333 Colorectal Neoplasms Diseases 0.000 description 9
238000002965 ELISA Methods 0.000 description 9
241000124008 Mammalia Species 0.000 description 9
102100033762 Proheparin-binding EGF-like growth factor Human genes 0.000 description 9
230000030833 cell death Effects 0.000 description 9
230000001472 cytotoxic effect Effects 0.000 description 9
238000005516 engineering process Methods 0.000 description 9
239000003102 growth factor Substances 0.000 description 9
239000001963 growth medium Substances 0.000 description 9
239000013612 plasmid Substances 0.000 description 9
230000000638 stimulation Effects 0.000 description 9
238000013518 transcription Methods 0.000 description 9
230000035897 transcription Effects 0.000 description 9
108050008874 Annexin Proteins 0.000 description 8
102000000412 Annexin Human genes 0.000 description 8
241000894006 Bacteria Species 0.000 description 8
206010055113 Breast cancer metastatic Diseases 0.000 description 8
GHASVSINZRGABV-UHFFFAOYSA-N Fluorouracil Chemical compound FC1=CNC(=O)NC1=O GHASVSINZRGABV-UHFFFAOYSA-N 0.000 description 8
101000871708 Homo sapiens Proheparin-binding EGF-like growth factor Proteins 0.000 description 8
FBOZXECLQNJBKD-ZDUSSCGKSA-N L-methotrexate Chemical compound C=1N=C2N=C(N)N=C(N)C2=NC=1CN(C)C1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 FBOZXECLQNJBKD-ZDUSSCGKSA-N 0.000 description 8
101800002648 Neuregulin-1 Proteins 0.000 description 8
206010035226 Plasma cell myeloma Diseases 0.000 description 8
NKANXQFJJICGDU-QPLCGJKRSA-N Tamoxifen Chemical compound C=1C=CC=CC=1C(/CC)=C(C=1C=CC(OCCN(C)C)=CC=1)/C1=CC=CC=C1 NKANXQFJJICGDU-QPLCGJKRSA-N 0.000 description 8
239000002253 acid Substances 0.000 description 8
125000000539 amino acid group Chemical group 0.000 description 8
239000000872 buffer Substances 0.000 description 8
230000004663 cell proliferation Effects 0.000 description 8
238000002512 chemotherapy Methods 0.000 description 8
230000004540 complement-dependent cytotoxicity Effects 0.000 description 8
231100000433 cytotoxic Toxicity 0.000 description 8
238000011161 development Methods 0.000 description 8
230000018109 developmental process Effects 0.000 description 8
239000013604 expression vector Substances 0.000 description 8
229960002949 fluorouracil Drugs 0.000 description 8
239000007788 liquid Substances 0.000 description 8
229960000485 methotrexate Drugs 0.000 description 8
201000000050 myeloid neoplasm Diseases 0.000 description 8
230000037361 pathway Effects 0.000 description 8
YBYRMVIVWMBXKQ-UHFFFAOYSA-N phenylmethanesulfonyl fluoride Chemical compound FS(=O)(=O)CC1=CC=CC=C1 YBYRMVIVWMBXKQ-UHFFFAOYSA-N 0.000 description 8
XJMOSONTPMZWPB-UHFFFAOYSA-M propidium iodide Chemical compound [I-].[I-].C12=CC(N)=CC=C2C2=CC=C(N)C=C2[N+](CCC[N+](C)(CC)CC)=C1C1=CC=CC=C1 XJMOSONTPMZWPB-UHFFFAOYSA-M 0.000 description 8
238000000746 purification Methods 0.000 description 8
230000002285 radioactive effect Effects 0.000 description 8
239000000243 solution Substances 0.000 description 8
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 8
CMSMOCZEIVJLDB-UHFFFAOYSA-N Cyclophosphamide Chemical compound ClCCN(CCCl)P1(=O)NCCCO1 CMSMOCZEIVJLDB-UHFFFAOYSA-N 0.000 description 7
102100024746 Dihydrofolate reductase Human genes 0.000 description 7
239000006144 Dulbecco’s modiﬁed Eagle's medium Substances 0.000 description 7
101800000155 Epiregulin Proteins 0.000 description 7
102400001329 Epiregulin Human genes 0.000 description 7
239000003098 androgen Substances 0.000 description 7
239000004037 angiogenesis inhibitor Substances 0.000 description 7
238000013459 approach Methods 0.000 description 7
108020001096 dihydrofolate reductase Proteins 0.000 description 7
231100000673 dose–response relationship Toxicity 0.000 description 7
239000000499 gel Substances 0.000 description 7
210000003292 kidney cell Anatomy 0.000 description 7
208000020816 lung neoplasm Diseases 0.000 description 7
239000000463 material Substances 0.000 description 7
239000003094 microcapsule Substances 0.000 description 7
208000002154 non-small cell lung carcinoma Diseases 0.000 description 7
239000000523 sample Substances 0.000 description 7
239000006228 supernatant Substances 0.000 description 7
208000029729 tumor suppressor gene on chromosome 11 Diseases 0.000 description 7
YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 6
102000002260 Alkaline Phosphatase Human genes 0.000 description 6
108020004774 Alkaline Phosphatase Proteins 0.000 description 6
CIWBSHSKHKDKBQ-JLAZNSOCSA-N Ascorbic acid Chemical compound OC[C@H](O)[C@H]1OC(=O)C(O)=C1O CIWBSHSKHKDKBQ-JLAZNSOCSA-N 0.000 description 6
WVDDGKGOMKODPV-UHFFFAOYSA-N Benzyl alcohol Chemical compound OCC1=CC=CC=C1 WVDDGKGOMKODPV-UHFFFAOYSA-N 0.000 description 6
108010047041 Complementarity Determining Regions Proteins 0.000 description 6
206010058467 Lung neoplasm malignant Diseases 0.000 description 6
ZDZOTLJHXYCWBA-VCVYQWHSSA-N N-debenzoyl-N-(tert-butoxycarbonyl)-10-deacetyltaxol Chemical compound O([C@H]1[C@H]2[C@@](C([C@H](O)C3=C(C)[C@@H](OC(=O)[C@H](O)[C@@H](NC(=O)OC(C)(C)C)C=4C=CC=CC=4)C[C@]1(O)C3(C)C)=O)(C)[C@@H](O)C[C@H]1OC[C@]12OC(=O)C)C(=O)C1=CC=CC=C1 ZDZOTLJHXYCWBA-VCVYQWHSSA-N 0.000 description 6
241000700159 Rattus Species 0.000 description 6
101710100963 Receptor tyrosine-protein kinase erbB-4 Proteins 0.000 description 6
108010073929 Vascular Endothelial Growth Factor A Proteins 0.000 description 6
102000005789 Vascular Endothelial Growth Factors Human genes 0.000 description 6
108010019530 Vascular Endothelial Growth Factors Proteins 0.000 description 6
241000700605 Viruses Species 0.000 description 6
230000003321 amplification Effects 0.000 description 6
239000012148 binding buffer Substances 0.000 description 6
229940098773 bovine serum albumin Drugs 0.000 description 6
239000012659 cardioprotective agent Substances 0.000 description 6
229940045200 cardioprotective agent Drugs 0.000 description 6
229960004397 cyclophosphamide Drugs 0.000 description 6
125000000151 cysteine group Chemical class N[C@@H](CS)C(=O)* 0.000 description 6
229960004679 doxorubicin Drugs 0.000 description 6
230000013595 glycosylation Effects 0.000 description 6
238000006206 glycosylation reaction Methods 0.000 description 6
238000012151 immunohistochemical method Methods 0.000 description 6
238000003780 insertion Methods 0.000 description 6
230000037431 insertion Effects 0.000 description 6
NOESYZHRGYRDHS-UHFFFAOYSA-N insulin Chemical compound N1C(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(NC(=O)CN)C(C)CC)CSSCC(C(NC(CO)C(=O)NC(CC(C)C)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CCC(N)=O)C(=O)NC(CC(C)C)C(=O)NC(CCC(O)=O)C(=O)NC(CC(N)=O)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CSSCC(NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2C=CC(O)=CC=2)NC(=O)C(CC(C)C)NC(=O)C(C)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2NC=NC=2)NC(=O)C(CO)NC(=O)CNC2=O)C(=O)NCC(=O)NC(CCC(O)=O)C(=O)NC(CCCNC(N)=N)C(=O)NCC(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC(O)=CC=3)C(=O)NC(C(C)O)C(=O)N3C(CCC3)C(=O)NC(CCCCN)C(=O)NC(C)C(O)=O)C(=O)NC(CC(N)=O)C(O)=O)=O)NC(=O)C(C(C)CC)NC(=O)C(CO)NC(=O)C(C(C)O)NC(=O)C1CSSCC2NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(N)CC=1C=CC=CC=1)C(C)C)CC1=CN=CN1 NOESYZHRGYRDHS-UHFFFAOYSA-N 0.000 description 6
150000002632 lipids Chemical class 0.000 description 6
210000004072 lung Anatomy 0.000 description 6
201000005202 lung cancer Diseases 0.000 description 6
230000036210 malignancy Effects 0.000 description 6
125000002496 methyl group Chemical group [H]C([H])([H])* 0.000 description 6
238000003199 nucleic acid amplification method Methods 0.000 description 6
239000002245 particle Substances 0.000 description 6
238000003752 polymerase chain reaction Methods 0.000 description 6
230000002829 reductive effect Effects 0.000 description 6
230000028327 secretion Effects 0.000 description 6
206010041823 squamous cell carcinoma Diseases 0.000 description 6
238000010186 staining Methods 0.000 description 6
239000000126 substance Substances 0.000 description 6
RCINICONZNJXQF-MZXODVADSA-N taxol Chemical compound O([C@@H]1[C@@]2(C[C@@H](C(C)=C(C2(C)C)[C@H](C([C@]2(C)[C@@H](O)C[C@H]3OC[C@]3([C@H]21)OC(C)=O)=O)OC(=O)C)OC(=O)[C@H](O)[C@@H](NC(=O)C=1C=CC=CC=1)C=1C=CC=CC=1)O)C(=O)C1=CC=CC=C1 RCINICONZNJXQF-MZXODVADSA-N 0.000 description 6
239000003053 toxin Substances 0.000 description 6
231100000765 toxin Toxicity 0.000 description 6
108700012359 toxins Proteins 0.000 description 6
238000012546 transfer Methods 0.000 description 6
JKMHFZQWWAIEOD-UHFFFAOYSA-N 2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid Chemical compound OCC[NH+]1CCN(CCS([O-])(=O)=O)CC1 JKMHFZQWWAIEOD-UHFFFAOYSA-N 0.000 description 5
108010033760 Amphiregulin Proteins 0.000 description 5
102100038778 Amphiregulin Human genes 0.000 description 5
101800001382 Betacellulin Proteins 0.000 description 5
102400001242 Betacellulin Human genes 0.000 description 5
241000282693 Cercopithecidae Species 0.000 description 5
241000196324 Embryophyta Species 0.000 description 5
108010087819 Fc receptors Proteins 0.000 description 5
102000009109 Fc receptors Human genes 0.000 description 5
DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 5
108010001336 Horseradish Peroxidase Proteins 0.000 description 5
108010073807 IgG Receptors Proteins 0.000 description 5
102000013462 Interleukin-12 Human genes 0.000 description 5
108010065805 Interleukin-12 Proteins 0.000 description 5
108010002350 Interleukin-2 Proteins 0.000 description 5
102000000588 Interleukin-2 Human genes 0.000 description 5
QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 5
102100029185 Low affinity immunoglobulin gamma Fc region receptor III-B Human genes 0.000 description 5
101800000675 Neuregulin-2 Proteins 0.000 description 5
108091028043 Nucleic acid sequence Proteins 0.000 description 5
206010033128 Ovarian cancer Diseases 0.000 description 5
206010061535 Ovarian neoplasm Diseases 0.000 description 5
229910019142 PO4 Inorganic materials 0.000 description 5
229930012538 Paclitaxel Natural products 0.000 description 5
239000002202 Polyethylene glycol Substances 0.000 description 5
102100022668 Pro-neuregulin-2, membrane-bound isoform Human genes 0.000 description 5
101710100969 Receptor tyrosine-protein kinase erbB-3 Proteins 0.000 description 5
208000015634 Rectal Neoplasms Diseases 0.000 description 5
208000005718 Stomach Neoplasms Diseases 0.000 description 5
239000003242 anti bacterial agent Substances 0.000 description 5
229940088710 antibiotic agent Drugs 0.000 description 5
230000000903 blocking effect Effects 0.000 description 5
239000003153 chemical reaction reagent Substances 0.000 description 5
210000001072 colon Anatomy 0.000 description 5
208000029742 colonic neoplasm Diseases 0.000 description 5
230000021615 conjugation Effects 0.000 description 5
238000004132 cross linking Methods 0.000 description 5
230000001086 cytosolic effect Effects 0.000 description 5
229960003668 docetaxel Drugs 0.000 description 5
238000002474 experimental method Methods 0.000 description 5
239000012091 fetal bovine serum Substances 0.000 description 5
238000002509 fluorescent in situ hybridization Methods 0.000 description 5
208000014829 head and neck neoplasm Diseases 0.000 description 5
230000016784 immunoglobulin production Effects 0.000 description 5
230000003834 intracellular effect Effects 0.000 description 5
208000014018 liver neoplasm Diseases 0.000 description 5
201000005249 lung adenocarcinoma Diseases 0.000 description 5
238000002703 mutagenesis Methods 0.000 description 5
231100000350 mutagenesis Toxicity 0.000 description 5
229960001592 paclitaxel Drugs 0.000 description 5
210000003819 peripheral blood mononuclear cell Anatomy 0.000 description 5
238000002823 phage display Methods 0.000 description 5
239000010452 phosphate Substances 0.000 description 5
229920001223 polyethylene glycol Polymers 0.000 description 5
206010038038 rectal cancer Diseases 0.000 description 5
201000001275 rectum cancer Diseases 0.000 description 5
150000003839 salts Chemical class 0.000 description 5
230000011664 signaling Effects 0.000 description 5
241000894007 species Species 0.000 description 5
230000003612 virological effect Effects 0.000 description 5
MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 4
108090001008 Avidin Proteins 0.000 description 4
230000004544 DNA amplification Effects 0.000 description 4
206010014733 Endometrial cancer Diseases 0.000 description 4
206010014759 Endometrial neoplasm Diseases 0.000 description 4
229940124226 Farnesyltransferase inhibitor Drugs 0.000 description 4
239000007995 HEPES buffer Substances 0.000 description 4
102000018251 Hypoxanthine Phosphoribosyltransferase Human genes 0.000 description 4
108010091358 Hypoxanthine Phosphoribosyltransferase Proteins 0.000 description 4
ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 4
AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 4
229930126263 Maytansine Natural products 0.000 description 4
108090000157 Metallothionein Proteins 0.000 description 4
NWIBSHFKIJFRCO-WUDYKRTCSA-N Mytomycin Chemical compound C1N2C(C(C(C)=C(N)C3=O)=O)=C3[C@@H](COC(N)=O)[C@@]2(OC)[C@@H]2[C@H]1N2 NWIBSHFKIJFRCO-WUDYKRTCSA-N 0.000 description 4
101800000673 Neuregulin-3 Proteins 0.000 description 4
101800002641 Neuregulin-4 Proteins 0.000 description 4
108091034117 Oligonucleotide Proteins 0.000 description 4
108090000430 Phosphatidylinositol 3-kinases Proteins 0.000 description 4
102000003993 Phosphatidylinositol 3-kinases Human genes 0.000 description 4
108091000080 Phosphotransferase Proteins 0.000 description 4
102100022659 Pro-neuregulin-3, membrane-bound isoform Human genes 0.000 description 4
102100022658 Pro-neuregulin-4, membrane-bound isoform Human genes 0.000 description 4
102000004022 Protein-Tyrosine Kinases Human genes 0.000 description 4
108090000412 Protein-Tyrosine Kinases Proteins 0.000 description 4
241000283984 Rodentia Species 0.000 description 4
230000018199 S phase Effects 0.000 description 4
FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 4
229940123237 Taxane Drugs 0.000 description 4
IQFYYKKMVGJFEH-XLPZGREQSA-N Thymidine Chemical compound O=C1NC(=O)C(C)=CN1[C@@H]1O[C@H](CO)[C@@H](O)C1 IQFYYKKMVGJFEH-XLPZGREQSA-N 0.000 description 4
QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 4
208000007097 Urinary Bladder Neoplasms Diseases 0.000 description 4
JXLYSJRDGCGARV-WWYNWVTFSA-N Vinblastine Natural products O=C(O[C@H]1[C@](O)(C(=O)OC)[C@@H]2N(C)c3c(cc(c(OC)c3)[C@]3(C(=O)OC)c4[nH]c5c(c4CCN4C[C@](O)(CC)C[C@H](C3)C4)cccc5)[C@@]32[C@H]2[C@@]1(CC)C=CCN2CC3)C JXLYSJRDGCGARV-WWYNWVTFSA-N 0.000 description 4
238000001042 affinity chromatography Methods 0.000 description 4
239000003817 anthracycline antibiotic agent Substances 0.000 description 4
230000002280 anti-androgenic effect Effects 0.000 description 4
230000003388 anti-hormonal effect Effects 0.000 description 4
239000000051 antiandrogen Substances 0.000 description 4
229940041181 antineoplastic drug Drugs 0.000 description 4
VSRXQHXAPYXROS-UHFFFAOYSA-N azanide;cyclobutane-1,1-dicarboxylic acid;platinum(2+) Chemical compound [NH2-].[NH2-].[Pt+2].OC(=O)C1(C(O)=O)CCC1 VSRXQHXAPYXROS-UHFFFAOYSA-N 0.000 description 4
239000008228 bacteriostatic water for injection Substances 0.000 description 4
230000008901 benefit Effects 0.000 description 4
210000000481 breast Anatomy 0.000 description 4
230000005907 cancer growth Effects 0.000 description 4
150000001720 carbohydrates Chemical group 0.000 description 4
229960004562 carboplatin Drugs 0.000 description 4
230000010261 cell growth Effects 0.000 description 4
238000005119 centrifugation Methods 0.000 description 4
238000004587 chromatography analysis Methods 0.000 description 4
238000007796 conventional method Methods 0.000 description 4
229920001577 copolymer Polymers 0.000 description 4
239000013078 crystal Substances 0.000 description 4
238000012217 deletion Methods 0.000 description 4
230000037430 deletion Effects 0.000 description 4
238000000326 densiometry Methods 0.000 description 4
238000012377 drug delivery Methods 0.000 description 4
230000002357 endometrial effect Effects 0.000 description 4
238000013467 fragmentation Methods 0.000 description 4
238000006062 fragmentation reaction Methods 0.000 description 4
206010017758 gastric cancer Diseases 0.000 description 4
230000002518 glial effect Effects 0.000 description 4
208000005017 glioblastoma Diseases 0.000 description 4
230000009422 growth inhibiting effect Effects 0.000 description 4
230000036541 health Effects 0.000 description 4
230000002440 hepatic effect Effects 0.000 description 4
206010073071 hepatocellular carcinoma Diseases 0.000 description 4
238000001114 immunoprecipitation Methods 0.000 description 4
238000001990 intravenous administration Methods 0.000 description 4
208000032839 leukemia Diseases 0.000 description 4
210000004698 lymphocyte Anatomy 0.000 description 4
239000006166 lysate Substances 0.000 description 4
238000013507 mapping Methods 0.000 description 4
WKPWGQKGSOKKOO-RSFHAFMBSA-N maytansine Chemical compound CO[C@@H]([C@@]1(O)C[C@](OC(=O)N1)([C@H]([C@@H]1O[C@@]1(C)[C@@H](OC(=O)[C@H](C)N(C)C(C)=O)CC(=O)N1C)C)[H])\C=C\C=C(C)\CC2=CC(OC)=C(Cl)C1=C2 WKPWGQKGSOKKOO-RSFHAFMBSA-N 0.000 description 4
239000002773 nucleotide Substances 0.000 description 4
125000003729 nucleotide group Chemical group 0.000 description 4
NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 4
102000020233 phosphotransferase Human genes 0.000 description 4
230000008488 polyadenylation Effects 0.000 description 4
238000000159 protein binding assay Methods 0.000 description 4
239000003528 protein farnesyltransferase inhibitor Substances 0.000 description 4
230000005180 public health Effects 0.000 description 4
238000003156 radioimmunoprecipitation Methods 0.000 description 4
238000010188 recombinant method Methods 0.000 description 4
238000012552 review Methods 0.000 description 4
230000019491 signal transduction Effects 0.000 description 4
238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 4
208000017572 squamous cell neoplasm Diseases 0.000 description 4
210000002784 stomach Anatomy 0.000 description 4
201000011549 stomach cancer Diseases 0.000 description 4
229960001603 tamoxifen Drugs 0.000 description 4
238000001890 transfection Methods 0.000 description 4
230000004614 tumor growth Effects 0.000 description 4
125000001493 tyrosinyl group Chemical group [H]OC1=C([H])C([H])=C(C([H])=C1[H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 4
241000701161 unidentified adenovirus Species 0.000 description 4
229960003048 vinblastine Drugs 0.000 description 4
JXLYSJRDGCGARV-XQKSVPLYSA-N vincaleukoblastine Chemical compound C([C@@H](C[C@]1(C(=O)OC)C=2C(=CC3=C([C@]45[C@H]([C@@]([C@H](OC(C)=O)[C@]6(CC)C=CCN([C@H]56)CC4)(O)C(=O)OC)N3C)C=2)OC)C[C@@](C2)(O)CC)N2CCC2=C1NC1=CC=CC=C21 JXLYSJRDGCGARV-XQKSVPLYSA-N 0.000 description 4
238000005406 washing Methods 0.000 description 4
NMWKYTGJWUAZPZ-WWHBDHEGSA-N (4S)-4-[[(4R,7S,10S,16S,19S,25S,28S,31R)-31-[[(2S)-2-[[(1R,6R,9S,12S,18S,21S,24S,27S,30S,33S,36S,39S,42R,47R,53S,56S,59S,62S,65S,68S,71S,76S,79S,85S)-47-[[(2S)-2-[[(2S)-4-amino-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-amino-3-methylbutanoyl]amino]-3-methylbutanoyl]amino]-3-hydroxypropanoyl]amino]-3-(1H-imidazol-4-yl)propanoyl]amino]-3-phenylpropanoyl]amino]-4-oxobutanoyl]amino]-3-carboxypropanoyl]amino]-18-(4-aminobutyl)-27,68-bis(3-amino-3-oxopropyl)-36,71,76-tribenzyl-39-(3-carbamimidamidopropyl)-24-(2-carboxyethyl)-21,56-bis(carboxymethyl)-65,85-bis[(1R)-1-hydroxyethyl]-59-(hydroxymethyl)-62,79-bis(1H-imidazol-4-ylmethyl)-9-methyl-33-(2-methylpropyl)-8,11,17,20,23,26,29,32,35,38,41,48,54,57,60,63,66,69,72,74,77,80,83,86-tetracosaoxo-30-propan-2-yl-3,4,44,45-tetrathia-7,10,16,19,22,25,28,31,34,37,40,49,55,58,61,64,67,70,73,75,78,81,84,87-tetracosazatetracyclo[40.31.14.012,16.049,53]heptaoctacontane-6-carbonyl]amino]-3-methylbutanoyl]amino]-7-(3-carbamimidamidopropyl)-25-(hydroxymethyl)-19-[(4-hydroxyphenyl)methyl]-28-(1H-imidazol-4-ylmethyl)-10-methyl-6,9,12,15,18,21,24,27,30-nonaoxo-16-propan-2-yl-1,2-dithia-5,8,11,14,17,20,23,26,29-nonazacyclodotriacontane-4-carbonyl]amino]-5-[[(2S)-1-[[(2S)-1-[[(2S)-3-carboxy-1-[[(2S)-1-[[(2S)-1-[[(1S)-1-carboxyethyl]amino]-4-methyl-1-oxopentan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-1-oxopropan-2-yl]amino]-1-oxopropan-2-yl]amino]-3-(1H-imidazol-4-yl)-1-oxopropan-2-yl]amino]-5-oxopentanoic acid Chemical compound CC(C)C[C@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](C)NC(=O)[C@H](Cc1c[nH]cn1)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@@H]1CSSC[C@H](NC(=O)[C@@H](NC(=O)[C@@H]2CSSC[C@@H]3NC(=O)[C@H](Cc4ccccc4)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](NC(=O)[C@H](Cc4c[nH]cn4)NC(=O)[C@H](CO)NC(=O)[C@H](CC(O)=O)NC(=O)[C@@H]4CCCN4C(=O)[C@H](CSSC[C@H](NC(=O)[C@@H](NC(=O)CNC(=O)[C@H](Cc4c[nH]cn4)NC(=O)[C@H](Cc4ccccc4)NC3=O)[C@@H](C)O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](Cc3ccccc3)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCCN)C(=O)N3CCC[C@H]3C(=O)N[C@@H](C)C(=O)N2)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](Cc2ccccc2)NC(=O)[C@H](Cc2c[nH]cn2)NC(=O)[C@H](CO)NC(=O)[C@@H](NC(=O)[C@@H](N)C(C)C)C(C)C)[C@@H](C)O)C(C)C)C(=O)N[C@@H](Cc2c[nH]cn2)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](Cc2ccc(O)cc2)C(=O)N[C@@H](C(C)C)C(=O)NCC(=O)N[C@@H](C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N1)C(=O)N[C@@H](C)C(O)=O NMWKYTGJWUAZPZ-WWHBDHEGSA-N 0.000 description 3
NFGXHKASABOEEW-UHFFFAOYSA-N 1-methylethyl 11-methoxy-3,7,11-trimethyl-2,4-dodecadienoate Chemical compound COC(C)(C)CCCC(C)CC=CC(C)=CC(=O)OC(C)C NFGXHKASABOEEW-UHFFFAOYSA-N 0.000 description 3
GANZODCWZFAEGN-UHFFFAOYSA-N 5-mercapto-2-nitro-benzoic acid Chemical compound OC(=O)C1=CC(S)=CC=C1[N+]([O-])=O GANZODCWZFAEGN-UHFFFAOYSA-N 0.000 description 3
VVIAGPKUTFNRDU-UHFFFAOYSA-N 6S-folinic acid Natural products C1NC=2NC(N)=NC(=O)C=2N(C=O)C1CNC1=CC=C(C(=O)NC(CCC(O)=O)C(O)=O)C=C1 VVIAGPKUTFNRDU-UHFFFAOYSA-N 0.000 description 3
STQGQHZAVUOBTE-UHFFFAOYSA-N 7-Cyan-hept-2t-en-4,6-diinsaeure Natural products C1=2C(O)=C3C(=O)C=4C(OC)=CC=CC=4C(=O)C3=C(O)C=2CC(O)(C(C)=O)CC1OC1CC(N)C(O)C(C)O1 STQGQHZAVUOBTE-UHFFFAOYSA-N 0.000 description 3
SPBDXSGPUHCETR-JFUDTMANSA-N 8883yp2r6d Chemical compound O1[C@@H](C)[C@H](O)[C@@H](OC)C[C@@H]1O[C@@H]1[C@@H](OC)C[C@H](O[C@@H]2C(=C/C[C@@H]3C[C@@H](C[C@@]4(O[C@@H]([C@@H](C)CC4)C(C)C)O3)OC(=O)[C@@H]3C=C(C)[C@@H](O)[C@H]4OC\C([C@@]34O)=C/C=C/[C@@H]2C)/C)O[C@H]1C.C1C[C@H](C)[C@@H]([C@@H](C)CC)O[C@@]21O[C@H](C\C=C(C)\[C@@H](O[C@@H]1O[C@@H](C)[C@H](O[C@@H]3O[C@@H](C)[C@H](O)[C@@H](OC)C3)[C@@H](OC)C1)[C@@H](C)\C=C\C=C/1[C@]3([C@H](C(=O)O4)C=C(C)[C@@H](O)[C@H]3OC\1)O)C[C@H]4C2 SPBDXSGPUHCETR-JFUDTMANSA-N 0.000 description 3
108010088751 Albumins Proteins 0.000 description 3
102000009027 Albumins Human genes 0.000 description 3
206010061424 Anal cancer Diseases 0.000 description 3
UHOVQNZJYSORNB-UHFFFAOYSA-N Benzene Chemical compound C1=CC=CC=C1 UHOVQNZJYSORNB-UHFFFAOYSA-N 0.000 description 3
206010005003 Bladder cancer Diseases 0.000 description 3
GAGWJHPBXLXJQN-UORFTKCHSA-N Capecitabine Chemical compound C1=C(F)C(NC(=O)OCCCCC)=NC(=O)N1[C@H]1[C@H](O)[C@H](O)[C@@H](C)O1 GAGWJHPBXLXJQN-UORFTKCHSA-N 0.000 description 3
108091035707 Consensus sequence Proteins 0.000 description 3
UHDGCWIWMRVCDJ-CCXZUQQUSA-N Cytarabine Chemical compound O=C1N=C(N)C=CN1[C@H]1[C@@H](O)[C@H](O)[C@@H](CO)O1 UHDGCWIWMRVCDJ-CCXZUQQUSA-N 0.000 description 3
241000701022 Cytomegalovirus Species 0.000 description 3
KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 3
102000056372 ErbB-3 Receptor Human genes 0.000 description 3
102000044591 ErbB-4 Receptor Human genes 0.000 description 3
241000233866 Fungi Species 0.000 description 3
206010017993 Gastrointestinal neoplasms Diseases 0.000 description 3
108010010803 Gelatin Proteins 0.000 description 3
WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 3
WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 3
241000238631 Hexapoda Species 0.000 description 3
102000006496 Immunoglobulin Heavy Chains Human genes 0.000 description 3
108010019476 Immunoglobulin Heavy Chains Proteins 0.000 description 3
108010067060 Immunoglobulin Variable Region Proteins 0.000 description 3
102000017727 Immunoglobulin Variable Region Human genes 0.000 description 3
102000004877 Insulin Human genes 0.000 description 3
108090001061 Insulin Proteins 0.000 description 3
208000008839 Kidney Neoplasms Diseases 0.000 description 3
241000235649 Kluyveromyces Species 0.000 description 3
QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 3
CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 3
ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 3
HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 description 3
FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 3
ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 3
108010000817 Leuprolide Proteins 0.000 description 3
102000003792 Metallothionein Human genes 0.000 description 3
OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 3
229930193140 Neomycin Natural products 0.000 description 3
102000043276 Oncogene Human genes 0.000 description 3
241000283973 Oryctolagus cuniculus Species 0.000 description 3
206010061902 Pancreatic neoplasm Diseases 0.000 description 3
102000035195 Peptidases Human genes 0.000 description 3
108091005804 Peptidases Proteins 0.000 description 3
229920001213 Polysorbate 20 Polymers 0.000 description 3
239000004365 Protease Substances 0.000 description 3
108091008611 Protein Kinase B Proteins 0.000 description 3
102100033810 RAC-alpha serine/threonine-protein kinase Human genes 0.000 description 3
108020004511 Recombinant DNA Proteins 0.000 description 3
206010038389 Renal cancer Diseases 0.000 description 3
108010039491 Ricin Proteins 0.000 description 3
239000012722 SDS sample buffer Substances 0.000 description 3
206010061934 Salivary gland cancer Diseases 0.000 description 3
229920002684 Sepharose Polymers 0.000 description 3
MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 3
241000607720 Serratia Species 0.000 description 3
206010041067 Small cell lung cancer Diseases 0.000 description 3
101710087249 Small toxin Proteins 0.000 description 3
238000002105 Southern blotting Methods 0.000 description 3
FOCVUCIESVLUNU-UHFFFAOYSA-N Thiotepa Chemical compound C1CN1P(N1CC1)(=S)N1CC1 FOCVUCIESVLUNU-UHFFFAOYSA-N 0.000 description 3
239000004473 Threonine Substances 0.000 description 3
208000024770 Thyroid neoplasm Diseases 0.000 description 3
241000251539 Vertebrata <Metazoa> Species 0.000 description 3
206010047741 Vulval cancer Diseases 0.000 description 3
238000002835 absorbance Methods 0.000 description 3
150000007513 acids Chemical class 0.000 description 3
230000003213 activating effect Effects 0.000 description 3
239000002671 adjuvant Substances 0.000 description 3
235000004279 alanine Nutrition 0.000 description 3
201000007538 anal carcinoma Diseases 0.000 description 3
230000001772 anti-angiogenic effect Effects 0.000 description 3
229940046836 anti-estrogen Drugs 0.000 description 3
230000001833 anti-estrogenic effect Effects 0.000 description 3
230000001640 apoptogenic effect Effects 0.000 description 3
238000003149 assay kit Methods 0.000 description 3
230000003305 autocrine Effects 0.000 description 3
230000001580 bacterial effect Effects 0.000 description 3
230000001588 bifunctional effect Effects 0.000 description 3
238000001574 biopsy Methods 0.000 description 3
229960002685 biotin Drugs 0.000 description 3
235000020958 biotin Nutrition 0.000 description 3
239000011616 biotin Substances 0.000 description 3
239000011575 calcium Substances 0.000 description 3
210000004978 chinese hamster ovary cell Anatomy 0.000 description 3
239000003593 chromogenic compound Substances 0.000 description 3
DQLATGHUWYMOKM-UHFFFAOYSA-L cisplatin Chemical compound N[Pt](N)(Cl)Cl DQLATGHUWYMOKM-UHFFFAOYSA-L 0.000 description 3
229960004316 cisplatin Drugs 0.000 description 3
239000002299 complementary DNA Substances 0.000 description 3
238000004590 computer program Methods 0.000 description 3
239000003431 cross linking reagent Substances 0.000 description 3
235000018417 cysteine Nutrition 0.000 description 3
STQGQHZAVUOBTE-VGBVRHCVSA-N daunorubicin Chemical compound O([C@H]1C[C@@](O)(CC=2C(O)=C3C(=O)C=4C=CC=C(C=4C(=O)C3=C(O)C=21)OC)C(C)=O)[C@H]1C[C@H](N)[C@H](O)[C@H](C)O1 STQGQHZAVUOBTE-VGBVRHCVSA-N 0.000 description 3
229960005156 digoxin Drugs 0.000 description 3
239000003085 diluting agent Substances 0.000 description 3
238000010790 dilution Methods 0.000 description 3
239000012895 dilution Substances 0.000 description 3
239000000539 dimer Substances 0.000 description 3
230000002255 enzymatic effect Effects 0.000 description 3
229960001842 estramustine Drugs 0.000 description 3
FRPJXPJMRWBBIH-RBRWEJTLSA-N estramustine Chemical compound ClCCN(CCCl)C(=O)OC1=CC=C2[C@H]3CC[C@](C)([C@H](CC4)O)[C@@H]4[C@@H]3CCC2=C1 FRPJXPJMRWBBIH-RBRWEJTLSA-N 0.000 description 3
239000000328 estrogen antagonist Substances 0.000 description 3
210000003527 eukaryotic cell Anatomy 0.000 description 3
229960002074 flutamide Drugs 0.000 description 3
MKXKFYHWDHIYRV-UHFFFAOYSA-N flutamide Chemical compound CC(C)C(=O)NC1=CC=C([N+]([O-])=O)C(C(F)(F)F)=C1 MKXKFYHWDHIYRV-UHFFFAOYSA-N 0.000 description 3
235000008191 folinic acid Nutrition 0.000 description 3
239000011672 folinic acid Substances 0.000 description 3
VVIAGPKUTFNRDU-ABLWVSNPSA-N folinic acid Chemical compound C1NC=2NC(N)=NC(=O)C=2N(C=O)C1CNC1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 VVIAGPKUTFNRDU-ABLWVSNPSA-N 0.000 description 3
238000009472 formulation Methods 0.000 description 3
239000012737 fresh medium Substances 0.000 description 3
108020001507 fusion proteins Proteins 0.000 description 3
102000037865 fusion proteins Human genes 0.000 description 3
238000001502 gel electrophoresis Methods 0.000 description 3
239000008273 gelatin Substances 0.000 description 3
229920000159 gelatin Polymers 0.000 description 3
235000019322 gelatine Nutrition 0.000 description 3
235000011852 gelatine desserts Nutrition 0.000 description 3
238000001415 gene therapy Methods 0.000 description 3
210000004602 germ cell Anatomy 0.000 description 3
239000008103 glucose Substances 0.000 description 3
239000011544 gradient gel Substances 0.000 description 3
201000010536 head and neck cancer Diseases 0.000 description 3
230000001900 immune effect Effects 0.000 description 3
239000012642 immune effector Substances 0.000 description 3
229940072221 immunoglobulins Drugs 0.000 description 3
229940121354 immunomodulator Drugs 0.000 description 3
230000001976 improved effect Effects 0.000 description 3
239000003112 inhibitor Substances 0.000 description 3
239000007924 injection Substances 0.000 description 3
238000002347 injection Methods 0.000 description 3
229940125396 insulin Drugs 0.000 description 3
230000003993 interaction Effects 0.000 description 3
238000007912 intraperitoneal administration Methods 0.000 description 3
UWKQSNNFCGGAFS-XIFFEERXSA-N irinotecan Chemical compound C1=C2C(CC)=C3CN(C(C4=C([C@@](C(=O)OC4)(O)CC)C=4)=O)C=4C3=NC2=CC=C1OC(=O)N(CC1)CCC1N1CCCCC1 UWKQSNNFCGGAFS-XIFFEERXSA-N 0.000 description 3
238000002955 isolation Methods 0.000 description 3
210000003734 kidney Anatomy 0.000 description 3
201000010982 kidney cancer Diseases 0.000 description 3
229960001691 leucovorin Drugs 0.000 description 3
210000000265 leukocyte Anatomy 0.000 description 3
GFIJNRVAKGFPGQ-LIJARHBVSA-N leuprolide Chemical compound CCNC(=O)[C@@H]1CCCN1C(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@H](CO)NC(=O)[C@H](CC=1C2=CC=CC=C2NC=1)NC(=O)[C@H](CC=1N=CNC=1)NC(=O)[C@H]1NC(=O)CC1)CC1=CC=C(O)C=C1 GFIJNRVAKGFPGQ-LIJARHBVSA-N 0.000 description 3
229960004338 leuprorelin Drugs 0.000 description 3
230000000670 limiting effect Effects 0.000 description 3
201000007270 liver cancer Diseases 0.000 description 3
239000012139 lysis buffer Substances 0.000 description 3
210000002540 macrophage Anatomy 0.000 description 3
238000012423 maintenance Methods 0.000 description 3
208000015486 malignant pancreatic neoplasm Diseases 0.000 description 3
230000007246 mechanism Effects 0.000 description 3
GLVAUDGFNGKCSF-UHFFFAOYSA-N mercaptopurine Chemical compound S=C1NC=NC2=C1NC=N2 GLVAUDGFNGKCSF-UHFFFAOYSA-N 0.000 description 3
MYWUZJCMWCOHBA-VIFPVBQESA-N methamphetamine Chemical compound CN[C@@H](C)CC1=CC=CC=C1 MYWUZJCMWCOHBA-VIFPVBQESA-N 0.000 description 3
229960004452 methionine Drugs 0.000 description 3
239000004005 microsphere Substances 0.000 description 3
KKZJGLLVHKMTCM-UHFFFAOYSA-N mitoxantrone Chemical compound O=C1C2=C(O)C=CC(O)=C2C(=O)C2=C1C(NCCNCCO)=CC=C2NCCNCCO KKZJGLLVHKMTCM-UHFFFAOYSA-N 0.000 description 3
229960001156 mitoxantrone Drugs 0.000 description 3
229940086322 navelbine Drugs 0.000 description 3
229960004927 neomycin Drugs 0.000 description 3
238000011275 oncology therapy Methods 0.000 description 3
210000000056 organ Anatomy 0.000 description 3
210000000496 pancreas Anatomy 0.000 description 3
201000002528 pancreatic cancer Diseases 0.000 description 3
208000008443 pancreatic carcinoma Diseases 0.000 description 3
201000002628 peritoneum cancer Diseases 0.000 description 3
102000013415 peroxidase activity proteins Human genes 0.000 description 3
108040007629 peroxidase activity proteins Proteins 0.000 description 3
239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 3
235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 3
229960004618 prednisone Drugs 0.000 description 3
XOFYZVNMUHMLCC-ZPOLXVRWSA-N prednisone Chemical compound O=C1C=C[C@]2(C)[C@H]3C(=O)C[C@](C)([C@@](CC4)(O)C(=O)CO)[C@@H]4[C@@H]3CCC2=C1 XOFYZVNMUHMLCC-ZPOLXVRWSA-N 0.000 description 3
239000003755 preservative agent Substances 0.000 description 3
230000009467 reduction Effects 0.000 description 3
230000002441 reversible effect Effects 0.000 description 3
210000003079 salivary gland Anatomy 0.000 description 3
201000003804 salivary gland carcinoma Diseases 0.000 description 3
208000000587 small cell lung carcinoma Diseases 0.000 description 3
150000003384 small molecules Chemical class 0.000 description 3
230000004936 stimulating effect Effects 0.000 description 3
238000007920 subcutaneous administration Methods 0.000 description 3
230000002195 synergetic effect Effects 0.000 description 3
DKPFODGZWDEEBT-QFIAKTPHSA-N taxane Chemical class C([C@]1(C)CCC[C@@H](C)[C@H]1C1)C[C@H]2[C@H](C)CC[C@@H]1C2(C)C DKPFODGZWDEEBT-QFIAKTPHSA-N 0.000 description 3
229940124597 therapeutic agent Drugs 0.000 description 3
201000002510 thyroid cancer Diseases 0.000 description 3
210000001685 thyroid gland Anatomy 0.000 description 3
238000013519 translation Methods 0.000 description 3
201000005112 urinary bladder cancer Diseases 0.000 description 3
206010046766 uterine cancer Diseases 0.000 description 3
CILBMBUYJCWATM-PYGJLNRPSA-N vinorelbine ditartrate Chemical compound OC(=O)[C@H](O)[C@@H](O)C(O)=O.OC(=O)[C@H](O)[C@@H](O)C(O)=O.C1N(CC=2C3=CC=CC=C3NC=22)CC(CC)=C[C@H]1C[C@]2(C(=O)OC)C1=CC([C@]23[C@H]([C@@]([C@H](OC(C)=O)[C@]4(CC)C=CCN([C@H]34)CC2)(O)C(=O)OC)N2C)=C2C=C1OC CILBMBUYJCWATM-PYGJLNRPSA-N 0.000 description 3
201000005102 vulva cancer Diseases 0.000 description 3
BMKDZUISNHGIBY-ZETCQYMHSA-N (+)-dexrazoxane Chemical compound C([C@H](C)N1CC(=O)NC(=O)C1)N1CC(=O)NC(=O)C1 BMKDZUISNHGIBY-ZETCQYMHSA-N 0.000 description 2
IEXUMDBQLIVNHZ-YOUGDJEHSA-N (8s,11r,13r,14s,17s)-11-[4-(dimethylamino)phenyl]-17-hydroxy-17-(3-hydroxypropyl)-13-methyl-1,2,6,7,8,11,12,14,15,16-decahydrocyclopenta[a]phenanthren-3-one Chemical compound C1=CC(N(C)C)=CC=C1[C@@H]1C2=C3CCC(=O)C=C3CC[C@H]2[C@H](CC[C@]2(O)CCCO)[C@@]2(C)C1 IEXUMDBQLIVNHZ-YOUGDJEHSA-N 0.000 description 2
FDKXTQMXEQVLRF-ZHACJKMWSA-N (E)-dacarbazine Chemical compound CN(C)\N=N\c1[nH]cnc1C(N)=O FDKXTQMXEQVLRF-ZHACJKMWSA-N 0.000 description 2
GVJHHUAWPYXKBD-UHFFFAOYSA-N (±)-α-Tocopherol Chemical compound OC1=C(C)C(C)=C2OC(CCCC(C)CCCC(C)CCCC(C)C)(C)CCC2=C1C GVJHHUAWPYXKBD-UHFFFAOYSA-N 0.000 description 2
TZCPCKNHXULUIY-RGULYWFUSA-N 1,2-distearoyl-sn-glycero-3-phosphoserine Chemical compound CCCCCCCCCCCCCCCCCC(=O)OC[C@H](COP(O)(=O)OC[C@H](N)C(O)=O)OC(=O)CCCCCCCCCCCCCCCCC TZCPCKNHXULUIY-RGULYWFUSA-N 0.000 description 2
GZCWLCBFPRFLKL-UHFFFAOYSA-N 1-prop-2-ynoxypropan-2-ol Chemical group CC(O)COCC#C GZCWLCBFPRFLKL-UHFFFAOYSA-N 0.000 description 2
QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 2
LSBDFXRDZJMBSC-UHFFFAOYSA-N 2-phenylacetamide Chemical class NC(=O)CC1=CC=CC=C1 LSBDFXRDZJMBSC-UHFFFAOYSA-N 0.000 description 2
UAIUNKRWKOVEES-UHFFFAOYSA-N 3,3',5,5'-tetramethylbenzidine Chemical compound CC1=C(N)C(C)=CC(C=2C=C(C)C(N)=C(C)C=2)=C1 UAIUNKRWKOVEES-UHFFFAOYSA-N 0.000 description 2
VPFUWHKTPYPNGT-UHFFFAOYSA-N 3-(3,4-dihydroxyphenyl)-1-(5-hydroxy-2,2-dimethylchromen-6-yl)propan-1-one Chemical compound OC1=C2C=CC(C)(C)OC2=CC=C1C(=O)CCC1=CC=C(O)C(O)=C1 VPFUWHKTPYPNGT-UHFFFAOYSA-N 0.000 description 2
OSJPPGNTCRNQQC-UWTATZPHSA-N 3-phospho-D-glyceric acid Chemical compound OC(=O)[C@H](O)COP(O)(O)=O OSJPPGNTCRNQQC-UWTATZPHSA-N 0.000 description 2
AOJJSUZBOXZQNB-VTZDEGQISA-N 4'-epidoxorubicin Chemical compound O([C@H]1C[C@@](O)(CC=2C(O)=C3C(=O)C=4C=CC=C(C=4C(=O)C3=C(O)C=21)OC)C(=O)CO)[C@H]1C[C@H](N)[C@@H](O)[C@H](C)O1 AOJJSUZBOXZQNB-VTZDEGQISA-N 0.000 description 2
TVZGACDUOSZQKY-LBPRGKRZSA-N 4-aminofolic acid Chemical compound C1=NC2=NC(N)=NC(N)=C2N=C1CNC1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 TVZGACDUOSZQKY-LBPRGKRZSA-N 0.000 description 2
102000013563 Acid Phosphatase Human genes 0.000 description 2
108010051457 Acid Phosphatase Proteins 0.000 description 2
208000010507 Adenocarcinoma of Lung Diseases 0.000 description 2
229920000936 Agarose Polymers 0.000 description 2
101710154825 Aminoglycoside 3'-phosphotransferase Proteins 0.000 description 2
206010003445 Ascites Diseases 0.000 description 2
BSYNRYMUTXBXSQ-UHFFFAOYSA-N Aspirin Chemical compound CC(=O)OC1=CC=CC=C1C(O)=O BSYNRYMUTXBXSQ-UHFFFAOYSA-N 0.000 description 2
IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 2
241000194108 Bacillus licheniformis Species 0.000 description 2
DWRXFEITVBNRMK-UHFFFAOYSA-N Beta-D-1-Arabinofuranosylthymine Natural products O=C1NC(=O)C(C)=CN1C1C(O)C(O)C(CO)O1 DWRXFEITVBNRMK-UHFFFAOYSA-N 0.000 description 2
108010006654 Bleomycin Proteins 0.000 description 2
241000701822 Bovine papillomavirus Species 0.000 description 2
206010008342 Cervix carcinoma Diseases 0.000 description 2
108020004705 Codon Proteins 0.000 description 2
206010052358 Colorectal cancer metastatic Diseases 0.000 description 2
SRBFZHDQGSBBOR-IOVATXLUSA-N D-xylopyranose Chemical compound O[C@@H]1COC(O)[C@H](O)[C@H]1O SRBFZHDQGSBBOR-IOVATXLUSA-N 0.000 description 2
108010092160 Dactinomycin Proteins 0.000 description 2
102000007260 Deoxyribonuclease I Human genes 0.000 description 2
108010008532 Deoxyribonuclease I Proteins 0.000 description 2
LTMHDMANZUZIPE-AMTYYWEZSA-N Digoxin Natural products O([C@H]1[C@H](C)O[C@H](O[C@@H]2C[C@@H]3[C@@](C)([C@@H]4[C@H]([C@]5(O)[C@](C)([C@H](O)C4)[C@H](C4=CC(=O)OC4)CC5)CC3)CC2)C[C@@H]1O)[C@H]1O[C@H](C)[C@@H](O[C@H]2O[C@@H](C)[C@H](O)[C@@H](O)C2)[C@@H](O)C1 LTMHDMANZUZIPE-AMTYYWEZSA-N 0.000 description 2
BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 2
108090000204 Dipeptidase 1 Proteins 0.000 description 2
241000255925 Diptera Species 0.000 description 2
101150029707 ERBB2 gene Proteins 0.000 description 2
HTIJFSOGRVMCQR-UHFFFAOYSA-N Epirubicin Natural products COc1cccc2C(=O)c3c(O)c4CC(O)(CC(OC5CC(N)C(=O)C(C)O5)c4c(O)c3C(=O)c12)C(=O)CO HTIJFSOGRVMCQR-UHFFFAOYSA-N 0.000 description 2
102000003951 Erythropoietin Human genes 0.000 description 2
108090000394 Erythropoietin Proteins 0.000 description 2
241000206602 Eukaryota Species 0.000 description 2
108010021468 Fc gamma receptor IIA Proteins 0.000 description 2
108010021472 Fc gamma receptor IIB Proteins 0.000 description 2
102000012673 Follicle Stimulating Hormone Human genes 0.000 description 2
108010079345 Follicle Stimulating Hormone Proteins 0.000 description 2
WSFSSNUMVMOOMR-UHFFFAOYSA-N Formaldehyde Chemical compound O=C WSFSSNUMVMOOMR-UHFFFAOYSA-N 0.000 description 2
102100031132 Glucose-6-phosphate isomerase Human genes 0.000 description 2
108010070600 Glucose-6-phosphate isomerase Proteins 0.000 description 2
SXRSQZLOMIGNAQ-UHFFFAOYSA-N Glutaraldehyde Chemical compound O=CCCCC=O SXRSQZLOMIGNAQ-UHFFFAOYSA-N 0.000 description 2
ZWZWYGMENQVNFU-UHFFFAOYSA-N Glycerophosphorylserin Natural products OC(=O)C(N)COP(O)(=O)OCC(O)CO ZWZWYGMENQVNFU-UHFFFAOYSA-N 0.000 description 2
239000004471 Glycine Substances 0.000 description 2
244000068988 Glycine max Species 0.000 description 2
235000010469 Glycine max Nutrition 0.000 description 2
102000003886 Glycoproteins Human genes 0.000 description 2
108090000288 Glycoproteins Proteins 0.000 description 2
102000009465 Growth Factor Receptors Human genes 0.000 description 2
108010009202 Growth Factor Receptors Proteins 0.000 description 2
101800001649 Heparin-binding EGF-like growth factor Proteins 0.000 description 2
208000009889 Herpes Simplex Diseases 0.000 description 2
108010000521 Human Growth Hormone Proteins 0.000 description 2
102000002265 Human Growth Hormone Human genes 0.000 description 2
239000000854 Human Growth Hormone Substances 0.000 description 2
101150017040 I gene Proteins 0.000 description 2
102000013463 Immunoglobulin Light Chains Human genes 0.000 description 2
108010065825 Immunoglobulin Light Chains Proteins 0.000 description 2
244000285963 Kluyveromyces fragilis Species 0.000 description 2
241001138401 Kluyveromyces lactis Species 0.000 description 2
PWKSKIMOESPYIA-BYPYZUCNSA-N L-N-acetyl-Cysteine Chemical compound CC(=O)N[C@@H](CS)C(O)=O PWKSKIMOESPYIA-BYPYZUCNSA-N 0.000 description 2
DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 2
AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 2
KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 description 2
102100029204 Low affinity immunoglobulin gamma Fc region receptor II-a Human genes 0.000 description 2
102100029205 Low affinity immunoglobulin gamma Fc region receptor II-b Human genes 0.000 description 2
102000009151 Luteinizing Hormone Human genes 0.000 description 2
108010073521 Luteinizing Hormone Proteins 0.000 description 2
206010025323 Lymphomas Diseases 0.000 description 2
KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 2
230000027311 M phase Effects 0.000 description 2
239000004907 Macro-emulsion Substances 0.000 description 2
102000018697 Membrane Proteins Human genes 0.000 description 2
108010052285 Membrane Proteins Proteins 0.000 description 2
230000004989 O-glycosylation Effects 0.000 description 2
108020005187 Oligonucleotide Probes Proteins 0.000 description 2
102000004316 Oxidoreductases Human genes 0.000 description 2
108090000854 Oxidoreductases Proteins 0.000 description 2
ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Natural products OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 2
241000276498 Pollachius virens Species 0.000 description 2
102000052575 Proto-Oncogene Human genes 0.000 description 2
108700020978 Proto-Oncogene Proteins 0.000 description 2
239000012980 RPMI-1640 medium Substances 0.000 description 2
102100029986 Receptor tyrosine-protein kinase erbB-3 Human genes 0.000 description 2
102100029981 Receptor tyrosine-protein kinase erbB-4 Human genes 0.000 description 2
108010083644 Ribonucleases Proteins 0.000 description 2
102000006382 Ribonucleases Human genes 0.000 description 2
241000607142 Salmonella Species 0.000 description 2
206010039491 Sarcoma Diseases 0.000 description 2
VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 2
QAOWNCQODCNURD-UHFFFAOYSA-L Sulfate Chemical compound [O-]S([O-])(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-L 0.000 description 2
AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 2
102000036693 Thrombopoietin Human genes 0.000 description 2
108010041111 Thrombopoietin Proteins 0.000 description 2
102000006601 Thymidine Kinase Human genes 0.000 description 2
108020004440 Thymidine kinase Proteins 0.000 description 2
102000011923 Thyrotropin Human genes 0.000 description 2
108010061174 Thyrotropin Proteins 0.000 description 2
102000009618 Transforming Growth Factors Human genes 0.000 description 2
108010009583 Transforming Growth Factors Proteins 0.000 description 2
108060008682 Tumor Necrosis Factor Proteins 0.000 description 2
102000000852 Tumor Necrosis Factor-alpha Human genes 0.000 description 2
208000006105 Uterine Cervical Neoplasms Diseases 0.000 description 2
208000002495 Uterine Neoplasms Diseases 0.000 description 2
KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 2
208000004354 Vulvar Neoplasms Diseases 0.000 description 2
230000005856 abnormality Effects 0.000 description 2
229960004308 acetylcysteine Drugs 0.000 description 2
RJURFGZVJUQBHK-UHFFFAOYSA-N actinomycin D Natural products CC1OC(=O)C(C(C)C)N(C)C(=O)CN(C)C(=O)C2CCCN2C(=O)C(C(C)C)NC(=O)C1NC(=O)C1=C(N)C(=O)C(C)=C2OC(C(C)=CC=C3C(=O)NC4C(=O)NC(C(N5CCCC5C(=O)N(C)CC(=O)N(C)C(C(C)C)C(=O)OC4C)=O)C(C)C)=C3N=C21 RJURFGZVJUQBHK-UHFFFAOYSA-N 0.000 description 2
230000009471 action Effects 0.000 description 2
239000013543 active substance Substances 0.000 description 2
OIRDTQYFTABQOQ-KQYNXXCUSA-N adenosine Chemical compound C1=NC=2C(N)=NC=NC=2N1[C@@H]1O[C@H](CO)[C@@H](O)[C@H]1O OIRDTQYFTABQOQ-KQYNXXCUSA-N 0.000 description 2
230000009824 affinity maturation Effects 0.000 description 2
238000012867 alanine scanning Methods 0.000 description 2
229960003896 aminopterin Drugs 0.000 description 2
230000002491 angiogenic effect Effects 0.000 description 2
230000000259 anti-tumor effect Effects 0.000 description 2
230000000890 antigenic effect Effects 0.000 description 2
239000013059 antihormonal agent Substances 0.000 description 2
239000003963 antioxidant agent Substances 0.000 description 2
235000006708 antioxidants Nutrition 0.000 description 2
235000010323 ascorbic acid Nutrition 0.000 description 2
229960005070 ascorbic acid Drugs 0.000 description 2
239000011668 ascorbic acid Substances 0.000 description 2
210000001130 astrocyte Anatomy 0.000 description 2
210000003719 b-lymphocyte Anatomy 0.000 description 2
244000052616 bacterial pathogen Species 0.000 description 2
230000009286 beneficial effect Effects 0.000 description 2
235000019445 benzyl alcohol Nutrition 0.000 description 2
102000005936 beta-Galactosidase Human genes 0.000 description 2
108010005774 beta-Galactosidase Proteins 0.000 description 2
IQFYYKKMVGJFEH-UHFFFAOYSA-N beta-L-thymidine Natural products O=C1NC(=O)C(C)=CN1C1OC(CO)C(O)C1 IQFYYKKMVGJFEH-UHFFFAOYSA-N 0.000 description 2
102000006635 beta-lactamase Human genes 0.000 description 2
OYVAGSVQBOHSSS-UAPAGMARSA-O bleomycin A2 Chemical compound N([C@H](C(=O)N[C@H](C)[C@@H](O)[C@H](C)C(=O)N[C@@H]([C@H](O)C)C(=O)NCCC=1SC=C(N=1)C=1SC=C(N=1)C(=O)NCCC[S+](C)C)[C@@H](O[C@H]1[C@H]([C@@H](O)[C@H](O)[C@H](CO)O1)O[C@@H]1[C@H]([C@@H](OC(N)=O)[C@H](O)[C@@H](CO)O1)O)C=1N=CNC=1)C(=O)C1=NC([C@H](CC(N)=O)NC[C@H](N)C(N)=O)=NC(N)=C1C OYVAGSVQBOHSSS-UAPAGMARSA-O 0.000 description 2
210000004369 blood Anatomy 0.000 description 2
239000008280 blood Substances 0.000 description 2
108010006025 bovine growth hormone Proteins 0.000 description 2
210000004899 c-terminal region Anatomy 0.000 description 2
229930195731 calicheamicin Natural products 0.000 description 2
HXCHCVDVKSCDHU-LULTVBGHSA-N calicheamicin Chemical compound C1[C@H](OC)[C@@H](NCC)CO[C@H]1O[C@H]1[C@H](O[C@@H]2C\3=C(NC(=O)OC)C(=O)C[C@](C/3=C/CSSSC)(O)C#C\C=C/C#C2)O[C@H](C)[C@@H](NO[C@@H]2O[C@H](C)[C@@H](SC(=O)C=3C(=C(OC)C(O[C@H]4[C@@H]([C@H](OC)[C@@H](O)[C@H](C)O4)O)=C(I)C=3C)OC)[C@@H](O)C2)[C@@H]1O HXCHCVDVKSCDHU-LULTVBGHSA-N 0.000 description 2
125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 2
YCIMNLLNPGFGHC-UHFFFAOYSA-N catechol Chemical compound OC1=CC=CC=C1O YCIMNLLNPGFGHC-UHFFFAOYSA-N 0.000 description 2
230000001413 cellular effect Effects 0.000 description 2
201000010881 cervical cancer Diseases 0.000 description 2
239000002738 chelating agent Substances 0.000 description 2
229960004630 chlorambucil Drugs 0.000 description 2
JCKYGMPEJWAADB-UHFFFAOYSA-N chlorambucil Chemical compound OC(=O)CCCC1=CC=C(N(CCCl)CCCl)C=C1 JCKYGMPEJWAADB-UHFFFAOYSA-N 0.000 description 2
HVYWMOMLDIMFJA-DPAQBDIFSA-N cholesterol Chemical compound C1C=C2C[C@@H](O)CC[C@]2(C)[C@@H]2[C@@H]1[C@@H]1CC[C@H]([C@H](C)CCCC(C)C)[C@@]1(C)CC2 HVYWMOMLDIMFJA-DPAQBDIFSA-N 0.000 description 2
238000011260 co-administration Methods 0.000 description 2
238000012875 competitive assay Methods 0.000 description 2
230000024203 complement activation Effects 0.000 description 2
238000010668 complexation reaction Methods 0.000 description 2
230000001268 conjugating effect Effects 0.000 description 2
238000010276 construction Methods 0.000 description 2
239000000356 contaminant Substances 0.000 description 2
238000003235 crystal violet staining Methods 0.000 description 2
238000012258 culturing Methods 0.000 description 2
230000009089 cytolysis Effects 0.000 description 2
230000006378 damage Effects 0.000 description 2
229960000975 daunorubicin Drugs 0.000 description 2
230000002950 deficient Effects 0.000 description 2
230000003111 delayed effect Effects 0.000 description 2
238000000502 dialysis Methods 0.000 description 2
230000004069 differentiation Effects 0.000 description 2
230000029087 digestion Effects 0.000 description 2
LTMHDMANZUZIPE-PUGKRICDSA-N digoxin Chemical compound C1[C@H](O)[C@H](O)[C@@H](C)O[C@H]1O[C@@H]1[C@@H](C)O[C@@H](O[C@@H]2[C@H](O[C@@H](O[C@@H]3C[C@@H]4[C@]([C@@H]5[C@H]([C@]6(CC[C@@H]([C@@]6(C)[C@H](O)C5)C=5COC(=O)C=5)O)CC4)(C)CC3)C[C@@H]2O)C)C[C@@H]1O LTMHDMANZUZIPE-PUGKRICDSA-N 0.000 description 2
LTMHDMANZUZIPE-UHFFFAOYSA-N digoxine Natural products C1C(O)C(O)C(C)OC1OC1C(C)OC(OC2C(OC(OC3CC4C(C5C(C6(CCC(C6(C)C(O)C5)C=5COC(=O)C=5)O)CC4)(C)CC3)CC2O)C)CC1O LTMHDMANZUZIPE-UHFFFAOYSA-N 0.000 description 2
150000004662 dithiols Chemical class 0.000 description 2
239000002552 dosage form Substances 0.000 description 2
230000004064 dysfunction Effects 0.000 description 2
VLCYCQAOQCDTCN-UHFFFAOYSA-N eflornithine Chemical compound NCCCC(N)(C(F)F)C(O)=O VLCYCQAOQCDTCN-UHFFFAOYSA-N 0.000 description 2
238000001962 electrophoresis Methods 0.000 description 2
229960001904 epirubicin Drugs 0.000 description 2
229940105423 erythropoietin Drugs 0.000 description 2
150000002148 esters Chemical class 0.000 description 2
229940011871 estrogen Drugs 0.000 description 2
239000000262 estrogen Substances 0.000 description 2
238000011156 evaluation Methods 0.000 description 2
239000013613 expression plasmid Substances 0.000 description 2
238000001914 filtration Methods 0.000 description 2
XRECTZIEBJDKEO-UHFFFAOYSA-N flucytosine Chemical compound NC1=NC(=O)NC=C1F XRECTZIEBJDKEO-UHFFFAOYSA-N 0.000 description 2
229960004413 flucytosine Drugs 0.000 description 2
238000001943 fluorescence-activated cell sorting Methods 0.000 description 2
229910052731 fluorine Inorganic materials 0.000 description 2
OVBPIULPVIDEAO-LBPRGKRZSA-N folic acid Chemical compound C=1N=C2NC(N)=NC(=O)C2=NC=1CNC1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 OVBPIULPVIDEAO-LBPRGKRZSA-N 0.000 description 2
229940028334 follicle stimulating hormone Drugs 0.000 description 2
230000002538 fungal effect Effects 0.000 description 2
229930182830 galactose Natural products 0.000 description 2
108010089491 gamma-heregulin Proteins 0.000 description 2
230000002496 gastric effect Effects 0.000 description 2
229960005277 gemcitabine Drugs 0.000 description 2
SDUQYLNIPVEERB-QPPQHZFASA-N gemcitabine Chemical compound O=C1N=C(N)C=CN1[C@H]1C(F)(F)[C@H](O)[C@@H](CO)O1 SDUQYLNIPVEERB-QPPQHZFASA-N 0.000 description 2
230000000762 glandular Effects 0.000 description 2
229960002989 glutamic acid Drugs 0.000 description 2
ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 2
108020004445 glyceraldehyde-3-phosphate dehydrogenase Proteins 0.000 description 2
102000006602 glyceraldehyde-3-phosphate dehydrogenase Human genes 0.000 description 2
239000000833 heterodimer Substances 0.000 description 2
229960002885 histidine Drugs 0.000 description 2
102000051957 human ERBB2 Human genes 0.000 description 2
JYGXADMDTFJGBT-VWUMJDOOSA-N hydrocortisone Chemical compound O=C1CC[C@]2(C)[C@H]3[C@@H](O)C[C@](C)([C@@](CC4)(O)C(=O)CO)[C@@H]4[C@@H]3CCC2=C1 JYGXADMDTFJGBT-VWUMJDOOSA-N 0.000 description 2
150000002431 hydrogen Chemical class 0.000 description 2
229910052739 hydrogen Inorganic materials 0.000 description 2
239000001257 hydrogen Substances 0.000 description 2
238000012872 hydroxylapatite chromatography Methods 0.000 description 2
229920003063 hydroxymethyl cellulose Polymers 0.000 description 2
229940031574 hydroxymethyl cellulose Drugs 0.000 description 2
FDGQSTZJBFJUBT-UHFFFAOYSA-N hypoxanthine Chemical compound O=C1NC=NC2=C1NC=N2 FDGQSTZJBFJUBT-UHFFFAOYSA-N 0.000 description 2
238000003384 imaging method Methods 0.000 description 2
208000026278 immune system disease Diseases 0.000 description 2
238000002649 immunization Methods 0.000 description 2
230000003053 immunization Effects 0.000 description 2
238000003119 immunoblot Methods 0.000 description 2
230000002163 immunogen Effects 0.000 description 2
230000006698 induction Effects 0.000 description 2
208000015181 infectious disease Diseases 0.000 description 2
230000002757 inflammatory effect Effects 0.000 description 2
108091008042 inhibitory receptors Proteins 0.000 description 2
ZPNFWUPYTFPOJU-LPYSRVMUSA-N iniprol Chemical compound C([C@H]1C(=O)NCC(=O)NCC(=O)N[C@H]2CSSC[C@H]3C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@H](C(N[C@H](C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC=4C=CC=CC=4)C(=O)N[C@@H](CC=4C=CC(O)=CC=4)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC=4C=CC=CC=4)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCCN)NC(=O)[C@H](C)NC(=O)[C@H](CCCNC(N)=N)NC2=O)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](CC=2C=CC=CC=2)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H]2N(CCC2)C(=O)[C@@H](N)CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N2[C@@H](CCC2)C(=O)N2[C@@H](CCC2)C(=O)N[C@@H](CC=2C=CC(O)=CC=2)C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(=O)N2[C@@H](CCC2)C(=O)N3)C(=O)NCC(=O)NCC(=O)N[C@@H](C)C(O)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@H](C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@H](C(=O)N1)C(C)C)[C@@H](C)O)[C@@H](C)CC)=O)[C@@H](C)CC)C1=CC=C(O)C=C1 ZPNFWUPYTFPOJU-LPYSRVMUSA-N 0.000 description 2
239000007928 intraperitoneal injection Substances 0.000 description 2
108020001756 ligand binding domains Proteins 0.000 description 2
210000005229 liver cell Anatomy 0.000 description 2
229940040129 luteinizing hormone Drugs 0.000 description 2
RLSSMJSEOOYNOY-UHFFFAOYSA-N m-cresol Chemical compound CC1=CC=CC(O)=C1 RLSSMJSEOOYNOY-UHFFFAOYSA-N 0.000 description 2
239000011159 matrix material Substances 0.000 description 2
238000005259 measurement Methods 0.000 description 2
HAWPXGHAZFHHAD-UHFFFAOYSA-N mechlorethamine Chemical compound ClCCN(C)CCCl HAWPXGHAZFHHAD-UHFFFAOYSA-N 0.000 description 2
229960004961 mechlorethamine Drugs 0.000 description 2
229960001428 mercaptopurine Drugs 0.000 description 2
108020004999 messenger RNA Proteins 0.000 description 2
230000004060 metabolic process Effects 0.000 description 2
229930182817 methionine Natural products 0.000 description 2
125000001360 methionine group Chemical group N[C@@H](CCSC)C(=O)* 0.000 description 2
HPNSFSBZBAHARI-UHFFFAOYSA-N micophenolic acid Natural products OC1=C(CC=C(C)CCC(O)=O)C(OC)=C(C)C2=C1C(=O)OC2 HPNSFSBZBAHARI-UHFFFAOYSA-N 0.000 description 2
239000004530 micro-emulsion Substances 0.000 description 2
229960004857 mitomycin Drugs 0.000 description 2
210000001616 monocyte Anatomy 0.000 description 2
229940126619 mouse monoclonal antibody Drugs 0.000 description 2
229960000951 mycophenolic acid Drugs 0.000 description 2
HPNSFSBZBAHARI-RUDMXATFSA-N mycophenolic acid Chemical compound OC1=C(C\C=C(/C)CCC(O)=O)C(OC)=C(C)C2=C1C(=O)OC2 HPNSFSBZBAHARI-RUDMXATFSA-N 0.000 description 2
239000002088 nanocapsule Substances 0.000 description 2
239000002105 nanoparticle Substances 0.000 description 2
210000000822 natural killer cell Anatomy 0.000 description 2
230000007935 neutral effect Effects 0.000 description 2
210000000440 neutrophil Anatomy 0.000 description 2
231100000252 nontoxic Toxicity 0.000 description 2
230000003000 nontoxic effect Effects 0.000 description 2
235000015097 nutrients Nutrition 0.000 description 2
239000002751 oligonucleotide probe Substances 0.000 description 2
229950011093 onapristone Drugs 0.000 description 2
230000002611 ovarian Effects 0.000 description 2
208000030940 penile carcinoma Diseases 0.000 description 2
201000008174 penis carcinoma Diseases 0.000 description 2
AQIXEPGDORPWBJ-UHFFFAOYSA-N pentan-3-ol Chemical compound CCC(O)CC AQIXEPGDORPWBJ-UHFFFAOYSA-N 0.000 description 2
238000010647 peptide synthesis reaction Methods 0.000 description 2
210000001322 periplasm Anatomy 0.000 description 2
239000000825 pharmaceutical preparation Substances 0.000 description 2
238000003566 phosphorylation assay Methods 0.000 description 2
BASFCYQUMIYNBI-UHFFFAOYSA-N platinum Chemical compound [Pt] BASFCYQUMIYNBI-UHFFFAOYSA-N 0.000 description 2
229920001451 polypropylene glycol Polymers 0.000 description 2
229940068977 polysorbate 20 Drugs 0.000 description 2
229920002981 polyvinylidene fluoride Polymers 0.000 description 2
239000011148 porous material Substances 0.000 description 2
OXCMYAYHXIHQOA-UHFFFAOYSA-N potassium;[2-butyl-5-chloro-3-[[4-[2-(1,2,4-triaza-3-azanidacyclopenta-1,4-dien-5-yl)phenyl]phenyl]methyl]imidazol-4-yl]methanol Chemical compound [K+].CCCCC1=NC(Cl)=C(CO)N1CC1=CC=C(C=2C(=CC=CC=2)C2=N[N-]N=N2)C=C1 OXCMYAYHXIHQOA-UHFFFAOYSA-N 0.000 description 2
238000011533 pre-incubation Methods 0.000 description 2
230000002335 preservative effect Effects 0.000 description 2
230000003449 preventive effect Effects 0.000 description 2
125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 2
230000035755 proliferation Effects 0.000 description 2
QELSKZZBTMNZEB-UHFFFAOYSA-N propylparaben Chemical compound CCCOC(=O)C1=CC=C(O)C=C1 QELSKZZBTMNZEB-UHFFFAOYSA-N 0.000 description 2
RXWNCPJZOCPEPQ-NVWDDTSBSA-N puromycin Chemical compound C1=CC(OC)=CC=C1C[C@H](N)C(=O)N[C@H]1[C@@H](O)[C@H](N2C3=NC=NC(=C3N=C2)N(C)C)O[C@@H]1CO RXWNCPJZOCPEPQ-NVWDDTSBSA-N 0.000 description 2
229960004622 raloxifene Drugs 0.000 description 2
GZUITABIAKMVPG-UHFFFAOYSA-N raloxifene Chemical compound C1=CC(O)=CC=C1C1=C(C(=O)C=2C=CC(OCCN3CCCCC3)=CC=2)C2=CC=C(O)C=C2S1 GZUITABIAKMVPG-UHFFFAOYSA-N 0.000 description 2
239000011347 resin Substances 0.000 description 2
229920005989 resin Polymers 0.000 description 2
GHMLBKRAJCXXBS-UHFFFAOYSA-N resorcinol Chemical compound OC1=CC=CC(O)=C1 GHMLBKRAJCXXBS-UHFFFAOYSA-N 0.000 description 2
230000035945 sensitivity Effects 0.000 description 2
238000000926 separation method Methods 0.000 description 2
238000002741 site-directed mutagenesis Methods 0.000 description 2
239000011780 sodium chloride Substances 0.000 description 2
239000002904 solvent Substances 0.000 description 2
238000011301 standard therapy Methods 0.000 description 2
PVYJZLYGTZKPJE-UHFFFAOYSA-N streptonigrin Chemical compound C=1C=C2C(=O)C(OC)=C(N)C(=O)C2=NC=1C(C=1N)=NC(C(O)=O)=C(C)C=1C1=CC=C(OC)C(OC)=C1O PVYJZLYGTZKPJE-UHFFFAOYSA-N 0.000 description 2
235000000346 sugar Nutrition 0.000 description 2
150000008163 sugars Chemical class 0.000 description 2
230000004654 survival pathway Effects 0.000 description 2
208000024891 symptom Diseases 0.000 description 2
230000008685 targeting Effects 0.000 description 2
238000011285 therapeutic regimen Methods 0.000 description 2
FYSNRJHAOHDILO-UHFFFAOYSA-N thionyl chloride Chemical compound ClS(Cl)=O FYSNRJHAOHDILO-UHFFFAOYSA-N 0.000 description 2
229960001196 thiotepa Drugs 0.000 description 2
229940104230 thymidine Drugs 0.000 description 2
WYWHKKSPHMUBEB-UHFFFAOYSA-N tioguanine Chemical compound N1C(N)=NC(=S)C2=C1N=CN2 WYWHKKSPHMUBEB-UHFFFAOYSA-N 0.000 description 2
231100000041 toxicology testing Toxicity 0.000 description 2
230000002103 transcriptional effect Effects 0.000 description 2
230000009466 transformation Effects 0.000 description 2
241001430294 unidentified retrovirus Species 0.000 description 2
238000011144 upstream manufacturing Methods 0.000 description 2
210000003932 urinary bladder Anatomy 0.000 description 2
229960004528 vincristine Drugs 0.000 description 2
OGWKCGZFUXNPDA-XQKSVPLYSA-N vincristine Chemical compound C([N@]1C[C@@H](C[C@]2(C(=O)OC)C=3C(=CC4=C([C@]56[C@H]([C@@]([C@H](OC(C)=O)[C@]7(CC)C=CCN([C@H]67)CC5)(O)C(=O)OC)N4C=O)C=3)OC)C[C@@](C1)(O)CC)CC1=C2NC2=CC=CC=C12 OGWKCGZFUXNPDA-XQKSVPLYSA-N 0.000 description 2
OGWKCGZFUXNPDA-UHFFFAOYSA-N vincristine Natural products C1C(CC)(O)CC(CC2(C(=O)OC)C=3C(=CC4=C(C56C(C(C(OC(C)=O)C7(CC)C=CCN(C67)CC5)(O)C(=O)OC)N4C=O)C=3)OC)CN1CCC1=C2NC2=CC=CC=C12 OGWKCGZFUXNPDA-UHFFFAOYSA-N 0.000 description 2
238000001262 western blot Methods 0.000 description 2
239000012130 whole-cell lysate Substances 0.000 description 2
229940053867 xeloda Drugs 0.000 description 2
HDTRYLNUVZCQOY-UHFFFAOYSA-N α-D-glucopyranosyl-α-D-glucopyranoside Natural products OC1C(O)C(O)C(CO)OC1OC1C(O)C(O)C(O)C(CO)O1 HDTRYLNUVZCQOY-UHFFFAOYSA-N 0.000 description 1
DIGQNXIGRZPYDK-WKSCXVIASA-N (2R)-6-amino-2-[[2-[[(2S)-2-[[2-[[(2R)-2-[[(2S)-2-[[(2R,3S)-2-[[2-[[(2S)-2-[[2-[[(2S)-2-[[(2S)-2-[[(2R)-2-[[(2S,3S)-2-[[(2R)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[2-[[(2S)-2-[[(2R)-2-[[2-[[2-[[2-[(2-amino-1-hydroxyethylidene)amino]-3-carboxy-1-hydroxypropylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1-hydroxyethylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1,3-dihydroxypropylidene]amino]-1-hydroxyethylidene]amino]-1-hydroxypropylidene]amino]-1,3-dihydroxypropylidene]amino]-1,3-dihydroxypropylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1,3-dihydroxybutylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1-hydroxypropylidene]amino]-1,3-dihydroxypropylidene]amino]-1-hydroxyethylidene]amino]-1,5-dihydroxy-5-iminopentylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1,3-dihydroxybutylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1,3-dihydroxypropylidene]amino]-1-hydroxyethylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1-hydroxyethylidene]amino]hexanoic acid Chemical compound C[C@@H]([C@@H](C(=N[C@@H](CS)C(=N[C@@H](C)C(=N[C@@H](CO)C(=NCC(=N[C@@H](CCC(=N)O)C(=NC(CS)C(=N[C@H]([C@H](C)O)C(=N[C@H](CS)C(=N[C@H](CO)C(=NCC(=N[C@H](CS)C(=NCC(=N[C@H](CCCCN)C(=O)O)O)O)O)O)O)O)O)O)O)O)O)O)O)N=C([C@H](CS)N=C([C@H](CO)N=C([C@H](CO)N=C([C@H](C)N=C(CN=C([C@H](CO)N=C([C@H](CS)N=C(CN=C(C(CS)N=C(C(CC(=O)O)N=C(CN)O)O)O)O)O)O)O)O)O)O)O)O DIGQNXIGRZPYDK-WKSCXVIASA-N 0.000 description 1
WDQLRUYAYXDIFW-RWKIJVEZSA-N (2r,3r,4s,5r,6r)-4-[(2s,3r,4s,5r,6r)-3,5-dihydroxy-4-[(2r,3r,4s,5s,6r)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy-6-[[(2r,3r,4s,5s,6r)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxymethyl]oxan-2-yl]oxy-6-(hydroxymethyl)oxane-2,3,5-triol Chemical compound O[C@@H]1[C@@H](CO)O[C@@H](O)[C@H](O)[C@H]1O[C@H]1[C@H](O)[C@@H](O[C@H]2[C@@H]([C@@H](O)[C@H](O)[C@@H](CO)O2)O)[C@H](O)[C@@H](CO[C@H]2[C@@H]([C@@H](O)[C@H](O)[C@@H](CO)O2)O)O1 WDQLRUYAYXDIFW-RWKIJVEZSA-N 0.000 description 1
FLWWDYNPWOSLEO-HQVZTVAUSA-N (2s)-2-[[4-[1-(2-amino-4-oxo-1h-pteridin-6-yl)ethyl-methylamino]benzoyl]amino]pentanedioic acid Chemical compound C=1N=C2NC(N)=NC(=O)C2=NC=1C(C)N(C)C1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 FLWWDYNPWOSLEO-HQVZTVAUSA-N 0.000 description 1
QZNNVYOVQUKYSC-JEDNCBNOSA-N (2s)-2-amino-3-(1h-imidazol-5-yl)propanoic acid;hydron;chloride Chemical compound Cl.OC(=O)[C@@H](N)CC1=CN=CN1 QZNNVYOVQUKYSC-JEDNCBNOSA-N 0.000 description 1
XMQUEQJCYRFIQS-YFKPBYRVSA-N (2s)-2-amino-5-ethoxy-5-oxopentanoic acid Chemical compound CCOC(=O)CC[C@H](N)C(O)=O XMQUEQJCYRFIQS-YFKPBYRVSA-N 0.000 description 1
KYBXNPIASYUWLN-WUCPZUCCSA-N (2s)-5-hydroxypyrrolidine-2-carboxylic acid Chemical compound OC1CC[C@@H](C(O)=O)N1 KYBXNPIASYUWLN-WUCPZUCCSA-N 0.000 description 1
WCGUUGGRBIKTOS-GPOJBZKASA-N (3beta)-3-hydroxyurs-12-en-28-oic acid Chemical compound C1C[C@H](O)C(C)(C)[C@@H]2CC[C@@]3(C)[C@]4(C)CC[C@@]5(C(O)=O)CC[C@@H](C)[C@H](C)[C@H]5C4=CC[C@@H]3[C@]21C WCGUUGGRBIKTOS-GPOJBZKASA-N 0.000 description 1
MZOFCQQQCNRIBI-VMXHOPILSA-N (3s)-4-[[(2s)-1-[[(2s)-1-[[(1s)-1-carboxy-2-hydroxyethyl]amino]-4-methyl-1-oxopentan-2-yl]amino]-5-(diaminomethylideneamino)-1-oxopentan-2-yl]amino]-3-[[2-[[(2s)-2,6-diaminohexanoyl]amino]acetyl]amino]-4-oxobutanoic acid Chemical compound OC[C@@H](C(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCN=C(N)N)NC(=O)[C@H](CC(O)=O)NC(=O)CNC(=O)[C@@H](N)CCCCN MZOFCQQQCNRIBI-VMXHOPILSA-N 0.000 description 1
XRBSKUSTLXISAB-XVVDYKMHSA-N (5r,6r,7r,8r)-8-hydroxy-7-(hydroxymethyl)-5-(3,4,5-trimethoxyphenyl)-5,6,7,8-tetrahydrobenzo[f][1,3]benzodioxole-6-carboxylic acid Chemical compound COC1=C(OC)C(OC)=CC([C@@H]2C3=CC=4OCOC=4C=C3[C@H](O)[C@@H](CO)[C@@H]2C(O)=O)=C1 XRBSKUSTLXISAB-XVVDYKMHSA-N 0.000 description 1
IEUUDEWWMRQUDS-UHFFFAOYSA-N (6-azaniumylidene-1,6-dimethoxyhexylidene)azanium;dichloride Chemical compound Cl.Cl.COC(=N)CCCCC(=N)OC IEUUDEWWMRQUDS-UHFFFAOYSA-N 0.000 description 1
JXVAMODRWBNUSF-KZQKBALLSA-N (7s,9r,10r)-7-[(2r,4s,5s,6s)-5-[[(2s,4as,5as,7s,9s,9ar,10ar)-2,9-dimethyl-3-oxo-4,4a,5a,6,7,9,9a,10a-octahydrodipyrano[4,2-a:4',3'-e][1,4]dioxin-7-yl]oxy]-4-(dimethylamino)-6-methyloxan-2-yl]oxy-10-[(2s,4s,5s,6s)-4-(dimethylamino)-5-hydroxy-6-methyloxan-2 Chemical compound O([C@@H]1C2=C(O)C=3C(=O)C4=CC=CC(O)=C4C(=O)C=3C(O)=C2[C@@H](O[C@@H]2O[C@@H](C)[C@@H](O[C@@H]3O[C@@H](C)[C@H]4O[C@@H]5O[C@@H](C)C(=O)C[C@@H]5O[C@H]4C3)[C@H](C2)N(C)C)C[C@]1(O)CC)[C@H]1C[C@H](N(C)C)[C@H](O)[C@H](C)O1 JXVAMODRWBNUSF-KZQKBALLSA-N 0.000 description 1
FPVKHBSQESCIEP-UHFFFAOYSA-N (8S)-3-(2-deoxy-beta-D-erythro-pentofuranosyl)-3,6,7,8-tetrahydroimidazo[4,5-d][1,3]diazepin-8-ol Natural products C1C(O)C(CO)OC1N1C(NC=NCC2O)=C2N=C1 FPVKHBSQESCIEP-UHFFFAOYSA-N 0.000 description 1
LKJPYSCBVHEWIU-KRWDZBQOSA-N (R)-bicalutamide Chemical compound C([C@@](O)(C)C(=O)NC=1C=C(C(C#N)=CC=1)C(F)(F)F)S(=O)(=O)C1=CC=C(F)C=C1 LKJPYSCBVHEWIU-KRWDZBQOSA-N 0.000 description 1
AGNGYMCLFWQVGX-AGFFZDDWSA-N (e)-1-[(2s)-2-amino-2-carboxyethoxy]-2-diazonioethenolate Chemical compound OC(=O)[C@@H](N)CO\C([O-])=C\[N+]#N AGNGYMCLFWQVGX-AGFFZDDWSA-N 0.000 description 1
108091032973 (ribonucleotides)n+m Proteins 0.000 description 1
NWUYHJFMYQTDRP-UHFFFAOYSA-N 1,2-bis(ethenyl)benzene;1-ethenyl-2-ethylbenzene;styrene Chemical compound C=CC1=CC=CC=C1.CCC1=CC=CC=C1C=C.C=CC1=CC=CC=C1C=C NWUYHJFMYQTDRP-UHFFFAOYSA-N 0.000 description 1
VILFTWLXLYIEMV-UHFFFAOYSA-N 1,5-difluoro-2,4-dinitrobenzene Chemical compound [O-][N+](=O)C1=CC([N+]([O-])=O)=C(F)C=C1F VILFTWLXLYIEMV-UHFFFAOYSA-N 0.000 description 1
MYBLAOJMRYYKMS-RTRLPJTCSA-N 1-(2-chloroethyl)-1-nitroso-3-[(3r,4r,5s,6r)-2,4,5-trihydroxy-6-(hydroxymethyl)oxan-3-yl]urea Chemical compound OC[C@H]1OC(O)[C@H](NC(=O)N(CCCl)N=O)[C@@H](O)[C@@H]1O MYBLAOJMRYYKMS-RTRLPJTCSA-N 0.000 description 1
PRDFBSVERLRRMY-UHFFFAOYSA-N 2'-(4-ethoxyphenyl)-5-(4-methylpiperazin-1-yl)-2,5'-bibenzimidazole Chemical compound C1=CC(OCC)=CC=C1C1=NC2=CC=C(C=3NC4=CC(=CC=C4N=3)N3CCN(C)CC3)C=C2N1 PRDFBSVERLRRMY-UHFFFAOYSA-N 0.000 description 1
YBBNVCVOACOHIG-UHFFFAOYSA-N 2,2-diamino-1,4-bis(4-azidophenyl)-3-butylbutane-1,4-dione Chemical compound C=1C=C(N=[N+]=[N-])C=CC=1C(=O)C(N)(N)C(CCCC)C(=O)C1=CC=C(N=[N+]=[N-])C=C1 YBBNVCVOACOHIG-UHFFFAOYSA-N 0.000 description 1
LDGWQMRUWMSZIU-LQDDAWAPSA-M 2,3-bis[(z)-octadec-9-enoxy]propyl-trimethylazanium;chloride Chemical compound [Cl-].CCCCCCCC\C=C/CCCCCCCCOCC(C[N+](C)(C)C)OCCCCCCCC\C=C/CCCCCCCC LDGWQMRUWMSZIU-LQDDAWAPSA-M 0.000 description 1
BTOTXLJHDSNXMW-POYBYMJQSA-N 2,3-dideoxyuridine Chemical compound O1[C@H](CO)CC[C@@H]1N1C(=O)NC(=O)C=C1 BTOTXLJHDSNXMW-POYBYMJQSA-N 0.000 description 1
KGLPWQKSKUVKMJ-UHFFFAOYSA-N 2,3-dihydrophthalazine-1,4-dione Chemical class C1=CC=C2C(=O)NNC(=O)C2=C1 KGLPWQKSKUVKMJ-UHFFFAOYSA-N 0.000 description 1
FALRKNHUBBKYCC-UHFFFAOYSA-N 2-(chloromethyl)pyridine-3-carbonitrile Chemical compound ClCC1=NC=CC=C1C#N FALRKNHUBBKYCC-UHFFFAOYSA-N 0.000 description 1
FZDFGHZZPBUTGP-UHFFFAOYSA-N 2-[[2-[bis(carboxymethyl)amino]-3-(4-isothiocyanatophenyl)propyl]-[2-[bis(carboxymethyl)amino]propyl]amino]acetic acid Chemical compound OC(=O)CN(CC(O)=O)C(C)CN(CC(O)=O)CC(N(CC(O)=O)CC(O)=O)CC1=CC=C(N=C=S)C=C1 FZDFGHZZPBUTGP-UHFFFAOYSA-N 0.000 description 1
FBUTXZSKZCQABC-UHFFFAOYSA-N 2-amino-1-methyl-7h-purine-6-thione Chemical compound S=C1N(C)C(N)=NC2=C1NC=N2 FBUTXZSKZCQABC-UHFFFAOYSA-N 0.000 description 1
QCXJFISCRQIYID-IAEPZHFASA-N 2-amino-1-n-[(3s,6s,7r,10s,16s)-3-[(2s)-butan-2-yl]-7,11,14-trimethyl-2,5,9,12,15-pentaoxo-10-propan-2-yl-8-oxa-1,4,11,14-tetrazabicyclo[14.3.0]nonadecan-6-yl]-4,6-dimethyl-3-oxo-9-n-[(3s,6s,7r,10s,16s)-7,11,14-trimethyl-2,5,9,12,15-pentaoxo-3,10-di(propa Chemical compound C[C@H]1OC(=O)[C@H](C(C)C)N(C)C(=O)CN(C)C(=O)[C@@H]2CCCN2C(=O)[C@H](C(C)C)NC(=O)[C@H]1NC(=O)C1=C(N=C2C(C(=O)N[C@@H]3C(=O)N[C@H](C(N4CCC[C@H]4C(=O)N(C)CC(=O)N(C)[C@@H](C(C)C)C(=O)O[C@@H]3C)=O)[C@@H](C)CC)=C(N)C(=O)C(C)=C2O2)C2=C(C)C=C1 QCXJFISCRQIYID-IAEPZHFASA-N 0.000 description 1
125000000979 2-amino-2-oxoethyl group Chemical group [H]C([*])([H])C(=O)N([H])[H] 0.000 description 1
CTRPRMNBTVRDFH-UHFFFAOYSA-N 2-n-methyl-1,3,5-triazine-2,4,6-triamine Chemical class CNC1=NC(N)=NC(N)=N1 CTRPRMNBTVRDFH-UHFFFAOYSA-N 0.000 description 1
AOPRXJXHLWYPQR-UHFFFAOYSA-N 2-phenoxyacetamide Chemical class NC(=O)COC1=CC=CC=C1 AOPRXJXHLWYPQR-UHFFFAOYSA-N 0.000 description 1
LBYVZRFDLNAPRC-UHFFFAOYSA-N 2-sulfanylguanidine Chemical compound NC(=N)NS LBYVZRFDLNAPRC-UHFFFAOYSA-N 0.000 description 1
102100039377 28 kDa heat- and acid-stable phosphoprotein Human genes 0.000 description 1
101710176122 28 kDa heat- and acid-stable phosphoprotein Proteins 0.000 description 1
NDMPLJNOPCLANR-UHFFFAOYSA-N 3,4-dihydroxy-15-(4-hydroxy-18-methoxycarbonyl-5,18-seco-ibogamin-18-yl)-16-methoxy-1-methyl-6,7-didehydro-aspidospermidine-3-carboxylic acid methyl ester Natural products C1C(CC)(O)CC(CC2(C(=O)OC)C=3C(=CC4=C(C56C(C(C(O)C7(CC)C=CCN(C67)CC5)(O)C(=O)OC)N4C)C=3)OC)CN1CCC1=C2NC2=CC=CC=C12 NDMPLJNOPCLANR-UHFFFAOYSA-N 0.000 description 1
PWMYMKOUNYTVQN-UHFFFAOYSA-N 3-(8,8-diethyl-2-aza-8-germaspiro[4.5]decan-2-yl)-n,n-dimethylpropan-1-amine Chemical compound C1C[Ge](CC)(CC)CCC11CN(CCCN(C)C)CC1 PWMYMKOUNYTVQN-UHFFFAOYSA-N 0.000 description 1
UMCMPZBLKLEWAF-BCTGSCMUSA-N 3-[(3-cholamidopropyl)dimethylammonio]propane-1-sulfonate Chemical compound C([C@H]1C[C@H]2O)[C@H](O)CC[C@]1(C)[C@@H]1[C@@H]2[C@@H]2CC[C@H]([C@@H](CCC(=O)NCCC[N+](C)(C)CCCS([O-])(=O)=O)C)[C@@]2(C)[C@@H](O)C1 UMCMPZBLKLEWAF-BCTGSCMUSA-N 0.000 description 1
MIJYXULNPSFWEK-GTOFXWBISA-N 3beta-hydroxyolean-12-en-28-oic acid Chemical compound C1C[C@H](O)C(C)(C)[C@@H]2CC[C@@]3(C)[C@]4(C)CC[C@@]5(C(O)=O)CCC(C)(C)C[C@H]5C4=CC[C@@H]3[C@]21C MIJYXULNPSFWEK-GTOFXWBISA-N 0.000 description 1
CNJLMVZFWLNOEP-UHFFFAOYSA-N 4,7,7-trimethylbicyclo[4.1.0]heptan-5-one Chemical compound O=C1C(C)CCC2C(C)(C)C12 CNJLMVZFWLNOEP-UHFFFAOYSA-N 0.000 description 1
OBWSOTREAMFOCQ-UHFFFAOYSA-N 4-(4-amino-3,5-dimethylphenyl)-2,6-dimethylaniline;hydrochloride Chemical compound Cl.CC1=C(N)C(C)=CC(C=2C=C(C)C(N)=C(C)C=2)=C1 OBWSOTREAMFOCQ-UHFFFAOYSA-N 0.000 description 1
XZKIHKMTEMTJQX-UHFFFAOYSA-N 4-Nitrophenyl Phosphate Chemical compound OP(O)(=O)OC1=CC=C([N+]([O-])=O)C=C1 XZKIHKMTEMTJQX-UHFFFAOYSA-N 0.000 description 1
QFVHZQCOUORWEI-UHFFFAOYSA-N 4-[(4-anilino-5-sulfonaphthalen-1-yl)diazenyl]-5-hydroxynaphthalene-2,7-disulfonic acid Chemical compound C=12C(O)=CC(S(O)(=O)=O)=CC2=CC(S(O)(=O)=O)=CC=1N=NC(C1=CC=CC(=C11)S(O)(=O)=O)=CC=C1NC1=CC=CC=C1 QFVHZQCOUORWEI-UHFFFAOYSA-N 0.000 description 1
DODQJNMQWMSYGS-QPLCGJKRSA-N 4-[(z)-1-[4-[2-(dimethylamino)ethoxy]phenyl]-1-phenylbut-1-en-2-yl]phenol Chemical compound C=1C=C(O)C=CC=1C(/CC)=C(C=1C=CC(OCCN(C)C)=CC=1)/C1=CC=CC=C1 DODQJNMQWMSYGS-QPLCGJKRSA-N 0.000 description 1
101710169336 5'-deoxyadenosine deaminase Proteins 0.000 description 1
IDPUKCWIGUEADI-UHFFFAOYSA-N 5-[bis(2-chloroethyl)amino]uracil Chemical class ClCCN(CCCl)C1=CNC(=O)NC1=O IDPUKCWIGUEADI-UHFFFAOYSA-N 0.000 description 1
NMUSYJAQQFHJEW-KVTDHHQDSA-N 5-azacytidine Chemical compound O=C1N=C(N)N=CN1[C@H]1[C@H](O)[C@H](O)[C@@H](CO)O1 NMUSYJAQQFHJEW-KVTDHHQDSA-N 0.000 description 1
FHIDNBAQOFJWCA-UAKXSSHOSA-N 5-fluorouridine Chemical compound O[C@@H]1[C@H](O)[C@@H](CO)O[C@H]1N1C(=O)NC(=O)C(F)=C1 FHIDNBAQOFJWCA-UAKXSSHOSA-N 0.000 description 1
229940117976 5-hydroxylysine Drugs 0.000 description 1
WYXSYVWAUAUWLD-SHUUEZRQSA-N 6-azauridine Chemical compound O[C@@H]1[C@H](O)[C@@H](CO)O[C@H]1N1C(=O)NC(=O)C=N1 WYXSYVWAUAUWLD-SHUUEZRQSA-N 0.000 description 1
ZGXJTSGNIOSYLO-UHFFFAOYSA-N 88755TAZ87 Chemical compound NCC(=O)CCC(O)=O ZGXJTSGNIOSYLO-UHFFFAOYSA-N 0.000 description 1
HDZZVAMISRMYHH-UHFFFAOYSA-N 9beta-Ribofuranosyl-7-deazaadenin Natural products C1=CC=2C(N)=NC=NC=2N1C1OC(CO)C(O)C1O HDZZVAMISRMYHH-UHFFFAOYSA-N 0.000 description 1
108010066676 Abrin Proteins 0.000 description 1
QTBSBXVTEAMEQO-UHFFFAOYSA-M Acetate Chemical compound CC([O-])=O QTBSBXVTEAMEQO-UHFFFAOYSA-M 0.000 description 1
102000007469 Actins Human genes 0.000 description 1
108010085238 Actins Proteins 0.000 description 1
108010059616 Activins Proteins 0.000 description 1
208000030090 Acute Disease Diseases 0.000 description 1
102100036664 Adenosine deaminase Human genes 0.000 description 1
241000256173 Aedes albopictus Species 0.000 description 1
101710187573 Alcohol dehydrogenase 2 Proteins 0.000 description 1
101710133776 Alcohol dehydrogenase class-3 Proteins 0.000 description 1
102100023635 Alpha-fetoprotein Human genes 0.000 description 1
108090000672 Annexin A5 Proteins 0.000 description 1
102000004121 Annexin A5 Human genes 0.000 description 1
108010039627 Aprotinin Proteins 0.000 description 1
239000004475 Arginine Substances 0.000 description 1
208000002109 Argyria Diseases 0.000 description 1
102000009133 Arylsulfatases Human genes 0.000 description 1
DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 1
241000228212 Aspergillus Species 0.000 description 1
241000351920 Aspergillus nidulans Species 0.000 description 1
241000228245 Aspergillus niger Species 0.000 description 1
101000669426 Aspergillus restrictus Ribonuclease mitogillin Proteins 0.000 description 1
101710192393 Attachment protein G3P Proteins 0.000 description 1
241001203868 Autographa californica Species 0.000 description 1
108091008875 B cell receptors Proteins 0.000 description 1
238000011725 BALB/c mouse Methods 0.000 description 1
235000014469 Bacillus subtilis Nutrition 0.000 description 1
108090000363 Bacterial Luciferases Proteins 0.000 description 1
VGGGPCQERPFHOB-MCIONIFRSA-N Bestatin Chemical compound CC(C)C[C@H](C(O)=O)NC(=O)[C@@H](O)[C@H](N)CC1=CC=CC=C1 VGGGPCQERPFHOB-MCIONIFRSA-N 0.000 description 1
241000255789 Bombyx mori Species 0.000 description 1
241000409811 Bombyx mori nucleopolyhedrovirus Species 0.000 description 1
241000283690 Bos taurus Species 0.000 description 1
COVZYZSDYWQREU-UHFFFAOYSA-N Busulfan Chemical compound CS(=O)(=O)OCCCCOS(C)(=O)=O COVZYZSDYWQREU-UHFFFAOYSA-N 0.000 description 1
239000002126 C01EB10 - Adenosine Substances 0.000 description 1
OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 1
UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 1
241000222120 Candida <Saccharomycetales> Species 0.000 description 1
241000222122 Candida albicans Species 0.000 description 1
241000282472 Canis lupus familiaris Species 0.000 description 1
101710158575 Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase Proteins 0.000 description 1
GAGWJHPBXLXJQN-UHFFFAOYSA-N Capecitabine Natural products C1=C(F)C(NC(=O)OCCCCC)=NC(=O)N1C1C(O)C(O)C(C)O1 GAGWJHPBXLXJQN-UHFFFAOYSA-N 0.000 description 1
108090000565 Capsid Proteins Proteins 0.000 description 1
101710169873 Capsid protein G8P Proteins 0.000 description 1
OKTJSMMVPCPJKN-NJFSPNSNSA-N Carbon-14 Chemical compound [14C] OKTJSMMVPCPJKN-NJFSPNSNSA-N 0.000 description 1
BVKZGUZCCUSVTD-UHFFFAOYSA-L Carbonate Chemical compound [O-]C([O-])=O BVKZGUZCCUSVTD-UHFFFAOYSA-L 0.000 description 1
SHHKQEUPHAENFK-UHFFFAOYSA-N Carboquone Chemical compound O=C1C(C)=C(N2CC2)C(=O)C(C(COC(N)=O)OC)=C1N1CC1 SHHKQEUPHAENFK-UHFFFAOYSA-N 0.000 description 1
102000004031 Carboxy-Lyases Human genes 0.000 description 1
108090000489 Carboxy-Lyases Proteins 0.000 description 1
102000005367 Carboxypeptidases Human genes 0.000 description 1
108010006303 Carboxypeptidases Proteins 0.000 description 1
208000005623 Carcinogenesis Diseases 0.000 description 1
208000031229 Cardiomyopathies Diseases 0.000 description 1
DLGOEMSEDOSKAD-UHFFFAOYSA-N Carmustine Chemical compound ClCCNC(=O)N(N=O)CCCl DLGOEMSEDOSKAD-UHFFFAOYSA-N 0.000 description 1
108090000712 Cathepsin B Proteins 0.000 description 1
102000004225 Cathepsin B Human genes 0.000 description 1
102400001321 Cathepsin L Human genes 0.000 description 1
108090000624 Cathepsin L Proteins 0.000 description 1
102000005600 Cathepsins Human genes 0.000 description 1
108010084457 Cathepsins Proteins 0.000 description 1
102000000844 Cell Surface Receptors Human genes 0.000 description 1
108010001857 Cell Surface Receptors Proteins 0.000 description 1
231100000023 Cell-mediated cytotoxicity Toxicity 0.000 description 1
206010057250 Cell-mediated cytotoxicity Diseases 0.000 description 1
102100023321 Ceruloplasmin Human genes 0.000 description 1
JWBOIMRXGHLCPP-UHFFFAOYSA-N Chloditan Chemical compound C=1C=CC=C(Cl)C=1C(C(Cl)Cl)C1=CC=C(Cl)C=C1 JWBOIMRXGHLCPP-UHFFFAOYSA-N 0.000 description 1
VEXZGXHMUGYJMC-UHFFFAOYSA-M Chloride anion Chemical compound [Cl-] VEXZGXHMUGYJMC-UHFFFAOYSA-M 0.000 description 1
241000282552 Chlorocebus aethiops Species 0.000 description 1
102100021809 Chorionic somatomammotropin hormone 1 Human genes 0.000 description 1
208000017667 Chronic Disease Diseases 0.000 description 1
108090000746 Chymosin Proteins 0.000 description 1
KRKNYBCHXYNGOX-UHFFFAOYSA-K Citrate Chemical compound [O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O KRKNYBCHXYNGOX-UHFFFAOYSA-K 0.000 description 1
102000007644 Colony-Stimulating Factors Human genes 0.000 description 1
108010071942 Colony-Stimulating Factors Proteins 0.000 description 1
108020004635 Complementary DNA Proteins 0.000 description 1
229920000742 Cotton Polymers 0.000 description 1
241000699800 Cricetinae Species 0.000 description 1
108700032819 Croton tiglium crotin II Proteins 0.000 description 1
102000000311 Cytosine Deaminase Human genes 0.000 description 1
108010080611 Cytosine Deaminase Proteins 0.000 description 1
102100037579 D-3-phosphoglycerate dehydrogenase Human genes 0.000 description 1
FBPFZTCFMRRESA-FSIIMWSLSA-N D-Glucitol Natural products OC[C@H](O)[C@H](O)[C@@H](O)[C@H](O)CO FBPFZTCFMRRESA-FSIIMWSLSA-N 0.000 description 1
IGXWBGJHJZYPQS-SSDOTTSWSA-N D-Luciferin Chemical compound OC(=O)[C@H]1CSC(C=2SC3=CC=C(O)C=C3N=2)=N1 IGXWBGJHJZYPQS-SSDOTTSWSA-N 0.000 description 1
FBPFZTCFMRRESA-KVTDHHQDSA-N D-Mannitol Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-KVTDHHQDSA-N 0.000 description 1
QNAYBMKLOCPYGJ-UWTATZPHSA-N D-alanine Chemical compound C[C@@H](N)C(O)=O QNAYBMKLOCPYGJ-UWTATZPHSA-N 0.000 description 1
QNAYBMKLOCPYGJ-UHFFFAOYSA-N D-alpha-Ala Natural products CC([NH3+])C([O-])=O QNAYBMKLOCPYGJ-UHFFFAOYSA-N 0.000 description 1
150000008574 D-amino acids Chemical group 0.000 description 1
ZZZCUOFIHGPKAK-UHFFFAOYSA-N D-erythro-ascorbic acid Natural products OCC1OC(=O)C(O)=C1O ZZZCUOFIHGPKAK-UHFFFAOYSA-N 0.000 description 1
FBPFZTCFMRRESA-JGWLITMVSA-N D-glucitol Chemical compound OC[C@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-JGWLITMVSA-N 0.000 description 1
WQZGKKKJIJFFOK-QTVWNMPRSA-N D-mannopyranose Chemical compound OC[C@H]1OC(O)[C@@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-QTVWNMPRSA-N 0.000 description 1
XUIIKFGFIJCVMT-GFCCVEGCSA-N D-thyroxine Chemical compound IC1=CC(C[C@@H](N)C(O)=O)=CC(I)=C1OC1=CC(I)=C(O)C(I)=C1 XUIIKFGFIJCVMT-GFCCVEGCSA-N 0.000 description 1
102000053602 DNA Human genes 0.000 description 1
239000012624 DNA alkylating agent Substances 0.000 description 1
WEAHRLBPCANXCN-UHFFFAOYSA-N Daunomycin Natural products CCC1(O)CC(OC2CC(N)C(O)C(C)O2)c3cc4C(=O)c5c(OC)cccc5C(=O)c4c(O)c3C1 WEAHRLBPCANXCN-UHFFFAOYSA-N 0.000 description 1
CYCGRDQQIOGCKX-UHFFFAOYSA-N Dehydro-luciferin Natural products OC(=O)C1=CSC(C=2SC3=CC(O)=CC=C3N=2)=N1 CYCGRDQQIOGCKX-UHFFFAOYSA-N 0.000 description 1
101710088194 Dehydrogenase Proteins 0.000 description 1
108010053770 Deoxyribonucleases Proteins 0.000 description 1
102000016911 Deoxyribonucleases Human genes 0.000 description 1
241000702421 Dependoparvovirus Species 0.000 description 1
229920002307 Dextran Polymers 0.000 description 1
239000004375 Dextrin Substances 0.000 description 1
229920001353 Dextrin Polymers 0.000 description 1
102000016607 Diphtheria Toxin Human genes 0.000 description 1
108010053187 Diphtheria Toxin Proteins 0.000 description 1
206010059866 Drug resistance Diseases 0.000 description 1
108030004793 Dual-specificity kinases Proteins 0.000 description 1
SAMRUMKYXPVKPA-VFKOLLTISA-N Enocitabine Chemical compound O=C1N=C(NC(=O)CCCCCCCCCCCCCCCCCCCCC)C=CN1[C@H]1[C@@H](O)[C@H](O)[C@@H](CO)O1 SAMRUMKYXPVKPA-VFKOLLTISA-N 0.000 description 1
241000588914 Enterobacter Species 0.000 description 1
241000588921 Enterobacteriaceae Species 0.000 description 1
YQYJSBFKSSDGFO-UHFFFAOYSA-N Epihygromycin Natural products OC1C(O)C(C(=O)C)OC1OC(C(=C1)O)=CC=C1C=C(C)C(=O)NC1C(O)C(O)C2OCOC2C1O YQYJSBFKSSDGFO-UHFFFAOYSA-N 0.000 description 1
JKLISIRFYWXLQG-UHFFFAOYSA-N Epioleonolsaeure Natural products C1CC(O)C(C)(C)C2CCC3(C)C4(C)CCC5(C(O)=O)CCC(C)(C)CC5C4CCC3C21C JKLISIRFYWXLQG-UHFFFAOYSA-N 0.000 description 1
OBMLHUPNRURLOK-XGRAFVIBSA-N Epitiostanol Chemical compound C1[C@@H]2S[C@@H]2C[C@]2(C)[C@H]3CC[C@](C)([C@H](CC4)O)[C@@H]4[C@@H]3CC[C@H]21 OBMLHUPNRURLOK-XGRAFVIBSA-N 0.000 description 1
241000283086 Equidae Species 0.000 description 1
241000588698 Erwinia Species 0.000 description 1
241000588722 Escherichia Species 0.000 description 1
241001522878 Escherichia coli B Species 0.000 description 1
241001302584 Escherichia coli str. K-12 substr. W3110 Species 0.000 description 1
JOYRKODLDBILNP-UHFFFAOYSA-N Ethyl urethane Chemical compound CCOC(N)=O JOYRKODLDBILNP-UHFFFAOYSA-N 0.000 description 1
229910052693 Europium Inorganic materials 0.000 description 1
241000282326 Felis catus Species 0.000 description 1
102000018233 Fibroblast Growth Factor Human genes 0.000 description 1
108050007372 Fibroblast Growth Factor Proteins 0.000 description 1
241000724791 Filamentous phage Species 0.000 description 1
108090000331 Firefly luciferases Proteins 0.000 description 1
BJGNCJDXODQBOB-UHFFFAOYSA-N Fivefly Luciferin Natural products OC(=O)C1CSC(C=2SC3=CC(O)=CC=C3N=2)=N1 BJGNCJDXODQBOB-UHFFFAOYSA-N 0.000 description 1
241000700662 Fowlpox virus Species 0.000 description 1
229940123457 Free radical scavenger Drugs 0.000 description 1
230000037057 G1 phase arrest Effects 0.000 description 1
108010015133 Galactose oxidase Proteins 0.000 description 1
108010093031 Galactosidases Proteins 0.000 description 1
102000002464 Galactosidases Human genes 0.000 description 1
GYHNNYVSQQEPJS-UHFFFAOYSA-N Gallium Chemical compound [Ga] GYHNNYVSQQEPJS-UHFFFAOYSA-N 0.000 description 1
108700004714 Gelonium multiflorum GEL Proteins 0.000 description 1
108700039691 Genetic Promoter Regions Proteins 0.000 description 1
229930182566 Gentamicin Natural products 0.000 description 1
CEAZRRDELHUEMR-URQXQFDESA-N Gentamicin Chemical compound O1[C@H](C(C)NC)CC[C@@H](N)[C@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](NC)[C@@](C)(O)CO2)O)[C@H](N)C[C@@H]1N CEAZRRDELHUEMR-URQXQFDESA-N 0.000 description 1
108010073178 Glucan 1,4-alpha-Glucosidase Proteins 0.000 description 1
102100022624 Glucoamylase Human genes 0.000 description 1
102000030595 Glucokinase Human genes 0.000 description 1
108010021582 Glucokinase Proteins 0.000 description 1
239000004366 Glucose oxidase Substances 0.000 description 1
108010015776 Glucose oxidase Proteins 0.000 description 1
PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 1
102000006771 Gonadotropins Human genes 0.000 description 1
108010086677 Gonadotropins Proteins 0.000 description 1
108010069236 Goserelin Proteins 0.000 description 1
BLCLNMBMMGCOAS-URPVMXJPSA-N Goserelin Chemical compound C([C@@H](C(=O)N[C@H](COC(C)(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCN=C(N)N)C(=O)N1[C@@H](CCC1)C(=O)NNC(N)=O)NC(=O)[C@H](CO)NC(=O)[C@H](CC=1C2=CC=CC=C2NC=1)NC(=O)[C@H](CC=1NC=NC=1)NC(=O)[C@H]1NC(=O)CC1)C1=CC=C(O)C=C1 BLCLNMBMMGCOAS-URPVMXJPSA-N 0.000 description 1
244000299507 Gossypium hirsutum Species 0.000 description 1
208000031886 HIV Infections Diseases 0.000 description 1
208000037357 HIV infectious disease Diseases 0.000 description 1
101100082540 Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) pcp gene Proteins 0.000 description 1
206010019280 Heart failures Diseases 0.000 description 1
HTTJABKRGRZYRN-UHFFFAOYSA-N Heparin Chemical compound OC1C(NC(=O)C)C(O)OC(COS(O)(=O)=O)C1OC1C(OS(O)(=O)=O)C(O)C(OC2C(C(OS(O)(=O)=O)C(OC3C(C(O)C(O)C(O3)C(O)=O)OS(O)(=O)=O)C(CO)O2)NS(O)(=O)=O)C(C(O)=O)O1 HTTJABKRGRZYRN-UHFFFAOYSA-N 0.000 description 1
102000018710 Heparin-binding EGF-like Growth Factor Human genes 0.000 description 1
241000700721 Hepatitis B virus Species 0.000 description 1
102000005548 Hexokinase Human genes 0.000 description 1
108700040460 Hexokinases Proteins 0.000 description 1
102100026122 High affinity immunoglobulin gamma Fc receptor I Human genes 0.000 description 1
102100027619 Histidine-rich glycoprotein Human genes 0.000 description 1
101100118545 Holotrichia diomphalia EGF-like gene Proteins 0.000 description 1
241000282412 Homo Species 0.000 description 1
101000913074 Homo sapiens High affinity immunoglobulin gamma Fc receptor I Proteins 0.000 description 1
101001081399 Homo sapiens Histidine-rich glycoprotein Proteins 0.000 description 1
101000917826 Homo sapiens Low affinity immunoglobulin gamma Fc region receptor II-a Proteins 0.000 description 1
101000917824 Homo sapiens Low affinity immunoglobulin gamma Fc region receptor II-b Proteins 0.000 description 1
101001059454 Homo sapiens Serine/threonine-protein kinase MARK2 Proteins 0.000 description 1
108091006905 Human Serum Albumin Proteins 0.000 description 1
102000008100 Human Serum Albumin Human genes 0.000 description 1
241000701109 Human adenovirus 2 Species 0.000 description 1
241000701024 Human betaherpesvirus 5 Species 0.000 description 1
VSNHCAURESNICA-UHFFFAOYSA-N Hydroxyurea Chemical compound NC(=O)NO VSNHCAURESNICA-UHFFFAOYSA-N 0.000 description 1
UGQMRVRMYYASKQ-UHFFFAOYSA-N Hypoxanthine nucleoside Natural products OC1C(O)C(CO)OC1N1C(NC=NC2=O)=C2N=C1 UGQMRVRMYYASKQ-UHFFFAOYSA-N 0.000 description 1
MPBVHIBUJCELCL-UHFFFAOYSA-N Ibandronate Chemical compound CCCCCN(C)CCC(O)(P(O)(O)=O)P(O)(O)=O MPBVHIBUJCELCL-UHFFFAOYSA-N 0.000 description 1
XDXDZDZNSLXDNA-UHFFFAOYSA-N Idarubicin Natural products C1C(N)C(O)C(C)OC1OC1C2=C(O)C(C(=O)C3=CC=CC=C3C3=O)=C3C(O)=C2CC(O)(C(C)=O)C1 XDXDZDZNSLXDNA-UHFFFAOYSA-N 0.000 description 1
XDXDZDZNSLXDNA-TZNDIEGXSA-N Idarubicin Chemical compound C1[C@H](N)[C@H](O)[C@H](C)O[C@H]1O[C@@H]1C2=C(O)C(C(=O)C3=CC=CC=C3C3=O)=C3C(O)=C2C[C@@](O)(C(C)=O)C1 XDXDZDZNSLXDNA-TZNDIEGXSA-N 0.000 description 1
102100026120 IgG receptor FcRn large subunit p51 Human genes 0.000 description 1
101710177940 IgG receptor FcRn large subunit p51 Proteins 0.000 description 1
DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical class C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 1
102000009786 Immunoglobulin Constant Regions Human genes 0.000 description 1
108010009817 Immunoglobulin Constant Regions Proteins 0.000 description 1
108700005091 Immunoglobulin Genes Proteins 0.000 description 1
102000012745 Immunoglobulin Subunits Human genes 0.000 description 1
108010079585 Immunoglobulin Subunits Proteins 0.000 description 1
102100026818 Inhibin beta E chain Human genes 0.000 description 1
108090000723 Insulin-Like Growth Factor I Proteins 0.000 description 1
108090001117 Insulin-Like Growth Factor II Proteins 0.000 description 1
102100037852 Insulin-like growth factor I Human genes 0.000 description 1
102400000022 Insulin-like growth factor II Human genes 0.000 description 1
238000012695 Interfacial polymerization Methods 0.000 description 1
102000003996 Interferon-beta Human genes 0.000 description 1
108090000467 Interferon-beta Proteins 0.000 description 1
102000014150 Interferons Human genes 0.000 description 1
108010050904 Interferons Proteins 0.000 description 1
108010002352 Interleukin-1 Proteins 0.000 description 1
102000003814 Interleukin-10 Human genes 0.000 description 1
108090000174 Interleukin-10 Proteins 0.000 description 1
108090000177 Interleukin-11 Proteins 0.000 description 1
102000003815 Interleukin-11 Human genes 0.000 description 1
102100039064 Interleukin-3 Human genes 0.000 description 1
108010002386 Interleukin-3 Proteins 0.000 description 1
102000004388 Interleukin-4 Human genes 0.000 description 1
108090000978 Interleukin-4 Proteins 0.000 description 1
102100039897 Interleukin-5 Human genes 0.000 description 1
108010002616 Interleukin-5 Proteins 0.000 description 1
108090001005 Interleukin-6 Proteins 0.000 description 1
102000004889 Interleukin-6 Human genes 0.000 description 1
102100021592 Interleukin-7 Human genes 0.000 description 1
108010002586 Interleukin-7 Proteins 0.000 description 1
108090001007 Interleukin-8 Proteins 0.000 description 1
102000004890 Interleukin-8 Human genes 0.000 description 1
102100026871 Interleukin-9 Human genes 0.000 description 1
108010002335 Interleukin-9 Proteins 0.000 description 1
102000015696 Interleukins Human genes 0.000 description 1
108010063738 Interleukins Proteins 0.000 description 1
208000005016 Intestinal Neoplasms Diseases 0.000 description 1
241000588748 Klebsiella Species 0.000 description 1
241000235058 Komagataella pastoris Species 0.000 description 1
125000000998 L-alanino group Chemical group [H]N([*])[C@](C([H])([H])[H])([H])C(=O)O[H] 0.000 description 1
ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 description 1
229930182816 L-glutamine Natural products 0.000 description 1
LRQKBLKVPFOOQJ-YFKPBYRVSA-N L-norleucine Chemical compound CCCC[C@H]([NH3+])C([O-])=O LRQKBLKVPFOOQJ-YFKPBYRVSA-N 0.000 description 1
KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 1
JLERVPBPJHKRBJ-UHFFFAOYSA-N LY 117018 Chemical compound C1=CC(O)=CC=C1C1=C(C(=O)C=2C=CC(OCCN3CCCC3)=CC=2)C2=CC=C(O)C=C2S1 JLERVPBPJHKRBJ-UHFFFAOYSA-N 0.000 description 1
241000481961 Lachancea thermotolerans Species 0.000 description 1
102100038609 Lactoperoxidase Human genes 0.000 description 1
108010023244 Lactoperoxidase Proteins 0.000 description 1
GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 description 1
229920001491 Lentinan Polymers 0.000 description 1
GDBQQVLCIARPGH-UHFFFAOYSA-N Leupeptin Natural products CC(C)CC(NC(C)=O)C(=O)NC(CC(C)C)C(=O)NC(C=O)CCCN=C(N)N GDBQQVLCIARPGH-UHFFFAOYSA-N 0.000 description 1
HLFSDGLLUJUHTE-SNVBAGLBSA-N Levamisole Chemical compound C1([C@H]2CN3CCSC3=N2)=CC=CC=C1 HLFSDGLLUJUHTE-SNVBAGLBSA-N 0.000 description 1
GQYIWUVLTXOXAJ-UHFFFAOYSA-N Lomustine Chemical compound ClCCN(N=O)C(=O)NC1CCCCC1 GQYIWUVLTXOXAJ-UHFFFAOYSA-N 0.000 description 1
108060001084 Luciferase Proteins 0.000 description 1
239000005089 Luciferase Substances 0.000 description 1
DDWFXDSYGUXRAY-UHFFFAOYSA-N Luciferin Natural products CCc1c(C)c(CC2NC(=O)C(=C2C=C)C)[nH]c1Cc3[nH]c4C(=C5/NC(CC(=O)O)C(C)C5CC(=O)O)CC(=O)c4c3C DDWFXDSYGUXRAY-UHFFFAOYSA-N 0.000 description 1
235000007688 Lycopersicon esculentum Nutrition 0.000 description 1
102000004083 Lymphotoxin-alpha Human genes 0.000 description 1
108090000542 Lymphotoxin-alpha Proteins 0.000 description 1
239000004472 Lysine Substances 0.000 description 1
101001133631 Lysinibacillus sphaericus Penicillin acylase Proteins 0.000 description 1
241000282567 Macaca fascicularis Species 0.000 description 1
FYYHWMGAXLPEAU-UHFFFAOYSA-N Magnesium Chemical compound [Mg] FYYHWMGAXLPEAU-UHFFFAOYSA-N 0.000 description 1
101710125418 Major capsid protein Proteins 0.000 description 1
101710156564 Major tail protein Gp23 Proteins 0.000 description 1
108010026217 Malate Dehydrogenase Proteins 0.000 description 1
208000032271 Malignant tumor of penis Diseases 0.000 description 1
229930195725 Mannitol Natural products 0.000 description 1
VJRAUFKOOPNFIQ-UHFFFAOYSA-N Marcellomycin Natural products C12=C(O)C=3C(=O)C4=C(O)C=CC(O)=C4C(=O)C=3C=C2C(C(=O)OC)C(CC)(O)CC1OC(OC1C)CC(N(C)C)C1OC(OC1C)CC(O)C1OC1CC(O)C(O)C(C)O1 VJRAUFKOOPNFIQ-UHFFFAOYSA-N 0.000 description 1
241001599018 Melanogaster Species 0.000 description 1
206010027476 Metastases Diseases 0.000 description 1
229930192392 Mitomycin Natural products 0.000 description 1
244000302512 Momordica charantia Species 0.000 description 1
235000009811 Momordica charantia Nutrition 0.000 description 1
108010050619 Monokines Proteins 0.000 description 1
102000013967 Monokines Human genes 0.000 description 1
108010014251 Muramidase Proteins 0.000 description 1
102000016943 Muramidase Human genes 0.000 description 1
241000699660 Mus musculus Species 0.000 description 1
OVRNDRQMDRJTHS-CBQIKETKSA-N N-Acetyl-D-Galactosamine Chemical compound CC(=O)N[C@H]1[C@@H](O)O[C@H](CO)[C@H](O)[C@@H]1O OVRNDRQMDRJTHS-CBQIKETKSA-N 0.000 description 1
108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 1
NQTADLQHYWFPDB-UHFFFAOYSA-N N-Hydroxysuccinimide Chemical compound ON1C(=O)CCC1=O NQTADLQHYWFPDB-UHFFFAOYSA-N 0.000 description 1
OVBPIULPVIDEAO-UHFFFAOYSA-N N-Pteroyl-L-glutaminsaeure Natural products C=1N=C2NC(N)=NC(=O)C2=NC=1CNC1=CC=C(C(=O)NC(CCC(O)=O)C(O)=O)C=C1 OVBPIULPVIDEAO-UHFFFAOYSA-N 0.000 description 1
MBLBDJOUHNCFQT-UHFFFAOYSA-N N-acetyl-D-galactosamine Natural products CC(=O)NC(C=O)C(O)C(O)C(O)CO MBLBDJOUHNCFQT-UHFFFAOYSA-N 0.000 description 1
230000004988 N-glycosylation Effects 0.000 description 1
108010025020 Nerve Growth Factor Proteins 0.000 description 1
102000007072 Nerve Growth Factors Human genes 0.000 description 1
102000048238 Neuregulin-1 Human genes 0.000 description 1
206010029260 Neuroblastoma Diseases 0.000 description 1
241000221960 Neurospora Species 0.000 description 1
241000221961 Neurospora crassa Species 0.000 description 1
244000061176 Nicotiana tabacum Species 0.000 description 1
235000002637 Nicotiana tabacum Nutrition 0.000 description 1
239000000020 Nitrocellulose Substances 0.000 description 1
SYNHCENRCUAUNM-UHFFFAOYSA-N Nitrogen mustard N-oxide hydrochloride Chemical compound Cl.ClCC[N+]([O-])(C)CCCl SYNHCENRCUAUNM-UHFFFAOYSA-N 0.000 description 1
KGTDRFCXGRULNK-UHFFFAOYSA-N Nogalamycin Natural products COC1C(OC)(C)C(OC)C(C)OC1OC1C2=C(O)C(C(=O)C3=C(O)C=C4C5(C)OC(C(C(C5O)N(C)C)O)OC4=C3C3=O)=C3C=C2C(C(=O)OC)C(C)(O)C1 KGTDRFCXGRULNK-UHFFFAOYSA-N 0.000 description 1
SMNKEUVRHNWHAI-UHFFFAOYSA-N Officinalisin Natural products O1CC(O)C(O)C2(CO)C(O)C21OCCCC SMNKEUVRHNWHAI-UHFFFAOYSA-N 0.000 description 1
YBRJHZPWOMJYKQ-UHFFFAOYSA-N Oleanolic acid Natural products CC1(C)CC2C3=CCC4C5(C)CCC(O)C(C)(C)C5CCC4(C)C3(C)CCC2(C1)C(=O)O YBRJHZPWOMJYKQ-UHFFFAOYSA-N 0.000 description 1
MIJYXULNPSFWEK-UHFFFAOYSA-N Oleanolinsaeure Natural products C1CC(O)C(C)(C)C2CCC3(C)C4(C)CCC5(C(O)=O)CCC(C)(C)CC5C4=CCC3C21C MIJYXULNPSFWEK-UHFFFAOYSA-N 0.000 description 1
229930187135 Olivomycin Natural products 0.000 description 1
102100021079 Ornithine decarboxylase Human genes 0.000 description 1
108700005126 Ornithine decarboxylases Proteins 0.000 description 1
101100081884 Oryza sativa subsp. japonica OSA15 gene Proteins 0.000 description 1
101150082245 PSAG gene Proteins 0.000 description 1
240000005373 Panax quinquefolius Species 0.000 description 1
235000003140 Panax quinquefolius Nutrition 0.000 description 1
108010067372 Pancreatic elastase Proteins 0.000 description 1
102000016387 Pancreatic elastase Human genes 0.000 description 1
108090000526 Papain Proteins 0.000 description 1
102000003982 Parathyroid hormone Human genes 0.000 description 1
108090000445 Parathyroid hormone Proteins 0.000 description 1
229930182555 Penicillin Natural products 0.000 description 1
108010073038 Penicillin Amidase Proteins 0.000 description 1
JGSARLDLIJGVTE-MBNYWOFBSA-N Penicillin G Chemical compound N([C@H]1[C@H]2SC([C@@H](N2C1=O)C(O)=O)(C)C)C(=O)CC1=CC=CC=C1 JGSARLDLIJGVTE-MBNYWOFBSA-N 0.000 description 1
101710123388 Penicillin G acylase Proteins 0.000 description 1
108010087702 Penicillinase Proteins 0.000 description 1
241000228143 Penicillium Species 0.000 description 1
208000002471 Penile Neoplasms Diseases 0.000 description 1
206010034299 Penile cancer Diseases 0.000 description 1
108090000284 Pepsin A Proteins 0.000 description 1
102000057297 Pepsin A Human genes 0.000 description 1
102000015731 Peptide Hormones Human genes 0.000 description 1
108010038988 Peptide Hormones Proteins 0.000 description 1
240000007377 Petunia x hybrida Species 0.000 description 1
206010057249 Phagocytosis Diseases 0.000 description 1
102000001105 Phosphofructokinases Human genes 0.000 description 1
108010069341 Phosphofructokinases Proteins 0.000 description 1
102000012288 Phosphopyruvate Hydratase Human genes 0.000 description 1
108010022181 Phosphopyruvate Hydratase Proteins 0.000 description 1
108010004729 Phycoerythrin Proteins 0.000 description 1
KMSKQZKKOZQFFG-HSUXVGOQSA-N Pirarubicin Chemical compound O([C@H]1[C@@H](N)C[C@@H](O[C@H]1C)O[C@H]1C[C@@](O)(CC=2C(O)=C3C(=O)C=4C=CC=C(C=4C(=O)C3=C(O)C=21)OC)C(=O)CO)[C@H]1CCCCO1 KMSKQZKKOZQFFG-HSUXVGOQSA-N 0.000 description 1
240000004713 Pisum sativum Species 0.000 description 1
235000010582 Pisum sativum Nutrition 0.000 description 1
108010003044 Placental Lactogen Proteins 0.000 description 1
239000000381 Placental Lactogen Substances 0.000 description 1
229920000805 Polyaspartic acid Polymers 0.000 description 1
241001505332 Polyomavirus sp. Species 0.000 description 1
241000288906 Primates Species 0.000 description 1
108010076181 Proinsulin Proteins 0.000 description 1
102000003946 Prolactin Human genes 0.000 description 1
108010057464 Prolactin Proteins 0.000 description 1
ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
229940124158 Protease/peptidase inhibitor Drugs 0.000 description 1
108010029485 Protein Isoforms Proteins 0.000 description 1
102000001708 Protein Isoforms Human genes 0.000 description 1
241000588769 Proteus <enterobacteria> Species 0.000 description 1
241000589516 Pseudomonas Species 0.000 description 1
241000589517 Pseudomonas aeruginosa Species 0.000 description 1
101100084022 Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) lapA gene Proteins 0.000 description 1
LCTONWCANYUPML-UHFFFAOYSA-M Pyruvate Chemical compound CC(=O)C([O-])=O LCTONWCANYUPML-UHFFFAOYSA-M 0.000 description 1
102000013009 Pyruvate Kinase Human genes 0.000 description 1
108020005115 Pyruvate Kinase Proteins 0.000 description 1
238000002123 RNA extraction Methods 0.000 description 1
239000012979 RPMI medium Substances 0.000 description 1
102000004879 Racemases and epimerases Human genes 0.000 description 1
108090001066 Racemases and epimerases Proteins 0.000 description 1
AHHFEZNOXOZZQA-ZEBDFXRSSA-N Ranimustine Chemical compound CO[C@H]1O[C@H](CNC(=O)N(CCCl)N=O)[C@@H](O)[C@H](O)[C@H]1O AHHFEZNOXOZZQA-ZEBDFXRSSA-N 0.000 description 1
241000700157 Rattus norvegicus Species 0.000 description 1
101100501698 Rattus norvegicus Erbb4 gene Proteins 0.000 description 1
102000004278 Receptor Protein-Tyrosine Kinases Human genes 0.000 description 1
108090000873 Receptor Protein-Tyrosine Kinases Proteins 0.000 description 1
239000006146 Roswell Park Memorial Institute medium Substances 0.000 description 1
229910006124 SOCl2 Inorganic materials 0.000 description 1
241000235070 Saccharomyces Species 0.000 description 1
101100221606 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) COS7 gene Proteins 0.000 description 1
108010084592 Saporins Proteins 0.000 description 1
241000235347 Schizosaccharomyces pombe Species 0.000 description 1
241000311088 Schwanniomyces Species 0.000 description 1
241001123650 Schwanniomyces occidentalis Species 0.000 description 1
229920005654 Sephadex Polymers 0.000 description 1
239000012507 Sephadex™ Substances 0.000 description 1
102100028904 Serine/threonine-protein kinase MARK2 Human genes 0.000 description 1
108010071390 Serum Albumin Proteins 0.000 description 1
102000007562 Serum Albumin Human genes 0.000 description 1
241000607768 Shigella Species 0.000 description 1
241000700584 Simplexvirus Species 0.000 description 1
108020004682 Single-Stranded DNA Proteins 0.000 description 1
206010059516 Skin toxicity Diseases 0.000 description 1
102220497176 Small vasohibin-binding protein_T47D_mutation Human genes 0.000 description 1
VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 1
240000003768 Solanum lycopersicum Species 0.000 description 1
244000061456 Solanum tuberosum Species 0.000 description 1
235000002595 Solanum tuberosum Nutrition 0.000 description 1
241000256248 Spodoptera Species 0.000 description 1
241000256251 Spodoptera frugiperda Species 0.000 description 1
241000862969 Stella Species 0.000 description 1
108010057517 Strep-avidin conjugated horseradish peroxidase Proteins 0.000 description 1
108010090804 Streptavidin Proteins 0.000 description 1
241000187747 Streptomyces Species 0.000 description 1
229930006000 Sucrose Natural products 0.000 description 1
CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 1
108091008874 T cell receptors Proteins 0.000 description 1
102000016266 T-Cell Antigen Receptors Human genes 0.000 description 1
210000001744 T-lymphocyte Anatomy 0.000 description 1
101150006914 TRP1 gene Proteins 0.000 description 1
241000255588 Tephritidae Species 0.000 description 1
239000004098 Tetracycline Substances 0.000 description 1
108090001109 Thermolysin Proteins 0.000 description 1
108091036066 Three prime untranslated region Proteins 0.000 description 1
206010043515 Throat cancer Diseases 0.000 description 1
108010034949 Thyroglobulin Proteins 0.000 description 1
102000009843 Thyroglobulin Human genes 0.000 description 1
241001149964 Tolypocladium Species 0.000 description 1
IWEQQRMGNVVKQW-OQKDUQJOSA-N Toremifene citrate Chemical compound OC(=O)CC(O)(C(O)=O)CC(O)=O.C1=CC(OCCN(C)C)=CC=C1C(\C=1C=CC=CC=1)=C(\CCCl)C1=CC=CC=C1 IWEQQRMGNVVKQW-OQKDUQJOSA-N 0.000 description 1
101710120037 Toxin CcdB Proteins 0.000 description 1
102000004338 Transferrin Human genes 0.000 description 1
108090000901 Transferrin Proteins 0.000 description 1
102000006747 Transforming Growth Factor alpha Human genes 0.000 description 1
HDTRYLNUVZCQOY-WSWWMNSNSA-N Trehalose Natural products O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@H](O)[C@@H](O)[C@@H](O)[C@@H](CO)O1 HDTRYLNUVZCQOY-WSWWMNSNSA-N 0.000 description 1
241000223259 Trichoderma Species 0.000 description 1
UMILHIMHKXVDGH-UHFFFAOYSA-N Triethylene glycol diglycidyl ether Chemical compound C1OC1COCCOCCOCCOCC1CO1 UMILHIMHKXVDGH-UHFFFAOYSA-N 0.000 description 1
102000005924 Triose-Phosphate Isomerase Human genes 0.000 description 1
108700015934 Triose-phosphate isomerases Proteins 0.000 description 1
FYAMXEPQQLNQDM-UHFFFAOYSA-N Tris(1-aziridinyl)phosphine oxide Chemical compound C1CN1P(N1CC1)(=O)N1CC1 FYAMXEPQQLNQDM-UHFFFAOYSA-N 0.000 description 1
235000021307 Triticum Nutrition 0.000 description 1
244000098338 Triticum aestivum Species 0.000 description 1
LVTKHGUGBGNBPL-UHFFFAOYSA-N Trp-P-1 Chemical compound N1C2=CC=CC=C2C2=C1C(C)=C(N)N=C2C LVTKHGUGBGNBPL-UHFFFAOYSA-N 0.000 description 1
GLNADSQYFUSGOU-GPTZEZBUSA-J Trypan blue Chemical compound [Na+].[Na+].[Na+].[Na+].C1=C(S([O-])(=O)=O)C=C2C=C(S([O-])(=O)=O)C(/N=N/C3=CC=C(C=C3C)C=3C=C(C(=CC=3)\N=N\C=3C(=CC4=CC(=CC(N)=C4C=3O)S([O-])(=O)=O)S([O-])(=O)=O)C)=C(O)C2=C1N GLNADSQYFUSGOU-GPTZEZBUSA-J 0.000 description 1
108090000631 Trypsin Proteins 0.000 description 1
102000004142 Trypsin Human genes 0.000 description 1
229940122618 Trypsin inhibitor Drugs 0.000 description 1
101710162629 Trypsin inhibitor Proteins 0.000 description 1
206010054094 Tumour necrosis Diseases 0.000 description 1
206010053613 Type IV hypersensitivity reaction Diseases 0.000 description 1
108010092464 Urate Oxidase Proteins 0.000 description 1
108010046334 Urease Proteins 0.000 description 1
101150117115 V gene Proteins 0.000 description 1
244000000188 Vaccinium ovalifolium Species 0.000 description 1
240000001866 Vernicia fordii Species 0.000 description 1
229940122803 Vinca alkaloid Drugs 0.000 description 1
108020005202 Viral DNA Proteins 0.000 description 1
229930003268 Vitamin C Natural products 0.000 description 1
229930003427 Vitamin E Natural products 0.000 description 1
IXKSXJFAGXLQOQ-XISFHERQSA-N WHWLQLKPGQPMY Chemical group C([C@@H](C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N1CCC[C@H]1C(=O)NCC(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(O)=O)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(O)=O)NC(=O)[C@@H](N)CC=1C2=CC=CC=C2NC=1)C1=CNC=N1 IXKSXJFAGXLQOQ-XISFHERQSA-N 0.000 description 1
241000714205 Woolly monkey sarcoma virus Species 0.000 description 1
102100033220 Xanthine oxidase Human genes 0.000 description 1
108010093894 Xanthine oxidase Proteins 0.000 description 1
241000235013 Yarrowia Species 0.000 description 1
240000008042 Zea mays Species 0.000 description 1
235000016383 Zea mays subsp huehuetenangensis Nutrition 0.000 description 1
235000002017 Zea mays subsp mays Nutrition 0.000 description 1
ZYVSOIYQKUDENJ-ASUJBHBQSA-N [(2R,3R,4R,6R)-6-[[(6S,7S)-6-[(2S,4R,5R,6R)-4-[(2R,4R,5R,6R)-4-[(2S,4S,5S,6S)-5-acetyloxy-4-hydroxy-4,6-dimethyloxan-2-yl]oxy-5-hydroxy-6-methyloxan-2-yl]oxy-5-hydroxy-6-methyloxan-2-yl]oxy-7-[(3S,4R)-3,4-dihydroxy-1-methoxy-2-oxopentyl]-4,10-dihydroxy-3-methyl-5-oxo-7,8-dihydro-6H-anthracen-2-yl]oxy]-4-[(2R,4R,5R,6R)-4-hydroxy-5-methoxy-6-methyloxan-2-yl]oxy-2-methyloxan-3-yl] acetate Chemical class COC([C@@H]1Cc2cc3cc(O[C@@H]4C[C@@H](O[C@@H]5C[C@@H](O)[C@@H](OC)[C@@H](C)O5)[C@H](OC(C)=O)[C@@H](C)O4)c(C)c(O)c3c(O)c2C(=O)[C@H]1O[C@H]1C[C@@H](O[C@@H]2C[C@@H](O[C@H]3C[C@](C)(O)[C@@H](OC(C)=O)[C@H](C)O3)[C@H](O)[C@@H](C)O2)[C@H](O)[C@@H](C)O1)C(=O)[C@@H](O)[C@@H](C)O ZYVSOIYQKUDENJ-ASUJBHBQSA-N 0.000 description 1
SPJCRMJCFSJKDE-ZWBUGVOYSA-N [(3s,8s,9s,10r,13r,14s,17r)-10,13-dimethyl-17-[(2r)-6-methylheptan-2-yl]-2,3,4,7,8,9,11,12,14,15,16,17-dodecahydro-1h-cyclopenta[a]phenanthren-3-yl] 2-[4-[bis(2-chloroethyl)amino]phenyl]acetate Chemical compound O([C@@H]1CC2=CC[C@H]3[C@@H]4CC[C@@H]([C@]4(CC[C@@H]3[C@@]2(C)CC1)C)[C@H](C)CCCC(C)C)C(=O)CC1=CC=C(N(CCCl)CCCl)C=C1 SPJCRMJCFSJKDE-ZWBUGVOYSA-N 0.000 description 1
HIHOWBSBBDRPDW-PTHRTHQKSA-N [(3s,8s,9s,10r,13r,14s,17r)-10,13-dimethyl-17-[(2r)-6-methylheptan-2-yl]-2,3,4,7,8,9,11,12,14,15,16,17-dodecahydro-1h-cyclopenta[a]phenanthren-3-yl] n-[2-(dimethylamino)ethyl]carbamate Chemical compound C1C=C2C[C@@H](OC(=O)NCCN(C)C)CC[C@]2(C)[C@@H]2[C@@H]1[C@@H]1CC[C@H]([C@H](C)CCCC(C)C)[C@@]1(C)CC2 HIHOWBSBBDRPDW-PTHRTHQKSA-N 0.000 description 1
IFJUINDAXYAPTO-UUBSBJJBSA-N [(8r,9s,13s,14s,17s)-17-[2-[4-[4-[bis(2-chloroethyl)amino]phenyl]butanoyloxy]acetyl]oxy-13-methyl-6,7,8,9,11,12,14,15,16,17-decahydrocyclopenta[a]phenanthren-3-yl] benzoate Chemical compound C([C@@H]1[C@@H](C2=CC=3)CC[C@]4([C@H]1CC[C@@H]4OC(=O)COC(=O)CCCC=1C=CC(=CC=1)N(CCCl)CCCl)C)CC2=CC=3OC(=O)C1=CC=CC=C1 IFJUINDAXYAPTO-UUBSBJJBSA-N 0.000 description 1
IHGLINDYFMDHJG-UHFFFAOYSA-N [2-(4-methoxyphenyl)-3,4-dihydronaphthalen-1-yl]-[4-(2-pyrrolidin-1-ylethoxy)phenyl]methanone Chemical compound C1=CC(OC)=CC=C1C(CCC1=CC=CC=C11)=C1C(=O)C(C=C1)=CC=C1OCCN1CCCC1 IHGLINDYFMDHJG-UHFFFAOYSA-N 0.000 description 1
XZSRRNFBEIOBDA-CFNBKWCHSA-N [2-[(2s,4s)-4-[(2r,4s,5s,6s)-4-amino-5-hydroxy-6-methyloxan-2-yl]oxy-2,5,12-trihydroxy-7-methoxy-6,11-dioxo-3,4-dihydro-1h-tetracen-2-yl]-2-oxoethyl] 2,2-diethoxyacetate Chemical compound O([C@H]1C[C@](CC2=C(O)C=3C(=O)C4=CC=CC(OC)=C4C(=O)C=3C(O)=C21)(O)C(=O)COC(=O)C(OCC)OCC)[C@H]1C[C@H](N)[C@H](O)[C@H](C)O1 XZSRRNFBEIOBDA-CFNBKWCHSA-N 0.000 description 1
JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 1
238000009825 accumulation Methods 0.000 description 1
ZOZKYEHVNDEUCO-XUTVFYLZSA-N aceglatone Chemical compound O1C(=O)[C@H](OC(C)=O)[C@@H]2OC(=O)[C@@H](OC(=O)C)[C@@H]21 ZOZKYEHVNDEUCO-XUTVFYLZSA-N 0.000 description 1
229950002684 aceglatone Drugs 0.000 description 1
230000002378 acidificating effect Effects 0.000 description 1
229930188522 aclacinomycin Natural products 0.000 description 1
LJZPVWKMAYDYAS-QKKPTTNWSA-N aclacinomycin T Chemical class O([C@H]1C[C@]([C@@H](C2=CC=3C(=O)C4=CC=CC(O)=C4C(=O)C=3C(O)=C21)C(=O)OC)(O)CC)[C@H]1C[C@H](N(C)C)[C@H](O)[C@H](C)O1 LJZPVWKMAYDYAS-QKKPTTNWSA-N 0.000 description 1
229930183665 actinomycin Natural products 0.000 description 1
RJURFGZVJUQBHK-IIXSONLDSA-N actinomycin D Chemical compound C[C@H]1OC(=O)[C@H](C(C)C)N(C)C(=O)CN(C)C(=O)[C@@H]2CCCN2C(=O)[C@@H](C(C)C)NC(=O)[C@H]1NC(=O)C1=C(N)C(=O)C(C)=C2OC(C(C)=CC=C3C(=O)N[C@@H]4C(=O)N[C@@H](C(N5CCC[C@H]5C(=O)N(C)CC(=O)N(C)[C@@H](C(C)C)C(=O)O[C@@H]4C)=O)C(C)C)=C3N=C21 RJURFGZVJUQBHK-IIXSONLDSA-N 0.000 description 1
239000004480 active ingredient Substances 0.000 description 1
239000000488 activin Substances 0.000 description 1
239000000654 additive Substances 0.000 description 1
229960005305 adenosine Drugs 0.000 description 1
238000011360 adjunctive therapy Methods 0.000 description 1
230000004931 aggregating effect Effects 0.000 description 1
230000002776 aggregation Effects 0.000 description 1
238000004220 aggregation Methods 0.000 description 1
238000003349 alamar blue assay Methods 0.000 description 1
150000001299 aldehydes Chemical class 0.000 description 1
125000000217 alkyl group Chemical group 0.000 description 1
229940045714 alkyl sulfonate alkylating agent Drugs 0.000 description 1
150000008052 alkyl sulfonates Chemical class 0.000 description 1
229940100198 alkylating agent Drugs 0.000 description 1
239000002168 alkylating agent Substances 0.000 description 1
SHGAZHPCJJPHSC-YCNIQYBTSA-N all-trans-retinoic acid Chemical compound OC(=O)\C=C(/C)\C=C\C=C(/C)\C=C\C1=C(C)CCCC1(C)C SHGAZHPCJJPHSC-YCNIQYBTSA-N 0.000 description 1
HDTRYLNUVZCQOY-LIZSDCNHSA-N alpha,alpha-trehalose Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 HDTRYLNUVZCQOY-LIZSDCNHSA-N 0.000 description 1
WQZGKKKJIJFFOK-PHYPRBDBSA-N alpha-D-galactose Chemical compound OC[C@H]1O[C@H](O)[C@H](O)[C@@H](O)[C@H]1O WQZGKKKJIJFFOK-PHYPRBDBSA-N 0.000 description 1
108010026331 alpha-Fetoproteins Proteins 0.000 description 1
108010001818 alpha-sarcin Proteins 0.000 description 1
230000004075 alteration Effects 0.000 description 1
229960000473 altretamine Drugs 0.000 description 1
229940037003 alum Drugs 0.000 description 1
150000001412 amines Chemical class 0.000 description 1
229960003437 aminoglutethimide Drugs 0.000 description 1
ROBVIMPUHSLWNV-UHFFFAOYSA-N aminoglutethimide Chemical compound C=1C=C(N)C=CC=1C1(CC)CCC(=O)NC1=O ROBVIMPUHSLWNV-UHFFFAOYSA-N 0.000 description 1
229940126574 aminoglycoside antibiotic Drugs 0.000 description 1
239000002647 aminoglycoside antibiotic agent Substances 0.000 description 1
229960002749 aminolevulinic acid Drugs 0.000 description 1
238000012870 ammonium sulfate precipitation Methods 0.000 description 1
229960000723 ampicillin Drugs 0.000 description 1
AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 1
BBDAGFIXKZCXAH-CCXZUQQUSA-N ancitabine Chemical compound N=C1C=CN2[C@@H]3O[C@H](CO)[C@@H](O)[C@@H]3OC2=N1 BBDAGFIXKZCXAH-CCXZUQQUSA-N 0.000 description 1
229950000242 ancitabine Drugs 0.000 description 1
229940030486 androgens Drugs 0.000 description 1
239000002870 angiogenesis inducing agent Substances 0.000 description 1
238000010171 animal model Methods 0.000 description 1
239000003957 anion exchange resin Substances 0.000 description 1
150000001450 anions Chemical class 0.000 description 1
239000005557 antagonist Substances 0.000 description 1
230000009949 anti-apoptotic pathway Effects 0.000 description 1
230000001093 anti-cancer Effects 0.000 description 1
230000000340 anti-metabolite Effects 0.000 description 1
229940030495 antiandrogen sex hormone and modulator of the genital system Drugs 0.000 description 1
238000011091 antibody purification Methods 0.000 description 1
210000000628 antibody-producing cell Anatomy 0.000 description 1
238000011319 anticancer therapy Methods 0.000 description 1
239000003524 antilipemic agent Substances 0.000 description 1
229940100197 antimetabolite Drugs 0.000 description 1
239000002256 antimetabolite Substances 0.000 description 1
229940045687 antimetabolites folic acid analogs Drugs 0.000 description 1
229940045713 antineoplastic alkylating drug ethylene imines Drugs 0.000 description 1
230000003078 antioxidant effect Effects 0.000 description 1
239000003418 antiprogestin Substances 0.000 description 1
238000003782 apoptosis assay Methods 0.000 description 1
229960004405 aprotinin Drugs 0.000 description 1
PYMYPHUHKUWMLA-UHFFFAOYSA-N arabinose Natural products OCC(O)C(O)C(O)C=O PYMYPHUHKUWMLA-UHFFFAOYSA-N 0.000 description 1
150000008209 arabinosides Chemical class 0.000 description 1
ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
125000003118 aryl group Chemical group 0.000 description 1
235000009582 asparagine Nutrition 0.000 description 1
229960001230 asparagine Drugs 0.000 description 1
125000000613 asparagine group Chemical group N[C@@H](CC(N)=O)C(=O)* 0.000 description 1
235000003704 aspartic acid Nutrition 0.000 description 1
238000011717 athymic nude mouse Methods 0.000 description 1
238000013475 authorization Methods 0.000 description 1
238000000376 autoradiography Methods 0.000 description 1
229960002756 azacitidine Drugs 0.000 description 1
150000001541 aziridines Chemical class 0.000 description 1
229960000686 benzalkonium chloride Drugs 0.000 description 1
229960001950 benzethonium chloride Drugs 0.000 description 1
UREZNYTWGJKWBI-UHFFFAOYSA-M benzethonium chloride Chemical compound [Cl-].C1=CC(C(C)(C)CC(C)(C)C)=CC=C1OCCOCC[N+](C)(C)CC1=CC=CC=C1 UREZNYTWGJKWBI-UHFFFAOYSA-M 0.000 description 1
CADWTSSKOVRVJC-UHFFFAOYSA-N benzyl(dimethyl)azanium;chloride Chemical compound [Cl-].C[NH+](C)CC1=CC=CC=C1 CADWTSSKOVRVJC-UHFFFAOYSA-N 0.000 description 1
SRBFZHDQGSBBOR-UHFFFAOYSA-N beta-D-Pyranose-Lyxose Natural products OC1COC(O)C(O)C1O SRBFZHDQGSBBOR-UHFFFAOYSA-N 0.000 description 1
WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 1
108010051210 beta-Fructofuranosidase Proteins 0.000 description 1
OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 description 1
229960000997 bicalutamide Drugs 0.000 description 1
238000002306 biochemical method Methods 0.000 description 1
239000013060 biological fluid Substances 0.000 description 1
238000005460 biophysical method Methods 0.000 description 1
210000003443 bladder cell Anatomy 0.000 description 1
201000000053 blastoma Diseases 0.000 description 1
229960001561 bleomycin Drugs 0.000 description 1
230000036772 blood pressure Effects 0.000 description 1
210000004204 blood vessel Anatomy 0.000 description 1
230000036760 body temperature Effects 0.000 description 1
230000037396 body weight Effects 0.000 description 1
238000009835 boiling Methods 0.000 description 1
238000006664 bond formation reaction Methods 0.000 description 1
229960002092 busulfan Drugs 0.000 description 1
DQXBYHZEEUGOBF-UHFFFAOYSA-N but-3-enoic acid;ethene Chemical compound C=C.OC(=O)CC=C DQXBYHZEEUGOBF-UHFFFAOYSA-N 0.000 description 1
LRHPLDYGYMQRHN-UHFFFAOYSA-N butyl alcohol Substances CCCCO LRHPLDYGYMQRHN-UHFFFAOYSA-N 0.000 description 1
125000000484 butyl group Chemical group [H]C([*])([H])C([H])([H])C([H])([H])C([H])([H])[H] 0.000 description 1
108700002839 cactinomycin Proteins 0.000 description 1
229950009908 cactinomycin Drugs 0.000 description 1
229910052791 calcium Inorganic materials 0.000 description 1
239000001110 calcium chloride Substances 0.000 description 1
235000011148 calcium chloride Nutrition 0.000 description 1
229910001628 calcium chloride Inorganic materials 0.000 description 1
239000001506 calcium phosphate Substances 0.000 description 1
229910000389 calcium phosphate Inorganic materials 0.000 description 1
235000011010 calcium phosphates Nutrition 0.000 description 1
244000309466 calf Species 0.000 description 1
IVFYLRMMHVYGJH-PVPPCFLZSA-N calusterone Chemical compound C1C[C@]2(C)[C@](O)(C)CC[C@H]2[C@@H]2[C@@H](C)CC3=CC(=O)CC[C@]3(C)[C@H]21 IVFYLRMMHVYGJH-PVPPCFLZSA-N 0.000 description 1
229950009823 calusterone Drugs 0.000 description 1
230000036952 cancer formation Effects 0.000 description 1
229960004117 capecitabine Drugs 0.000 description 1
235000014633 carbohydrates Nutrition 0.000 description 1
229960002115 carboquone Drugs 0.000 description 1
231100000504 carcinogenesis Toxicity 0.000 description 1
230000001451 cardiotoxic effect Effects 0.000 description 1
229960005243 carmustine Drugs 0.000 description 1
239000000969 carrier Substances 0.000 description 1
108010047060 carzinophilin Proteins 0.000 description 1
238000012219 cassette mutagenesis Methods 0.000 description 1
239000003729 cation exchange resin Substances 0.000 description 1
230000006369 cell cycle progression Effects 0.000 description 1
238000010822 cell death assay Methods 0.000 description 1
230000024245 cell differentiation Effects 0.000 description 1
230000007910 cell fusion Effects 0.000 description 1
230000022534 cell killing Effects 0.000 description 1
210000000170 cell membrane Anatomy 0.000 description 1
230000015861 cell surface binding Effects 0.000 description 1
230000005890 cell-mediated cytotoxicity Effects 0.000 description 1
230000002032 cellular defenses Effects 0.000 description 1
230000030570 cellular localization Effects 0.000 description 1
230000036755 cellular response Effects 0.000 description 1
230000004700 cellular uptake Effects 0.000 description 1
238000012512 characterization method Methods 0.000 description 1
238000012412 chemical coupling Methods 0.000 description 1
239000007795 chemical reaction product Substances 0.000 description 1
CRQQGFGUEAVUIL-UHFFFAOYSA-N chlorothalonil Chemical compound ClC1=C(Cl)C(C#N)=C(Cl)C(C#N)=C1Cl CRQQGFGUEAVUIL-UHFFFAOYSA-N 0.000 description 1
235000012000 cholesterol Nutrition 0.000 description 1
230000010428 chromatin condensation Effects 0.000 description 1
239000013611 chromosomal DNA Substances 0.000 description 1
230000002759 chromosomal effect Effects 0.000 description 1
230000001684 chronic effect Effects 0.000 description 1
229940080701 chymosin Drugs 0.000 description 1
239000012459 cleaning agent Substances 0.000 description 1
238000003776 cleavage reaction Methods 0.000 description 1
230000004186 co-expression Effects 0.000 description 1
238000000749 co-immunoprecipitation Methods 0.000 description 1
238000011490 co-immunoprecipitation assay Methods 0.000 description 1
230000001149 cognitive effect Effects 0.000 description 1
229940047120 colony stimulating factors Drugs 0.000 description 1
238000002648 combination therapy Methods 0.000 description 1
230000001447 compensatory effect Effects 0.000 description 1
230000002860 competitive effect Effects 0.000 description 1
230000004154 complement system Effects 0.000 description 1
230000009918 complex formation Effects 0.000 description 1
239000008139 complexing agent Substances 0.000 description 1
239000005289 controlled pore glass Substances 0.000 description 1
239000007822 coupling agent Substances 0.000 description 1
238000002425 crystallisation Methods 0.000 description 1
230000008025 crystallization Effects 0.000 description 1
210000004748 cultured cell Anatomy 0.000 description 1
HPXRVTGHNJAIIH-UHFFFAOYSA-N cyclohexanol Chemical compound OC1CCCCC1 HPXRVTGHNJAIIH-UHFFFAOYSA-N 0.000 description 1
229960000978 cyproterone acetate Drugs 0.000 description 1
UWFYSQMTEOIJJG-FDTZYFLXSA-N cyproterone acetate Chemical compound C1=C(Cl)C2=CC(=O)[C@@H]3C[C@@H]3[C@]2(C)[C@@H]2[C@@H]1[C@@H]1CC[C@@](C(C)=O)(OC(=O)C)[C@@]1(C)CC2 UWFYSQMTEOIJJG-FDTZYFLXSA-N 0.000 description 1
UFULAYFCSOUIOV-UHFFFAOYSA-N cysteamine Chemical compound NCCS UFULAYFCSOUIOV-UHFFFAOYSA-N 0.000 description 1
XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
229960000684 cytarabine Drugs 0.000 description 1
108010057085 cytokine receptors Proteins 0.000 description 1
102000003675 cytokine receptors Human genes 0.000 description 1
239000000824 cytostatic agent Substances 0.000 description 1
230000001085 cytostatic effect Effects 0.000 description 1
210000001151 cytotoxic T lymphocyte Anatomy 0.000 description 1
229960003901 dacarbazine Drugs 0.000 description 1
229960000640 dactinomycin Drugs 0.000 description 1
125000001295 dansyl group Chemical group [H]C1=C([H])C(N(C([H])([H])[H])C([H])([H])[H])=C2C([H])=C([H])C([H])=C(C2=C1[H])S(*)(=O)=O 0.000 description 1
230000003247 decreasing effect Effects 0.000 description 1
230000007812 deficiency Effects 0.000 description 1
230000000593 degrading effect Effects 0.000 description 1
YSMODUONRAFBET-UHFFFAOYSA-N delta-DL-hydroxylysine Natural products NCC(O)CCC(N)C(O)=O YSMODUONRAFBET-UHFFFAOYSA-N 0.000 description 1
238000001514 detection method Methods 0.000 description 1
239000003599 detergent Substances 0.000 description 1
229950003913 detorubicin Drugs 0.000 description 1
229960000605 dexrazoxane Drugs 0.000 description 1
235000019425 dextrin Nutrition 0.000 description 1
238000010586 diagram Methods 0.000 description 1
229930191339 dianthin Natural products 0.000 description 1
WVYXNIXAMZOZFK-UHFFFAOYSA-N diaziquone Chemical compound O=C1C(NC(=O)OCC)=C(N2CC2)C(=O)C(NC(=O)OCC)=C1N1CC1 WVYXNIXAMZOZFK-UHFFFAOYSA-N 0.000 description 1
229950002389 diaziquone Drugs 0.000 description 1
238000002022 differential scanning fluorescence spectroscopy Methods 0.000 description 1
125000005442 diisocyanate group Chemical group 0.000 description 1
238000006471 dimerization reaction Methods 0.000 description 1
206010013023 diphtheria Diseases 0.000 description 1
150000002016 disaccharides Chemical class 0.000 description 1
238000004090 dissolution Methods 0.000 description 1
ZWIBGKZDAWNIFC-UHFFFAOYSA-N disuccinimidyl suberate Chemical compound O=C1CCC(=O)N1OC(=O)CCCCCCC(=O)ON1C(=O)CCC1=O ZWIBGKZDAWNIFC-UHFFFAOYSA-N 0.000 description 1
239000003534 dna topoisomerase inhibitor Substances 0.000 description 1
230000003828 downregulation Effects 0.000 description 1
ZWAOHEXOSAUJHY-ZIYNGMLESA-N doxifluridine Chemical compound O[C@@H]1[C@H](O)[C@@H](C)O[C@H]1N1C(=O)NC(=O)C(F)=C1 ZWAOHEXOSAUJHY-ZIYNGMLESA-N 0.000 description 1
229950005454 doxifluridine Drugs 0.000 description 1
NOTIQUSPUUHHEH-UXOVVSIBSA-N dromostanolone propionate Chemical compound C([C@@H]1CC2)C(=O)[C@H](C)C[C@]1(C)[C@@H]1[C@@H]2[C@@H]2CC[C@H](OC(=O)CC)[C@@]2(C)CC1 NOTIQUSPUUHHEH-UXOVVSIBSA-N 0.000 description 1
229950004683 drostanolone propionate Drugs 0.000 description 1
238000009510 drug design Methods 0.000 description 1
239000000975 dye Substances 0.000 description 1
229960002759 eflornithine Drugs 0.000 description 1
238000004520 electroporation Methods 0.000 description 1
239000012149 elution buffer Substances 0.000 description 1
201000008184 embryoma Diseases 0.000 description 1
230000012202 endocytosis Effects 0.000 description 1
201000003914 endometrial carcinoma Diseases 0.000 description 1
210000004696 endometrium Anatomy 0.000 description 1
210000002472 endoplasmic reticulum Anatomy 0.000 description 1
230000003511 endothelial effect Effects 0.000 description 1
229950011487 enocitabine Drugs 0.000 description 1
108010028531 enomycin Proteins 0.000 description 1
210000002919 epithelial cell Anatomy 0.000 description 1
229950002973 epitiostanol Drugs 0.000 description 1
YSMODUONRAFBET-UHNVWZDZSA-N erythro-5-hydroxy-L-lysine Chemical compound NC[C@H](O)CC[C@H](N)C(O)=O YSMODUONRAFBET-UHNVWZDZSA-N 0.000 description 1
229950002017 esorubicin Drugs 0.000 description 1
ITSGNOIFAJAQHJ-BMFNZSJVSA-N esorubicin Chemical compound O([C@H]1C[C@@](O)(CC=2C(O)=C3C(=O)C=4C=CC=C(C=4C(=O)C3=C(O)C=21)OC)C(=O)CO)[C@H]1C[C@H](N)C[C@H](C)O1 ITSGNOIFAJAQHJ-BMFNZSJVSA-N 0.000 description 1
102000015694 estrogen receptors Human genes 0.000 description 1
108010038795 estrogen receptors Proteins 0.000 description 1
238000012869 ethanol precipitation Methods 0.000 description 1
RTZKZFJDLAIYFH-UHFFFAOYSA-N ether Substances CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 1
239000005038 ethylene vinyl acetate Substances 0.000 description 1
229960005237 etoglucid Drugs 0.000 description 1
VJJPUSNTGOMMGY-MRVIYFEKSA-N etoposide Chemical compound COC1=C(O)C(OC)=CC([C@@H]2C3=CC=4OCOC=4C=C3[C@@H](O[C@H]3[C@@H]([C@@H](O)[C@@H]4O[C@H](C)OC[C@H]4O3)O)[C@@H]3[C@@H]2C(OC3)=O)=C1 VJJPUSNTGOMMGY-MRVIYFEKSA-N 0.000 description 1
OGPBJKLSAFTDLK-UHFFFAOYSA-N europium atom Chemical compound [Eu] OGPBJKLSAFTDLK-UHFFFAOYSA-N 0.000 description 1
238000001704 evaporation Methods 0.000 description 1
229940043168 fareston Drugs 0.000 description 1
210000003754 fetus Anatomy 0.000 description 1
239000000835 fiber Substances 0.000 description 1
229940126864 fibroblast growth factor Drugs 0.000 description 1
229960000390 fludarabine Drugs 0.000 description 1
GIUYCYHIANZCFB-FJFJXFQQSA-N fludarabine phosphate Chemical compound C1=NC=2C(N)=NC(F)=NC=2N1[C@@H]1O[C@H](COP(O)(O)=O)[C@@H](O)[C@@H]1O GIUYCYHIANZCFB-FJFJXFQQSA-N 0.000 description 1
239000012530 fluid Substances 0.000 description 1
GNBHRKFJIUUOQI-UHFFFAOYSA-N fluorescein Chemical compound O1C(=O)C2=CC=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 GNBHRKFJIUUOQI-UHFFFAOYSA-N 0.000 description 1
239000007850 fluorescent dye Substances 0.000 description 1
150000002222 fluorine compounds Chemical class 0.000 description 1
235000019152 folic acid Nutrition 0.000 description 1
239000011724 folic acid Substances 0.000 description 1
229960000304 folic acid Drugs 0.000 description 1
150000002224 folic acids Chemical class 0.000 description 1
230000037406 food intake Effects 0.000 description 1
235000012631 food intake Nutrition 0.000 description 1
229960004783 fotemustine Drugs 0.000 description 1
YAKWPXVTIGTRJH-UHFFFAOYSA-N fotemustine Chemical compound CCOP(=O)(OCC)C(C)NC(=O)N(CCCl)N=O YAKWPXVTIGTRJH-UHFFFAOYSA-N 0.000 description 1
238000005194 fractionation Methods 0.000 description 1
229910052733 gallium Inorganic materials 0.000 description 1
WIGCFUFOHFEKBI-UHFFFAOYSA-N gamma-tocopherol Natural products CC(C)CCCC(C)CCCC(C)CCCC1CCC2C(C)C(O)C(C)C(C)C2O1 WIGCFUFOHFEKBI-UHFFFAOYSA-N 0.000 description 1
238000003500 gene array Methods 0.000 description 1
BRZYSWJRSDMWLG-CAXSIQPQSA-N geneticin Natural products O1C[C@@](O)(C)[C@H](NC)[C@@H](O)[C@H]1O[C@@H]1[C@@H](O)[C@H](O[C@@H]2[C@@H]([C@@H](O)[C@H](O)[C@@H](C(C)O)O2)N)[C@@H](N)C[C@H]1N BRZYSWJRSDMWLG-CAXSIQPQSA-N 0.000 description 1
239000011521 glass Substances 0.000 description 1
102000018146 globin Human genes 0.000 description 1
108060003196 globin Proteins 0.000 description 1
229940116332 glucose oxidase Drugs 0.000 description 1
235000019420 glucose oxidase Nutrition 0.000 description 1
235000013922 glutamic acid Nutrition 0.000 description 1
239000004220 glutamic acid Substances 0.000 description 1
230000002414 glycolytic effect Effects 0.000 description 1
229930182470 glycoside Natural products 0.000 description 1
239000002622 gonadotropin Substances 0.000 description 1
229960002913 goserelin Drugs 0.000 description 1
210000003714 granulocyte Anatomy 0.000 description 1
239000000122 growth hormone Substances 0.000 description 1
230000009036 growth inhibition Effects 0.000 description 1
229940093915 gynecological organic acid Drugs 0.000 description 1
210000003128 head Anatomy 0.000 description 1
108010067006 heat stable toxin (E coli) Proteins 0.000 description 1
210000003958 hematopoietic stem cell Anatomy 0.000 description 1
229960002897 heparin Drugs 0.000 description 1
229920000669 heparin Polymers 0.000 description 1
229940022353 herceptin Drugs 0.000 description 1
125000000623 heterocyclic group Chemical group 0.000 description 1
238000005734 heterodimerization reaction Methods 0.000 description 1
UUVWYPNAQBNQJQ-UHFFFAOYSA-N hexamethylmelamine Chemical compound CN(C)C1=NC(N(C)C)=NC(N(C)C)=N1 UUVWYPNAQBNQJQ-UHFFFAOYSA-N 0.000 description 1
HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 1
238000001794 hormone therapy Methods 0.000 description 1
208000033519 human immunodeficiency virus infectious disease Diseases 0.000 description 1
229960000890 hydrocortisone Drugs 0.000 description 1
239000000017 hydrogel Substances 0.000 description 1
229920001477 hydrophilic polymer Polymers 0.000 description 1
230000002209 hydrophobic effect Effects 0.000 description 1
238000004191 hydrophobic interaction chromatography Methods 0.000 description 1
229920001600 hydrophobic polymer Polymers 0.000 description 1
125000002349 hydroxyamino group Chemical group [H]ON([H])[*] 0.000 description 1
229960001330 hydroxycarbamide Drugs 0.000 description 1
230000002267 hypothalamic effect Effects 0.000 description 1
229940015872 ibandronate Drugs 0.000 description 1
229960000908 idarubicin Drugs 0.000 description 1
229960001101 ifosfamide Drugs 0.000 description 1
HOMGKSMUEGBAAB-UHFFFAOYSA-N ifosfamide Chemical compound ClCCNP1(=O)OCCCN1CCCl HOMGKSMUEGBAAB-UHFFFAOYSA-N 0.000 description 1
150000002463 imidates Chemical class 0.000 description 1
230000014726 immortalization of host cell Effects 0.000 description 1
230000028993 immune response Effects 0.000 description 1
210000000987 immune system Anatomy 0.000 description 1
238000003018 immunoassay Methods 0.000 description 1
230000002055 immunohistochemical effect Effects 0.000 description 1
238000003364 immunohistochemistry Methods 0.000 description 1
238000013388 immunohistochemistry analysis Methods 0.000 description 1
239000012133 immunoprecipitate Substances 0.000 description 1
230000002637 immunotoxin Effects 0.000 description 1
229940051026 immunotoxin Drugs 0.000 description 1
239000002596 immunotoxin Substances 0.000 description 1
231100000608 immunotoxin Toxicity 0.000 description 1
230000008676 import Effects 0.000 description 1
DBIGHPPNXATHOF-UHFFFAOYSA-N improsulfan Chemical compound CS(=O)(=O)OCCCNCCCOS(C)(=O)=O DBIGHPPNXATHOF-UHFFFAOYSA-N 0.000 description 1
229950008097 improsulfan Drugs 0.000 description 1
238000007901 in situ hybridization Methods 0.000 description 1
238000011065 in-situ storage Methods 0.000 description 1
230000008595 infiltration Effects 0.000 description 1
238000001764 infiltration Methods 0.000 description 1
239000000893 inhibin Substances 0.000 description 1
230000000977 initiatory effect Effects 0.000 description 1
150000002484 inorganic compounds Chemical class 0.000 description 1
229910010272 inorganic material Inorganic materials 0.000 description 1
238000007689 inspection Methods 0.000 description 1
102000006495 integrins Human genes 0.000 description 1
108010044426 integrins Proteins 0.000 description 1
230000002452 interceptive effect Effects 0.000 description 1
229940047124 interferons Drugs 0.000 description 1
229940047122 interleukins Drugs 0.000 description 1
201000002313 intestinal cancer Diseases 0.000 description 1
230000004068 intracellular signaling Effects 0.000 description 1
238000007918 intramuscular administration Methods 0.000 description 1
238000007919 intrasynovial administration Methods 0.000 description 1
238000007913 intrathecal administration Methods 0.000 description 1
238000010253 intravenous injection Methods 0.000 description 1
239000001573 invertase Substances 0.000 description 1
235000011073 invertase Nutrition 0.000 description 1
238000005342 ion exchange Methods 0.000 description 1
239000000797 iron chelating agent Substances 0.000 description 1
229940075525 iron chelating agent Drugs 0.000 description 1
229930027917 kanamycin Natural products 0.000 description 1
229960000318 kanamycin Drugs 0.000 description 1
SBUJHOSQTJFQJX-NOAMYHISSA-N kanamycin Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CN)O[C@@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](N)[C@H](O)[C@@H](CO)O2)O)[C@H](N)C[C@@H]1N SBUJHOSQTJFQJX-NOAMYHISSA-N 0.000 description 1
229930182823 kanamycin A Natural products 0.000 description 1
210000002510 keratinocyte Anatomy 0.000 description 1
108010045069 keyhole-limpet hemocyanin Proteins 0.000 description 1
230000002147 killing effect Effects 0.000 description 1
229940057428 lactoperoxidase Drugs 0.000 description 1
239000008101 lactose Substances 0.000 description 1
238000011031 large-scale manufacturing process Methods 0.000 description 1
239000004816 latex Substances 0.000 description 1
229920000126 latex Polymers 0.000 description 1
229940115286 lentinan Drugs 0.000 description 1
230000003902 lesion Effects 0.000 description 1
GDBQQVLCIARPGH-ULQDDVLXSA-N leupeptin Chemical compound CC(C)C[C@H](NC(C)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@H](C=O)CCCN=C(N)N GDBQQVLCIARPGH-ULQDDVLXSA-N 0.000 description 1
108010052968 leupeptin Proteins 0.000 description 1
RGLRXNKKBLIBQS-XNHQSDQCSA-N leuprolide acetate Chemical compound CC(O)=O.CCNC(=O)[C@@H]1CCCN1C(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@H](CO)NC(=O)[C@H](CC=1C2=CC=CC=C2NC=1)NC(=O)[C@H](CC=1N=CNC=1)NC(=O)[C@H]1NC(=O)CC1)CC1=CC=C(O)C=C1 RGLRXNKKBLIBQS-XNHQSDQCSA-N 0.000 description 1
229960001614 levamisole Drugs 0.000 description 1
UGFHIPBXIWJXNA-UHFFFAOYSA-N liarozole Chemical compound ClC1=CC=CC(C(C=2C=C3NC=NC3=CC=2)N2C=NC=C2)=C1 UGFHIPBXIWJXNA-UHFFFAOYSA-N 0.000 description 1
229950007056 liarozole Drugs 0.000 description 1
210000004185 liver Anatomy 0.000 description 1
230000004807 localization Effects 0.000 description 1
229960002247 lomustine Drugs 0.000 description 1
229960003538 lonidamine Drugs 0.000 description 1
WDRYRZXSPDWGEB-UHFFFAOYSA-N lonidamine Chemical compound C12=CC=CC=C2C(C(=O)O)=NN1CC1=CC=C(Cl)C=C1Cl WDRYRZXSPDWGEB-UHFFFAOYSA-N 0.000 description 1
101150074251 lpp gene Proteins 0.000 description 1
201000005296 lung carcinoma Diseases 0.000 description 1
210000005265 lung cell Anatomy 0.000 description 1
239000008176 lyophilized powder Substances 0.000 description 1
125000003588 lysine group Chemical group [H]N([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 1
239000004325 lysozyme Substances 0.000 description 1
229960000274 lysozyme Drugs 0.000 description 1
235000010335 lysozyme Nutrition 0.000 description 1
230000002101 lytic effect Effects 0.000 description 1
229910052749 magnesium Inorganic materials 0.000 description 1
239000011777 magnesium Substances 0.000 description 1
235000009973 maize Nutrition 0.000 description 1
230000003211 malignant effect Effects 0.000 description 1
239000000594 mannitol Substances 0.000 description 1
235000010355 mannitol Nutrition 0.000 description 1
MQXVYODZCMMZEM-ZYUZMQFOSA-N mannomustine Chemical compound ClCCNC[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CNCCCl MQXVYODZCMMZEM-ZYUZMQFOSA-N 0.000 description 1
229950008612 mannomustine Drugs 0.000 description 1
229960001924 melphalan Drugs 0.000 description 1
SGDBTWWWUNNDEQ-LBPRGKRZSA-N melphalan Chemical compound OC(=O)[C@@H](N)CC1=CC=C(N(CCCl)CCCl)C=C1 SGDBTWWWUNNDEQ-LBPRGKRZSA-N 0.000 description 1
229960003151 mercaptamine Drugs 0.000 description 1
229910052751 metal Inorganic materials 0.000 description 1
239000002184 metal Chemical class 0.000 description 1
230000009401 metastasis Effects 0.000 description 1
230000001394 metastastic effect Effects 0.000 description 1
206010061289 metastatic neoplasm Diseases 0.000 description 1
208000010658 metastatic prostate carcinoma Diseases 0.000 description 1
VJRAUFKOOPNFIQ-TVEKBUMESA-N methyl (1r,2r,4s)-4-[(2r,4s,5s,6s)-5-[(2s,4s,5s,6s)-5-[(2s,4s,5s,6s)-4,5-dihydroxy-6-methyloxan-2-yl]oxy-4-hydroxy-6-methyloxan-2-yl]oxy-4-(dimethylamino)-6-methyloxan-2-yl]oxy-2-ethyl-2,5,7,10-tetrahydroxy-6,11-dioxo-3,4-dihydro-1h-tetracene-1-carboxylat Chemical compound O([C@H]1[C@@H](O)C[C@@H](O[C@H]1C)O[C@H]1[C@H](C[C@@H](O[C@H]1C)O[C@H]1C[C@]([C@@H](C2=CC=3C(=O)C4=C(O)C=CC(O)=C4C(=O)C=3C(O)=C21)C(=O)OC)(O)CC)N(C)C)[C@H]1C[C@H](O)[C@H](O)[C@H](C)O1 VJRAUFKOOPNFIQ-TVEKBUMESA-N 0.000 description 1
239000004292 methyl p-hydroxybenzoate Substances 0.000 description 1
235000010270 methyl p-hydroxybenzoate Nutrition 0.000 description 1
229960002216 methylparaben Drugs 0.000 description 1
244000005700 microbiome Species 0.000 description 1
238000000520 microinjection Methods 0.000 description 1
108010029942 microperoxidase Proteins 0.000 description 1
235000013336 milk Nutrition 0.000 description 1
239000008267 milk Substances 0.000 description 1
210000004080 milk Anatomy 0.000 description 1
VFKZTMPDYBFSTM-GUCUJZIJSA-N mitolactol Chemical compound BrC[C@H](O)[C@@H](O)[C@@H](O)[C@H](O)CBr VFKZTMPDYBFSTM-GUCUJZIJSA-N 0.000 description 1
229950010913 mitolactol Drugs 0.000 description 1
229960000350 mitotane Drugs 0.000 description 1
108010010621 modeccin Proteins 0.000 description 1
239000003607 modifier Substances 0.000 description 1
ZDZOTLJHXYCWBA-BSEPLHNVSA-N molport-006-823-826 Chemical compound O([C@H]1[C@H]2[C@@](C([C@H](O)C3=C(C)[C@@H](OC(=O)[C@H](O)[C@@H](NC(=O)OC(C)(C)C)C=4C=CC=CC=4)C[C@@]1(O)C3(C)C)=O)(C)[C@@H](O)C[C@H]1OC[C@]12OC(=O)C)C(=O)C1=CC=CC=C1 ZDZOTLJHXYCWBA-BSEPLHNVSA-N 0.000 description 1
238000004264 monolayer culture Methods 0.000 description 1
239000000178 monomer Substances 0.000 description 1
150000002772 monosaccharides Chemical class 0.000 description 1
FOYWNSCCNCUEPU-UHFFFAOYSA-N mopidamol Chemical compound C12=NC(N(CCO)CCO)=NC=C2N=C(N(CCO)CCO)N=C1N1CCCCC1 FOYWNSCCNCUEPU-UHFFFAOYSA-N 0.000 description 1
229950010718 mopidamol Drugs 0.000 description 1
230000002107 myocardial effect Effects 0.000 description 1
210000004165 myocardium Anatomy 0.000 description 1
GNOLWGAJQVLBSM-UHFFFAOYSA-N n,n,5,7-tetramethyl-1,2,3,4-tetrahydronaphthalen-1-amine Chemical compound C1=C(C)C=C2C(N(C)C)CCCC2=C1C GNOLWGAJQVLBSM-UHFFFAOYSA-N 0.000 description 1
JYIYPKOJFKMEKS-UHFFFAOYSA-N n-(2,2-dimethyl-1-phenylpropylidene)hydroxylamine Chemical compound CC(C)(C)C(=NO)C1=CC=CC=C1 JYIYPKOJFKMEKS-UHFFFAOYSA-N 0.000 description 1
210000003739 neck Anatomy 0.000 description 1
230000035407 negative regulation of cell proliferation Effects 0.000 description 1
QZGIWPZCWHMVQL-UIYAJPBUSA-N neocarzinostatin chromophore Chemical compound O1[C@H](C)[C@H](O)[C@H](O)[C@@H](NC)[C@H]1O[C@@H]1C/2=C/C#C[C@H]3O[C@@]3([C@@H]3OC(=O)OC3)C#CC\2=C[C@H]1OC(=O)C1=C(O)C=CC2=C(C)C=C(OC)C=C12 QZGIWPZCWHMVQL-UIYAJPBUSA-N 0.000 description 1
210000005036 nerve Anatomy 0.000 description 1
230000001537 neural effect Effects 0.000 description 1
208000007538 neurilemmoma Diseases 0.000 description 1
229960002653 nilutamide Drugs 0.000 description 1
XWXYUMMDTVBTOU-UHFFFAOYSA-N nilutamide Chemical compound O=C1C(C)(C)NC(=O)N1C1=CC=C([N+]([O-])=O)C(C(F)(F)F)=C1 XWXYUMMDTVBTOU-UHFFFAOYSA-N 0.000 description 1
229960001420 nimustine Drugs 0.000 description 1
VFEDRRNHLBGPNN-UHFFFAOYSA-N nimustine Chemical compound CC1=NC=C(CNC(=O)N(CCCl)N=O)C(N)=N1 VFEDRRNHLBGPNN-UHFFFAOYSA-N 0.000 description 1
YMVWGSQGCWCDGW-UHFFFAOYSA-N nitracrine Chemical compound C1=CC([N+]([O-])=O)=C2C(NCCCN(C)C)=C(C=CC=C3)C3=NC2=C1 YMVWGSQGCWCDGW-UHFFFAOYSA-N 0.000 description 1
229950008607 nitracrine Drugs 0.000 description 1
229920001220 nitrocellulos Polymers 0.000 description 1
229910052757 nitrogen Inorganic materials 0.000 description 1
229950009266 nogalamycin Drugs 0.000 description 1
KGTDRFCXGRULNK-JYOBTZKQSA-N nogalamycin Chemical compound CO[C@@H]1[C@@](OC)(C)[C@@H](OC)[C@H](C)O[C@H]1O[C@@H]1C2=C(O)C(C(=O)C3=C(O)C=C4[C@@]5(C)O[C@H]([C@H]([C@@H]([C@H]5O)N(C)C)O)OC4=C3C3=O)=C3C=C2[C@@H](C(=O)OC)[C@@](C)(O)C1 KGTDRFCXGRULNK-JYOBTZKQSA-N 0.000 description 1
239000002736 nonionic surfactant Substances 0.000 description 1
230000001293 nucleolytic effect Effects 0.000 description 1
238000011580 nude mouse model Methods 0.000 description 1
229940100243 oleanolic acid Drugs 0.000 description 1
CZDBNBLGZNWKMC-MWQNXGTOSA-N olivomycin Chemical class O([C@@H]1C[C@@H](O[C@H](C)[C@@H]1O)OC=1C=C2C=C3C[C@H]([C@@H](C(=O)C3=C(O)C2=C(O)C=1)O[C@H]1O[C@@H](C)[C@H](O)[C@@H](OC2O[C@@H](C)[C@H](O)[C@@H](O)C2)C1)[C@H](OC)C(=O)[C@@H](O)[C@@H](C)O)[C@H]1C[C@H](O)[C@H](OC)[C@H](C)O1 CZDBNBLGZNWKMC-MWQNXGTOSA-N 0.000 description 1
150000007524 organic acids Chemical class 0.000 description 1
235000005985 organic acids Nutrition 0.000 description 1
230000004823 osteo-induction effect Effects 0.000 description 1
229960001756 oxaliplatin Drugs 0.000 description 1
DWAFYCQODLXJNR-BNTLRKBRSA-L oxaliplatin Chemical compound O1C(=O)C(=O)O[Pt]11N[C@@H]2CCCC[C@H]2N1 DWAFYCQODLXJNR-BNTLRKBRSA-L 0.000 description 1
230000003647 oxidation Effects 0.000 description 1
238000007254 oxidation reaction Methods 0.000 description 1
230000001590 oxidative effect Effects 0.000 description 1
230000036542 oxidative stress Effects 0.000 description 1
LXCFILQKKLGQFO-UHFFFAOYSA-N p-hydroxybenzoic acid methyl ester Natural products COC(=O)C1=CC=C(O)C=C1 LXCFILQKKLGQFO-UHFFFAOYSA-N 0.000 description 1
229940055729 papain Drugs 0.000 description 1
235000019834 papain Nutrition 0.000 description 1
239000012188 paraffin wax Substances 0.000 description 1
239000000199 parathyroid hormone Substances 0.000 description 1
229960001319 parathyroid hormone Drugs 0.000 description 1
230000036961 partial effect Effects 0.000 description 1
230000001575 pathological effect Effects 0.000 description 1
230000007170 pathology Effects 0.000 description 1
239000008188 pellet Substances 0.000 description 1
229940049954 penicillin Drugs 0.000 description 1
229950009506 penicillinase Drugs 0.000 description 1
229960002340 pentostatin Drugs 0.000 description 1
FPVKHBSQESCIEP-JQCXWYLXSA-N pentostatin Chemical compound C1[C@H](O)[C@@H](CO)O[C@H]1N1C(N=CNC[C@H]2O)=C2N=C1 FPVKHBSQESCIEP-JQCXWYLXSA-N 0.000 description 1
229940111202 pepsin Drugs 0.000 description 1
239000000813 peptide hormone Substances 0.000 description 1
239000000137 peptide hydrolase inhibitor Substances 0.000 description 1
125000001151 peptidyl group Chemical group 0.000 description 1
230000002093 peripheral effect Effects 0.000 description 1
235000020030 perry Nutrition 0.000 description 1
108700010839 phage proteins Proteins 0.000 description 1
230000008782 phagocytosis Effects 0.000 description 1
230000000144 pharmacologic effect Effects 0.000 description 1
238000001050 pharmacotherapy Methods 0.000 description 1
239000012071 phase Substances 0.000 description 1
108010076042 phenomycin Proteins 0.000 description 1
101150009573 phoA gene Proteins 0.000 description 1
WTJKGGKOPKCXLL-RRHRGVEJSA-N phosphatidylcholine Chemical compound CCCCCCCCCCCCCCCC(=O)OC[C@H](COP([O-])(=O)OCC[N+](C)(C)C)OC(=O)CCCCCCCC=CCCCCCCCC WTJKGGKOPKCXLL-RRHRGVEJSA-N 0.000 description 1
150000003904 phospholipids Chemical class 0.000 description 1
230000000865 phosphorylative effect Effects 0.000 description 1
230000004962 physiological condition Effects 0.000 description 1
229960000952 pipobroman Drugs 0.000 description 1
NJBFOOCLYDNZJN-UHFFFAOYSA-N pipobroman Chemical compound BrCCC(=O)N1CCN(C(=O)CCBr)CC1 NJBFOOCLYDNZJN-UHFFFAOYSA-N 0.000 description 1
NUKCGLDCWQXYOQ-UHFFFAOYSA-N piposulfan Chemical compound CS(=O)(=O)OCCC(=O)N1CCN(C(=O)CCOS(C)(=O)=O)CC1 NUKCGLDCWQXYOQ-UHFFFAOYSA-N 0.000 description 1
229950001100 piposulfan Drugs 0.000 description 1
229960001221 pirarubicin Drugs 0.000 description 1
229920003023 plastic Polymers 0.000 description 1
239000004033 plastic Substances 0.000 description 1
229910052697 platinum Inorganic materials 0.000 description 1
150000003057 platinum Chemical class 0.000 description 1
150000003058 platinum compounds Chemical class 0.000 description 1
229920001983 poloxamer Polymers 0.000 description 1
229920001200 poly(ethylene-vinyl acetate) Polymers 0.000 description 1
229920000747 poly(lactic acid) Polymers 0.000 description 1
229920002401 polyacrylamide Polymers 0.000 description 1
108010054442 polyalanine Proteins 0.000 description 1
108010064470 polyaspartate Proteins 0.000 description 1
229920000728 polyester Polymers 0.000 description 1
229920002338 polyhydroxyethylmethacrylate Polymers 0.000 description 1
229920000642 polymer Polymers 0.000 description 1
238000006116 polymerization reaction Methods 0.000 description 1
229920000136 polysorbate Polymers 0.000 description 1
229920002451 polyvinyl alcohol Polymers 0.000 description 1
229920000036 polyvinylpyrrolidone Polymers 0.000 description 1
239000001267 polyvinylpyrrolidone Substances 0.000 description 1
235000013855 polyvinylpyrrolidone Nutrition 0.000 description 1
238000010837 poor prognosis Methods 0.000 description 1
230000026341 positive regulation of angiogenesis Effects 0.000 description 1
230000001323 posttranslational effect Effects 0.000 description 1
239000000843 powder Substances 0.000 description 1
238000001556 precipitation Methods 0.000 description 1
230000000861 pro-apoptotic effect Effects 0.000 description 1
FYPMFJGVHOHGLL-UHFFFAOYSA-N probucol Chemical compound C=1C(C(C)(C)C)=C(O)C(C(C)(C)C)=CC=1SC(C)(C)SC1=CC(C(C)(C)C)=C(O)C(C(C)(C)C)=C1 FYPMFJGVHOHGLL-UHFFFAOYSA-N 0.000 description 1
229960003912 probucol Drugs 0.000 description 1
CPTBDICYNRMXFX-UHFFFAOYSA-N procarbazine Chemical compound CNNCC1=CC=C(C(=O)NC(C)C)C=C1 CPTBDICYNRMXFX-UHFFFAOYSA-N 0.000 description 1
229960000624 procarbazine Drugs 0.000 description 1
230000008569 process Effects 0.000 description 1
238000012545 processing Methods 0.000 description 1
230000003623 progesteronic effect Effects 0.000 description 1
230000005522 programmed cell death Effects 0.000 description 1
229940097325 prolactin Drugs 0.000 description 1
230000002062 proliferating effect Effects 0.000 description 1
230000000069 prophylactic effect Effects 0.000 description 1
235000010232 propyl p-hydroxybenzoate Nutrition 0.000 description 1
239000004405 propyl p-hydroxybenzoate Substances 0.000 description 1
WGYKZJWCGVVSQN-UHFFFAOYSA-N propylamine Chemical group CCCN WGYKZJWCGVVSQN-UHFFFAOYSA-N 0.000 description 1
229960003415 propylparaben Drugs 0.000 description 1
108010087851 prorelaxin Proteins 0.000 description 1
HZLWUYJLOIAQFC-UHFFFAOYSA-N prosapogenin PS-A Natural products C12CC(C)(C)CCC2(C(O)=O)CCC(C2(CCC3C4(C)C)C)(C)C1=CCC2C3(C)CCC4OC1OCC(O)C(O)C1O HZLWUYJLOIAQFC-UHFFFAOYSA-N 0.000 description 1
235000019833 protease Nutrition 0.000 description 1
235000019419 proteases Nutrition 0.000 description 1
238000001742 protein purification Methods 0.000 description 1
230000012743 protein tagging Effects 0.000 description 1
230000017854 proteolysis Effects 0.000 description 1
230000002797 proteolythic effect Effects 0.000 description 1
WOLQREOUPKZMEX-UHFFFAOYSA-N pteroyltriglutamic acid Chemical compound C=1N=C2NC(N)=NC(=O)C2=NC=1CNC1=CC=C(C(=O)NC(CCC(=O)NC(CCC(=O)NC(CCC(O)=O)C(O)=O)C(O)=O)C(O)=O)C=C1 WOLQREOUPKZMEX-UHFFFAOYSA-N 0.000 description 1
150000003212 purines Chemical class 0.000 description 1
229950010131 puromycin Drugs 0.000 description 1
150000003230 pyrimidines Chemical class 0.000 description 1
239000002516 radical scavenger Substances 0.000 description 1
150000003254 radicals Chemical class 0.000 description 1
238000003127 radioimmunoassay Methods 0.000 description 1
238000001959 radiotherapy Methods 0.000 description 1
238000002708 random mutagenesis Methods 0.000 description 1
229960002185 ranimustine Drugs 0.000 description 1
229910052761 rare earth metal Inorganic materials 0.000 description 1
150000002910 rare earth metals Chemical class 0.000 description 1
BMKDZUISNHGIBY-UHFFFAOYSA-N razoxane Chemical compound C1C(=O)NC(=O)CN1C(C)CN1CC(=O)NC(=O)C1 BMKDZUISNHGIBY-UHFFFAOYSA-N 0.000 description 1
229960000460 razoxane Drugs 0.000 description 1
238000003753 real-time PCR Methods 0.000 description 1
102000027426 receptor tyrosine kinases Human genes 0.000 description 1
108091008598 receptor tyrosine kinases Proteins 0.000 description 1
230000010837 receptor-mediated endocytosis Effects 0.000 description 1
238000003259 recombinant expression Methods 0.000 description 1
230000006798 recombination Effects 0.000 description 1
238000005215 recombination Methods 0.000 description 1
238000011084 recovery Methods 0.000 description 1
230000022983 regulation of cell cycle Effects 0.000 description 1
230000026267 regulation of growth Effects 0.000 description 1
229930002330 retinoic acid Natural products 0.000 description 1
239000012440 retinoic acid metabolism blocking agent Substances 0.000 description 1
238000004007 reversed phase HPLC Methods 0.000 description 1
PYWVYCXTNDRMGF-UHFFFAOYSA-N rhodamine B Chemical compound [Cl-].C=12C=CC(=[N+](CC)CC)C=C2OC2=CC(N(CC)CC)=CC=C2C=1C1=CC=CC=C1C(O)=O PYWVYCXTNDRMGF-UHFFFAOYSA-N 0.000 description 1
229950004892 rodorubicin Drugs 0.000 description 1
VHXNKPBCCMUMSW-FQEVSTJZSA-N rubitecan Chemical compound C1=CC([N+]([O-])=O)=C2C=C(CN3C4=CC5=C(C3=O)COC(=O)[C@]5(O)CC)C4=NC2=C1 VHXNKPBCCMUMSW-FQEVSTJZSA-N 0.000 description 1
239000012723 sample buffer Substances 0.000 description 1
238000013391 scatchard analysis Methods 0.000 description 1
206010039667 schwannoma Diseases 0.000 description 1
238000003345 scintillation counting Methods 0.000 description 1
230000007017 scission Effects 0.000 description 1
229940065287 selenium compound Drugs 0.000 description 1
150000003343 selenium compounds Chemical class 0.000 description 1
238000013207 serial dilution Methods 0.000 description 1
210000000717 sertoli cell Anatomy 0.000 description 1
230000035939 shock Effects 0.000 description 1
102000035025 signaling receptors Human genes 0.000 description 1
108091005475 signaling receptors Proteins 0.000 description 1
239000000377 silicon dioxide Substances 0.000 description 1
239000002356 single layer Substances 0.000 description 1
230000003007 single stranded DNA break Effects 0.000 description 1
229950001403 sizofiran Drugs 0.000 description 1
210000003491 skin Anatomy 0.000 description 1
231100000438 skin toxicity Toxicity 0.000 description 1
239000002002 slurry Substances 0.000 description 1
229940126586 small molecule drug Drugs 0.000 description 1
239000011734 sodium Substances 0.000 description 1
229910052708 sodium Inorganic materials 0.000 description 1
239000001632 sodium acetate Substances 0.000 description 1
235000017281 sodium acetate Nutrition 0.000 description 1
PTLRDCMBXHILCL-UHFFFAOYSA-M sodium arsenite Chemical compound [Na+].[O-][As]=O PTLRDCMBXHILCL-UHFFFAOYSA-M 0.000 description 1
TXBNDGDMWKVRQW-UHFFFAOYSA-M sodium;2-[[1,3-dihydroxy-2-(hydroxymethyl)propan-2-yl]azaniumyl]acetate;dodecyl sulfate Chemical compound [Na+].OCC(CO)(CO)NCC(O)=O.CCCCCCCCCCCCOS([O-])(=O)=O TXBNDGDMWKVRQW-UHFFFAOYSA-M 0.000 description 1
239000007787 solid Substances 0.000 description 1
239000007790 solid phase Substances 0.000 description 1
239000002195 soluble material Substances 0.000 description 1
239000000600 sorbitol Substances 0.000 description 1
125000006850 spacer group Chemical group 0.000 description 1
238000013319 spin trapping Methods 0.000 description 1
238000009987 spinning Methods 0.000 description 1
229950006315 spirogermanium Drugs 0.000 description 1
210000000952 spleen Anatomy 0.000 description 1
210000004988 splenocyte Anatomy 0.000 description 1
238000010561 standard procedure Methods 0.000 description 1
SFVFIFLLYFPGHH-UHFFFAOYSA-M stearalkonium chloride Chemical compound [Cl-].CCCCCCCCCCCCCCCCCC[N+](C)(C)CC1=CC=CC=C1 SFVFIFLLYFPGHH-UHFFFAOYSA-M 0.000 description 1
238000011146 sterile filtration Methods 0.000 description 1
238000003860 storage Methods 0.000 description 1
229960001052 streptozocin Drugs 0.000 description 1
ZSJLQEPLLKMAKR-GKHCUFPYSA-N streptozocin Chemical compound O=NN(C)C(=O)N[C@H]1[C@@H](O)O[C@H](CO)[C@@H](O)[C@@H]1O ZSJLQEPLLKMAKR-GKHCUFPYSA-N 0.000 description 1
238000010254 subcutaneous injection Methods 0.000 description 1
239000007929 subcutaneous injection Substances 0.000 description 1
229940014800 succinic anhydride Drugs 0.000 description 1
JJAHTWIKCUJRDK-UHFFFAOYSA-N succinimidyl 4-(N-maleimidomethyl)cyclohexane-1-carboxylate Chemical compound C1CC(CN2C(C=CC2=O)=O)CCC1C(=O)ON1C(=O)CCC1=O JJAHTWIKCUJRDK-UHFFFAOYSA-N 0.000 description 1
239000005720 sucrose Substances 0.000 description 1
108060007951 sulfatase Proteins 0.000 description 1
239000013589 supplement Substances 0.000 description 1
230000001629 suppression Effects 0.000 description 1
229960005314 suramin Drugs 0.000 description 1
FIAFUQMPZJWCLV-UHFFFAOYSA-N suramin Chemical compound OS(=O)(=O)C1=CC(S(O)(=O)=O)=C2C(NC(=O)C3=CC=C(C(=C3)NC(=O)C=3C=C(NC(=O)NC=4C=C(C=CC=4)C(=O)NC=4C(=CC=C(C=4)C(=O)NC=4C5=C(C=C(C=C5C(=CC=4)S(O)(=O)=O)S(O)(=O)=O)S(O)(=O)=O)C)C=CC=3)C)=CC=C(S(O)(=O)=O)C2=C1 FIAFUQMPZJWCLV-UHFFFAOYSA-N 0.000 description 1
239000004094 surface-active agent Substances 0.000 description 1
238000001356 surgical procedure Methods 0.000 description 1
239000000725 suspension Substances 0.000 description 1
238000004114 suspension culture Methods 0.000 description 1
238000013268 sustained release Methods 0.000 description 1
239000012730 sustained-release form Substances 0.000 description 1
238000003786 synthesis reaction Methods 0.000 description 1
229940063683 taxotere Drugs 0.000 description 1
NRUKOCRGYNPUPR-QBPJDGROSA-N teniposide Chemical compound COC1=C(O)C(OC)=CC([C@@H]2C3=CC=4OCOC=4C=C3[C@@H](O[C@H]3[C@@H]([C@@H](O)[C@@H]4O[C@@H](OC[C@H]4O3)C=3SC=CC=3)O)[C@@H]3[C@@H]2C(OC3)=O)=C1 NRUKOCRGYNPUPR-QBPJDGROSA-N 0.000 description 1
229960001278 teniposide Drugs 0.000 description 1
238000012360 testing method Methods 0.000 description 1
229960005353 testolactone Drugs 0.000 description 1
BPEWUONYVDABNZ-DZBHQSCQSA-N testolactone Chemical compound O=C1C=C[C@]2(C)[C@H]3CC[C@](C)(OC(=O)CC4)[C@@H]4[C@@H]3CCC2=C1 BPEWUONYVDABNZ-DZBHQSCQSA-N 0.000 description 1
229960002180 tetracycline Drugs 0.000 description 1
229930101283 tetracycline Natural products 0.000 description 1
235000019364 tetracycline Nutrition 0.000 description 1
150000003522 tetracyclines Chemical class 0.000 description 1
MPLHNVLQVRSVEE-UHFFFAOYSA-N texas red Chemical compound [O-]S(=O)(=O)C1=CC(S(Cl)(=O)=O)=CC=C1C(C1=CC=2CCCN3CCCC(C=23)=C1O1)=C2C1=C(CCC1)C3=[N+]1CCCC3=C2 MPLHNVLQVRSVEE-UHFFFAOYSA-N 0.000 description 1
RSPCKAHMRANGJZ-UHFFFAOYSA-N thiohydroxylamine Chemical compound SN RSPCKAHMRANGJZ-UHFFFAOYSA-N 0.000 description 1
125000003396 thiol group Chemical group [H]S* 0.000 description 1
150000003573 thiols Chemical class 0.000 description 1
RYYWUUFWQRZTIU-UHFFFAOYSA-K thiophosphate Chemical compound [O-]P([O-])([O-])=S RYYWUUFWQRZTIU-UHFFFAOYSA-K 0.000 description 1
125000000341 threoninyl group Chemical group [H]OC([H])(C([H])([H])[H])C([H])(N([H])[H])C(*)=O 0.000 description 1
229960002175 thyroglobulin Drugs 0.000 description 1
229940034208 thyroxine Drugs 0.000 description 1
XUIIKFGFIJCVMT-UHFFFAOYSA-N thyroxine-binding globulin Natural products IC1=CC(CC([NH3+])C([O-])=O)=CC(I)=C1OC1=CC(I)=C(O)C(I)=C1 XUIIKFGFIJCVMT-UHFFFAOYSA-N 0.000 description 1
YFTWHEBLORWGNI-UHFFFAOYSA-N tiamiprine Chemical compound CN1C=NC([N+]([O-])=O)=C1SC1=NC(N)=NC2=C1NC=N2 YFTWHEBLORWGNI-UHFFFAOYSA-N 0.000 description 1
229950011457 tiamiprine Drugs 0.000 description 1
229960003087 tioguanine Drugs 0.000 description 1
RUELTTOHQODFPA-UHFFFAOYSA-N toluene 2,6-diisocyanate Chemical compound CC1=C(N=C=O)C=CC=C1N=C=O RUELTTOHQODFPA-UHFFFAOYSA-N 0.000 description 1
230000000699 topical effect Effects 0.000 description 1
229940044693 topoisomerase inhibitor Drugs 0.000 description 1
XFCLJVABOIYOMF-QPLCGJKRSA-N toremifene Chemical compound C1=CC(OCCN(C)C)=CC=C1C(\C=1C=CC=CC=1)=C(\CCCl)C1=CC=CC=C1 XFCLJVABOIYOMF-QPLCGJKRSA-N 0.000 description 1
229960005026 toremifene Drugs 0.000 description 1
231100000331 toxic Toxicity 0.000 description 1
230000002588 toxic effect Effects 0.000 description 1
231100000027 toxicology Toxicity 0.000 description 1
239000011573 trace mineral Substances 0.000 description 1
235000013619 trace mineral Nutrition 0.000 description 1
230000005030 transcription termination Effects 0.000 description 1
239000012581 transferrin Substances 0.000 description 1
230000009261 transgenic effect Effects 0.000 description 1
230000007704 transition Effects 0.000 description 1
230000005945 translocation Effects 0.000 description 1
229940074410 trehalose Drugs 0.000 description 1
229940074409 trehalose dihydrate Drugs 0.000 description 1
229950001353 tretamine Drugs 0.000 description 1
IUCJMVBFZDHPDX-UHFFFAOYSA-N tretamine Chemical compound C1CN1C1=NC(N2CC2)=NC(N2CC2)=N1 IUCJMVBFZDHPDX-UHFFFAOYSA-N 0.000 description 1
229960001727 tretinoin Drugs 0.000 description 1
229960004560 triaziquone Drugs 0.000 description 1
PXSOHRWMIRDKMP-UHFFFAOYSA-N triaziquone Chemical compound O=C1C(N2CC2)=C(N2CC2)C(=O)C=C1N1CC1 PXSOHRWMIRDKMP-UHFFFAOYSA-N 0.000 description 1
QORWJWZARLRLPR-UHFFFAOYSA-H tricalcium bis(phosphate) Chemical compound [Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O QORWJWZARLRLPR-UHFFFAOYSA-H 0.000 description 1
229930013292 trichothecene Natural products 0.000 description 1
150000003327 trichothecene derivatives Chemical class 0.000 description 1
229960001670 trilostane Drugs 0.000 description 1
KVJXBPDAXMEYOA-CXANFOAXSA-N trilostane Chemical compound OC1=C(C#N)C[C@]2(C)[C@H]3CC[C@](C)([C@H](CC4)O)[C@@H]4[C@@H]3CC[C@@]32O[C@@H]31 KVJXBPDAXMEYOA-CXANFOAXSA-N 0.000 description 1
NOYPYLRCIDNJJB-UHFFFAOYSA-N trimetrexate Chemical compound COC1=C(OC)C(OC)=CC(NCC=2C(=C3C(N)=NC(N)=NC3=CC=2)C)=C1 NOYPYLRCIDNJJB-UHFFFAOYSA-N 0.000 description 1
229960001099 trimetrexate Drugs 0.000 description 1
229950000212 trioxifene Drugs 0.000 description 1
GPRLSGONYQIRFK-MNYXATJNSA-N triton Chemical compound [3H+] GPRLSGONYQIRFK-MNYXATJNSA-N 0.000 description 1
229960000875 trofosfamide Drugs 0.000 description 1
UMKFEPPTGMDVMI-UHFFFAOYSA-N trofosfamide Chemical compound ClCCN(CCCl)P1(=O)OCCCN1CCCl UMKFEPPTGMDVMI-UHFFFAOYSA-N 0.000 description 1
230000001228 trophic effect Effects 0.000 description 1
239000012588 trypsin Substances 0.000 description 1
239000002753 trypsin inhibitor Substances 0.000 description 1
HDZZVAMISRMYHH-LITAXDCLSA-N tubercidin Chemical compound C1=CC=2C(N)=NC=NC=2N1[C@@H]1O[C@@H](CO)[C@H](O)[C@H]1O HDZZVAMISRMYHH-LITAXDCLSA-N 0.000 description 1
108010087967 type I signal peptidase Proteins 0.000 description 1
229950009811 ubenimex Drugs 0.000 description 1
238000000108 ultra-filtration Methods 0.000 description 1
238000002604 ultrasonography Methods 0.000 description 1
238000002562 urinalysis Methods 0.000 description 1
229940096998 ursolic acid Drugs 0.000 description 1
PLSAJKYPRJGMHO-UHFFFAOYSA-N ursolic acid Natural products CC1CCC2(CCC3(C)C(C=CC4C5(C)CCC(O)C(C)(C)C5CCC34C)C2C1C)C(=O)O PLSAJKYPRJGMHO-UHFFFAOYSA-N 0.000 description 1
208000012991 uterine carcinoma Diseases 0.000 description 1
239000004474 valine Substances 0.000 description 1
230000002792 vascular Effects 0.000 description 1
210000003462 vein Anatomy 0.000 description 1
229960004355 vindesine Drugs 0.000 description 1
UGGWPQSBPIFKDZ-KOTLKJBCSA-N vindesine Chemical compound C([C@@H](C[C@]1(C(=O)OC)C=2C(=CC3=C([C@]45[C@H]([C@@]([C@H](O)[C@]6(CC)C=CCN([C@H]56)CC4)(O)C(N)=O)N3C)C=2)OC)C[C@@](C2)(O)CC)N2CCC2=C1N=C1[C]2C=CC=C1 UGGWPQSBPIFKDZ-KOTLKJBCSA-N 0.000 description 1
GBABOYUKABKIAF-IELIFDKJSA-N vinorelbine Chemical compound C1N(CC=2C3=CC=CC=C3NC=22)CC(CC)=C[C@H]1C[C@]2(C(=O)OC)C1=CC([C@]23[C@H]([C@@]([C@H](OC(C)=O)[C@]4(CC)C=CCN([C@H]34)CC2)(O)C(=O)OC)N2C)=C2C=C1OC GBABOYUKABKIAF-IELIFDKJSA-N 0.000 description 1
229960002066 vinorelbine Drugs 0.000 description 1
239000013603 viral vector Substances 0.000 description 1
235000019154 vitamin C Nutrition 0.000 description 1
239000011718 vitamin C Substances 0.000 description 1
235000019165 vitamin E Nutrition 0.000 description 1
229940046009 vitamin E Drugs 0.000 description 1
239000011709 vitamin E Substances 0.000 description 1
229950009268 zinostatin Drugs 0.000 description 1
229960000641 zorubicin Drugs 0.000 description 1
FBTUMDXHSRTGRV-ALTNURHMSA-N zorubicin Chemical compound O([C@H]1C[C@@](O)(CC=2C(O)=C3C(=O)C=4C=CC=C(C=4C(=O)C3=C(O)C=21)OC)C(\C)=N\NC(=O)C=1C=CC=CC=1)[C@H]1C[C@H](N)[C@H](O)[C@H](C)O1 FBTUMDXHSRTGRV-ALTNURHMSA-N 0.000 description 1
150000003952 β-lactams Chemical class 0.000 description 1

Classifications

- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K39/395—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/32—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against translation products of oncogenes
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K47/00—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient
- A61K47/50—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates
- A61K47/51—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent
- A61K47/68—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent the modifying agent being an antibody, an immunoglobulin or a fragment thereof, e.g. an Fc-fragment
- A61K47/6801—Drug-antibody or immunoglobulin conjugates defined by the pharmacologically or therapeutically active agent
- A61K47/6803—Drugs conjugated to an antibody or immunoglobulin, e.g. cisplatin-antibody conjugates
- A61K47/6807—Drugs conjugated to an antibody or immunoglobulin, e.g. cisplatin-antibody conjugates the drug or compound being a sugar, nucleoside, nucleotide, nucleic acid, e.g. RNA antisense
- A61K47/6809—Antibiotics, e.g. antitumor antibiotics anthracyclins, adriamycin, doxorubicin or daunomycin
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K2039/505—Medicinal preparations containing antigens or antibodies comprising antibodies
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K2039/505—Medicinal preparations containing antigens or antibodies comprising antibodies
- A61K2039/507—Comprising a combination of two or more separate antibodies
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
- C07K2317/24—Immunoglobulins specific features characterized by taxonomic origin containing regions, domains or residues from different species, e.g. chimeric, humanized or veneered
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
- C07K2317/73—Inducing cell death, e.g. apoptosis, necrosis or inhibition of cell proliferation
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
- C07K2317/76—Antagonist effect on antigen, e.g. neutralization or inhibition of binding

Landscapes

Health & Medical Sciences (AREA)
Chemical & Material Sciences (AREA)
Life Sciences & Earth Sciences (AREA)
Medicinal Chemistry (AREA)
Engineering & Computer Science (AREA)
Bioinformatics & Cheminformatics (AREA)
General Health & Medical Sciences (AREA)
Public Health (AREA)
Veterinary Medicine (AREA)
Organic Chemistry (AREA)
Pharmacology & Pharmacy (AREA)
Animal Behavior & Ethology (AREA)
Immunology (AREA)
Epidemiology (AREA)
Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
Biochemistry (AREA)
Molecular Biology (AREA)
General Chemical & Material Sciences (AREA)
Chemical Kinetics & Catalysis (AREA)
Mycology (AREA)
Genetics & Genomics (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Microbiology (AREA)
Oncology (AREA)
Biophysics (AREA)
Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
Peptides Or Proteins (AREA)
Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Micro-Organisms Or Cultivation Processes Thereof (AREA)
Acyclic And Carbocyclic Compounds In Medicinal Compositions (AREA)
Preparation Of Compounds By Using Micro-Organisms (AREA)
Medicinal Preparation (AREA)
Medicines Containing Material From Animals Or Micro-Organisms (AREA)
Medical Preparation Storing Or Oral Administration Devices (AREA)
Packages (AREA)

NO20016329A 1999-06-25 2001-12-21 Humanisert, monoklonalt antistoff som binder ErbB2/HER2, farmasoytisk formulering, immunkonjugat, isolert nukleinsyre, vektor, vertscelle og fremgangsmate for fremstilling av antistoff. NO328377B1 (no)

Applications Claiming Priority (2)

Application Number	Priority Date	Filing Date	Title
US14131699P	1999-06-25	1999-06-25
PCT/US2000/017366 WO2001000245A2 (en)	1999-06-25	2000-06-23	HUMANIZED ANTI-ErbB2 ANTIBODIES AND TREATMENT WITH ANTI-ErbB2 ANTIBODIES

Publications (3)

Publication Number	Publication Date
NO20016329D0 NO20016329D0 (no)	2001-12-21
NO20016329L NO20016329L (no)	2002-02-25
NO328377B1 true NO328377B1 (no)	2010-02-08

Family

ID=22495168

Family Applications (3)

Application Number	Title	Priority Date	Filing Date
NO20016329A NO328377B1 (no)	1999-06-25	2001-12-21	Humanisert, monoklonalt antistoff som binder ErbB2/HER2, farmasoytisk formulering, immunkonjugat, isolert nukleinsyre, vektor, vertscelle og fremgangsmate for fremstilling av antistoff.
NO20091792A NO336040B1 (no)	1999-06-25	2009-05-05	Anvendelse av antistoff som binder til ErbB2 og blokkerer ligandaktivering av en ErbB2-reseptor, for fremstilling av et medikament for behandling av kreft hos et menneske, anvendelse av rhuMAb 2C4 for fremstilling av et medikament for behandling av kreft, humanisert antistoff, immunkonjugat, affinitetsmodnet antistoff
NO2013005C NO2013005I1 (no)	1999-06-25	2013-03-12	Pertuzumab

Family Applications After (2)

Application Number	Title	Priority Date	Filing Date
NO20091792A NO336040B1 (no)	1999-06-25	2009-05-05	Anvendelse av antistoff som binder til ErbB2 og blokkerer ligandaktivering av en ErbB2-reseptor, for fremstilling av et medikament for behandling av kreft hos et menneske, anvendelse av rhuMAb 2C4 for fremstilling av et medikament for behandling av kreft, humanisert antistoff, immunkonjugat, affinitetsmodnet antistoff
NO2013005C NO2013005I1 (no)	1999-06-25	2013-03-12	Pertuzumab

Country Status (33)

Country	Link
EP (2)	EP2112167A3 (da)
JP (2)	JP4283474B2 (da)
KR (2)	KR100797308B1 (da)
CN (4)	CN101121750A (da)
AR (1)	AR024464A1 (da)
AT (2)	AT500848B1 (da)
AU (2)	AU784045B2 (da)
BE (1)	BE2013C020I2 (da)
BR (2)	BR122014028365B8 (da)
CA (2)	CA2376596C (da)
CH (1)	CH694589A5 (da)
CY (2)	CY1109525T1 (da)
CZ (1)	CZ299702B6 (da)
DE (2)	DE60042648D1 (da)
DK (1)	DK1189641T5 (da)
ES (1)	ES2329437T3 (da)
FR (1)	FR13C0016I2 (da)
GB (1)	GB2368796B (da)
GE (1)	GEP20104998B (da)
HK (1)	HK1044888A1 (da)
HU (1)	HU226742B1 (da)
IL (3)	IL146954A0 (da)
LU (1)	LU92164I2 (da)
MX (1)	MXPA01013458A (da)
NO (3)	NO328377B1 (da)
NZ (2)	NZ531426A (da)
PL (2)	PL204629B1 (da)
PT (1)	PT1189641E (da)
RU (2)	RU2270029C2 (da)
SI (3)	SI2283867T1 (da)
TR (1)	TR200103756T2 (da)
WO (1)	WO2001000245A2 (da)
ZA (2)	ZA200109786B (da)

Families Citing this family (228)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US8038994B2 (en)	1996-05-15	2011-10-18	Quest Pharmatech Inc.	Combination therapy for treating disease
WO2004009618A2 (en)	2002-07-18	2004-01-29	Crucell Holland B.V.	Recombinant production of mixtures of antibodies
CA2370466C (en) *	1999-06-25	2011-02-08	Sharon Erickson	Methods of treatment using anti-erbb antibody-maytansinoid conjugates
CH694589A5 (de) *	1999-06-25	2005-04-15	Genentech Inc	Humanisierte Anti-ErbB2-Antikörper und Behandlung mit Anti-ErbB2-Antikörpern.
US6825333B1 (en)	1999-08-20	2004-11-30	Chiron Corporation	EGFH2 genes and gene products
IL148114A0 (en)	1999-08-27	2002-09-12	Genentech Inc	DOSAGES FOR TREATMENT WITH ANTI-ErbB2 ANTIBODIES
WO2001024763A2 (en)	1999-10-01	2001-04-12	Immunogen, Inc.	Compositions and methods for treating cancer using immunoconjugates and chemotherapeutic agents
PL217410B1 (pl)	2000-05-19	2014-07-31	Genentech Inc	Zastosowanie antagonisty ErbB, antagonista ErbB do zastosowania w metodzie leczenia raka i sposób identyfikacji pacjenta skłonnego do korzystnej odpowiedzi na antagonistę ErbB przy leczeniu raka
EP1228766A1 (en) *	2001-01-31	2002-08-07	Max-Planck-Gesellschaft zur Förderung der Wissenschaften e.V.	PYK2 phosphorylation by HER3 induces tumor invasion
CA2464947C (en) *	2001-10-26	2012-05-22	Altarex Medical Corp.	Combination therapy for treating disease
JP2005535297A (ja) *	2002-04-11	2005-11-24	アムジェンインコーポレイテッド	Ｈｅｒ−２レセプターチロシンキナーゼ分子およびその使用
ITTO20020340A1 (it) *	2002-04-19	2003-10-20	Biother Di Contardi Gabriella	Localizzazione del recettore her2 mediante anticorpo umanizzato biotinilato.
AU2003237367A1 (en)	2002-06-03	2003-12-19	Chiron Corporation	Use of nrg4, or inhibitors thereof, in the treatment of colon and pancreatic cancer
AT413486B (de)	2002-07-03	2006-03-15	Igeneon Krebs Immuntherapie	Verwendung eines antikörpers gerichtet gegen lewis-antigene
NO340576B1 (no) *	2002-07-11	2017-05-15	Hoffmann La Roche	Rekombinant, humanisert antistoff 2C4 (rhuMab 2C4) for anvendelse sammen med et andre, forskjellig vekstinhiberende anti-ErbB2-antistoff i en fremgangsmåte for behandling av kreft i en pasient og anvendelse derav for fremstilling av et medikament
ES2392525T3 (es) *	2002-07-15	2012-12-11	F. Hoffmann-La Roche Ag	Tratamiento del cáncer con el anticuerpo dirigido contra ErbB2 rhuMAb 2C4
USRE47770E1 (en)	2002-07-18	2019-12-17	Merus N.V.	Recombinant production of mixtures of antibodies
US7264800B2 (en)	2002-07-18	2007-09-04	Helix Biopharma Corporation	Method and composition for inhibiting cancer cell growth
CA2492472C (en)	2002-07-18	2014-01-07	Helix Biopharma Corp.	Use of urease for inhibiting cancer cell growth
CA2494310A1 (en)	2002-08-01	2004-02-12	Immunomedics, Inc.	Alpha-fetoprotein immu31 antibodies and fusion proteins and methods of use thereof
US20040033228A1 (en)	2002-08-16	2004-02-19	Hans-Juergen Krause	Formulation of human antibodies for treating TNF-alpha associated disorders
CN101972478B (zh) *	2002-10-08	2012-10-31	免疫医疗公司	抗体治疗
WO2004054622A1 (en) *	2002-12-13	2004-07-01	Immunomedics, Inc.	Immunoconjugates with an intracellularly-cleavable linkage
EP1613736A4 (en) *	2003-03-11	2007-04-11	Dana Farber Cancer Inst Inc	INHIBITION OF VIRAL PATHOGENESIS
ATE517920T1 (de) *	2003-04-23	2011-08-15	Medarex Inc	Humanisierte antikörper gegen interferon-alpha- rezeptor-1 (ifnar-1)
US8088387B2 (en)	2003-10-10	2012-01-03	Immunogen Inc.	Method of targeting specific cell populations using cell-binding agent maytansinoid conjugates linked via a non-cleavable linker, said conjugates, and methods of making said conjugates
AT500651B9 (de) *	2003-05-27	2010-04-15	Altropus Gmbh	Aktiv immunisierender antikörper
US20100069614A1 (en)	2008-06-27	2010-03-18	Merus B.V.	Antibody producing non-human mammals
EP2395017A3 (en)	2003-05-30	2012-12-19	Merus B.V.	Design and use of paired variable regions of specific binding molecules
EP3095793B1 (en)	2003-07-28	2020-03-25	Genentech, Inc.	Reducing protein a leaching during protein a affinity chromatography
WO2005020923A2 (en) *	2003-08-29	2005-03-10	Cedars-Sinai Medical Center	Composition and method for the treatment of cancer and other physiologic conditions based on modulation of the ppar-gamma pathway and her-kinase axis
NZ545968A (en) *	2003-09-18	2010-01-29	Raven Biotechnologies Inc	KID3 and KID3 antibodies that bind thereto
MXPA06006009A (es) *	2003-11-28	2006-09-04	Mitra Medical Technology Ab	Direccionamiento de antigenos erb.
CA2567520A1 (en)	2004-06-01	2005-12-15	Genentech, Inc.	Maytansinoid-antibody conjugates
SV2006002143A (es) *	2004-06-16	2006-01-26	Genentech Inc	Uso de un anticuerpo para el tratamiento del cancer resistente al platino
PT1771482E (pt)	2004-07-22	2014-11-03	Genentech Inc	Composição de anticorpo her2
US20100111856A1 (en)	2004-09-23	2010-05-06	Herman Gill	Zirconium-radiolabeled, cysteine engineered antibody conjugates
EP3088004B1 (en)	2004-09-23	2018-03-28	Genentech, Inc.	Cysteine engineered antibodies and conjugates
JO3000B1 (ar)	2004-10-20	2016-09-05	Genentech Inc	مركبات أجسام مضادة .
RU2007125644A (ru) *	2004-12-07	2009-01-20	Дженентек Инк. (Us)	Отбор пациентов для терапии ингибитором her
WO2006078307A1 (en)	2005-01-21	2006-07-27	Genentech, Inc.	Fixed dosing of her antibodies
BRPI0606542A8 (pt)	2005-02-23	2018-03-20	Genentech Inc	métodos para aumentar o tempo de progressão de uma doença (ttp)
AR053272A1 (es)	2005-05-11	2007-04-25	Hoffmann La Roche	Determinacion de responsivos a la quimioterapia
AU2006255686A1 (en)	2005-06-06	2006-12-14	Genentech, Inc.	Transgenic models for different genes and their use for gene characterization
US7700299B2 (en)	2005-08-12	2010-04-20	Hoffmann-La Roche Inc.	Method for predicting the response to a treatment
JP2009504183A (ja)	2005-08-15	2009-02-05	ジェネンテック・インコーポレーテッド	遺伝子破壊、それに関連する組成物および方法
KR101164820B1 (ko)	2005-09-22	2012-07-12	삼성전자주식회사	디스플레이장치
US8080534B2 (en)	2005-10-14	2011-12-20	Phigenix, Inc	Targeting PAX2 for the treatment of breast cancer
US20090293137A1 (en)	2005-11-21	2009-11-26	Genentech, Inc.	Novel Gene Disruptions, Compositions and Methods Relating Thereto
AR056857A1 (es)	2005-12-30	2007-10-24	U3 Pharma Ag	Anticuerpos dirigidos hacia her-3 (receptor del factor de crecimiento epidérmico humano-3) y sus usos
JO2660B1 (en)	2006-01-20	2012-06-17	نوفارتيس ايه جي	Pi-3 inhibitors and methods of use
ZA200807714B (en)	2006-02-17	2010-01-27	Genentech Inc	Gene disruptions, compositions and methods relating thereto
TW200812615A (en)	2006-03-22	2008-03-16	Hoffmann La Roche	Tumor therapy with an antibody for vascular endothelial growth factor and an antibody for human epithelial growth factor receptor type 2
TW200808739A (en)	2006-04-06	2008-02-16	Novartis Vaccines & Diagnostic	Quinazolines for PDK1 inhibition
AU2007297565A1 (en)	2006-04-19	2008-03-27	Genentech, Inc.	Novel gene disruptions, compositions and methods relating thereto
PL2446904T3 (pl)	2006-05-30	2015-10-30	Genentech Inc	Przeciwciała anty-CD22, ich immunokoniugaty oraz ich zastosowania
JP2009539836A (ja) *	2006-06-05	2009-11-19	ジェネンテック・インコーポレーテッド	ＥＧＦまたはＴＧＦ−αのレベルの上昇が生じている癌患者の生存の延長
MY150756A (en)	2006-08-21	2014-02-28	Hoffmann La Roche	Tumor theraphy with an anti-vegf antibody
WO2008031531A1 (en) *	2006-09-15	2008-03-20	F. Hoffmann-La Roche Ag	Tumor therapy with a combination of anti-her2 antibodies
MY162056A (en) *	2006-10-12	2017-05-31	Univ Tokyo	Diagnosis and treatment of cancer using anti -ereg antibody
KR20140116546A (ko)	2006-10-27	2014-10-02	제넨테크, 인크.	항체 및 면역접합체 및 이들의 용도
ES2477497T3 (es)	2007-03-02	2014-07-17	Genentech, Inc.	Predicción de la respuesta a un inhibidor de la dimerización de HER basado en la expresión de HER3 bajo
EP2592156B1 (en)	2007-06-08	2016-04-20	Genentech, Inc.	Gene expression markers of tumor resistance to HER2 inhibitor treatment
US9551033B2 (en)	2007-06-08	2017-01-24	Genentech, Inc.	Gene expression markers of tumor resistance to HER2 inhibitor treatment
CN101918844A (zh) *	2007-06-18	2010-12-15	米迪缪尼有限公司	表达epha2和erbb2的细胞的协同治疗
JP2010533495A (ja)	2007-07-16	2010-10-28	ジェネンテック，インコーポレイテッド	ヒト化ＣＤ７９ｂ抗体およびイムノコンジュゲートならびにそれらの使用
TWI439286B (zh)	2007-07-16	2014-06-01	Genentech Inc	抗－ｃｄ７９ｂ抗體及免疫共軛物及使用方法
BRPI0817182A2 (pt)	2007-10-30	2015-03-17	Genentech Inc	Método para purificar um anticorpo e composições
JP2011504740A (ja)	2007-11-27	2011-02-17	アブリンクスエン．ヴェー．	ヘテロ二量体サイトカイン及び／又はこれらの受容体に指向性を有するアミノ酸配列、並びにこれを含むポリペプチド
JP2011506560A (ja)	2007-12-20	2011-03-03	ノバルティスアーゲー	Ｐｉ３キナーゼ阻害剤として用いられるチアゾール誘導体
PE20091174A1 (es) *	2007-12-27	2009-08-03	Chugai Pharmaceutical Co Ltd	Formulacion liquida con contenido de alta concentracion de anticuerpo
US8574577B2 (en)	2008-01-03	2013-11-05	The Scripps Research Institute	VEGF antibodies comprising modular recognition domains
US8557243B2 (en)	2008-01-03	2013-10-15	The Scripps Research Institute	EFGR antibodies comprising modular recognition domains
US8454960B2 (en)	2008-01-03	2013-06-04	The Scripps Research Institute	Multispecific antibody targeting and multivalency through modular recognition domains
US8557242B2 (en)	2008-01-03	2013-10-15	The Scripps Research Institute	ERBB2 antibodies comprising modular recognition domains
SG10201605629VA (en)	2008-01-03	2016-08-30	Scripps Research Inst	Antibody targeting through a modular recognition domain
TWI472339B (zh)	2008-01-30	2015-02-11	Genentech Inc	包含結合至ｈｅｒ２結構域ii之抗體及其酸性變異體的組合物
EP4427805A2 (en)	2008-01-31	2024-09-11	Genentech, Inc.	Anti-cd79b antibodies and immunoconjugates and methods of use
ES2544682T3 (es)	2008-03-14	2015-09-02	Genentech, Inc.	Variaciones genéticas asociadas con la resistencia a fármacos
AR070865A1 (es) *	2008-03-18	2010-05-12	Genentech Inc	Combinaciones de un conjugado anticuerpo- farmaco anti- her2 y agentes quimioterapeuticos y los metodos de uso
KR101592156B1 (ko)	2008-05-23	2016-02-04	시와 코퍼레이션	재생을 촉진하는 방법, 조성물 및 장치
BRPI0812682A2 (pt)	2008-06-16	2010-06-22	Genentech Inc	tratamento de cáncer de mama metastático
JP5705115B2 (ja)	2008-09-10	2015-04-22	ジェネンテック，インコーポレイテッド	蛋白質の酸化的分解の予防のための組成物および方法
PL2396036T3 (pl)	2009-02-13	2017-12-29	Immunomedics, Inc.	Immunokoniugaty z połączeniem rozszczepialnym wewnątrzkomórkowo
AU2010226453B2 (en)	2009-03-20	2013-11-21	Genentech, Inc.	Bispecific anti-HER antibodies
RU2587621C2 (ru)	2009-04-01	2016-06-20	Дженентек, Инк.	АНТИТЕЛА К FcRH5, ИХ ИММУНОКОНЪЮГАТЫ И СПОСОБЫ ИХ ПРИМЕНЕНИЯ
MX2011010169A (es)	2009-04-07	2011-10-11	Roche Glycart Ag	Anticuerpos biespecificos anti-erbb-1/anti-c-met.
EP2436397B1 (en)	2009-05-29	2017-05-10	Chugai Seiyaku Kabushiki Kaisha	Pharmaceutical composition containing antagonist of egf family ligand as component
WO2010136569A1 (en)	2009-05-29	2010-12-02	F. Hoffmann-La Roche Ag	Modulators for her2 signaling in her2 expressing patients with gastric cancer
US8293753B2 (en)	2009-07-02	2012-10-23	Novartis Ag	Substituted 2-carboxamide cycloamino ureas
US9345661B2 (en)	2009-07-31	2016-05-24	Genentech, Inc.	Subcutaneous anti-HER2 antibody formulations and uses thereof
BR112012002974B1 (pt)	2009-08-11	2022-06-07	Genentech, Inc	Processo para produzir um anticorpo em uma célula hospedeira de célula ovário de hamster chinês (cho) expressando o referido polipeptídeo
US20110047103A1 (en) *	2009-08-15	2011-02-24	Genentech, Inc.	Anti-angiogenesis therapy for the treatment of previously treated breast cancer
JP5787891B2 (ja)	2009-09-01	2015-09-30	ジェネンテック，インコーポレイテッド	改変されたプロテインａ溶離による向上したタンパク質精製
AR078161A1 (es)	2009-09-11	2011-10-19	Hoffmann La Roche	Formulaciones farmaceuticas muy concentradas de un anticuerpo anti cd20. uso de la formulacion. metodo de tratamiento.
WO2011044368A1 (en)	2009-10-07	2011-04-14	Macrogenics, Inc.	Fc region-containing polypeptides that exhibit improved effector function due to alterations of the extent of fucosylation, and methods for their use
CA2777825A1 (en) *	2009-10-28	2011-05-19	Abbott Biotherapeutics Corp.	Anti-egfr antibodies and their uses
MX2012005168A (es)	2009-11-05	2012-06-08	Genentech Inc	Metodos y composicion para secrecion de polipeptidos heterologos.
PT3351558T (pt)	2009-11-13	2020-04-09	Daiichi Sankyo Europe Gmbh	Material e métodos para tratamento ou prevenção de doenças associadas a her-3
EP2507381A4 (en)	2009-12-04	2016-07-20	Hoffmann La Roche	PLURISPECIFIC ANTIBODIES, ANTIBODY ANALOGUES, COMPOSITIONS AND METHODS
DK2532365T3 (da) *	2010-02-04	2016-08-15	Toray Industries	Farmaceutisk sammensætning til behandling og/eller forebyggelse af kræft
PL2536748T3 (pl)	2010-02-18	2015-01-30	Genentech Inc	Antagoniści neureguliny i ich zastosowanie w leczeniu nowotworu
US8609095B2 (en)	2010-03-04	2013-12-17	Symphogen A/S	Anti-HER2 antibodies and compositions
CA2792125C (en)	2010-03-22	2019-02-12	Genentech, Inc.	Compositions and methods useful for stabilizing protein-containing formulations
JP2013525484A (ja)	2010-05-03	2013-06-20	ジェネンテック，インコーポレイテッド	タンパク質含有製剤の粘度を低減させるために有用な組成物及び方法
WO2011146568A1 (en)	2010-05-19	2011-11-24	Genentech, Inc.	Predicting response to a her inhibitor
CA2800769C (en)	2010-05-27	2021-11-02	Genmab A/S	Monoclonal antibodies against her2 epitope
CA3051311A1 (en)	2010-05-27	2011-12-01	Genmab A/S	Monoclonal antibodies against her2
CA2800728C (en)	2010-05-28	2020-10-27	Genentech, Inc.	Decreasing lactate level and increasing polypeptide production by downregulating the expression of lactate dehydrogenase and pyruvate dehydrogenase kinase
WO2011153346A1 (en)	2010-06-03	2011-12-08	Genentech, Inc.	Immuno-pet imaging of antibodies and immunoconjugates and uses therefor
CN103068406B (zh)	2010-06-08	2017-06-30	基因泰克公司	半胱氨酸改造的抗体和偶联物
CA3111727C (en)	2010-06-24	2022-07-26	Genentech, Inc.	Compositions and methods for stabilizing protein-containing formulations
US20120100166A1 (en)	2010-07-15	2012-04-26	Zyngenia, Inc.	Ang-2 Binding Complexes and Uses Thereof
AR082418A1 (es)	2010-08-02	2012-12-05	Novartis Ag	Formas cristalinas de 1-(4-metil-5-[2-(2,2,2-trifluoro-1,1-dimetil-etil)-piridin-4-il]-tiazol-2-il)-amida de 2-amida del acido (s)-pirrolidin-1,2-dicarboxilico
TW201302793A (zh)	2010-09-03	2013-01-16	Glaxo Group Ltd	新穎之抗原結合蛋白
US8721571B2 (en)	2010-11-22	2014-05-13	Siwa Corporation	Selective removal of cells having accumulated agents
US20130245233A1 (en)	2010-11-24	2013-09-19	Ming Lei	Multispecific Molecules
JP5838221B2 (ja)	2010-12-21	2016-01-06	エフ・ホフマン−ラ・ロシュ・アクチェンゲゼルシャフト	アイソフォーム濃縮抗体調製物及びこれを得る方法
WO2012085113A1 (en)	2010-12-23	2012-06-28	Roche Diagnostics Gmbh	Binding agent
JP5766296B2 (ja)	2010-12-23	2015-08-19	エフ．ホフマン−ラロシュアーゲーＦ．Ｈｏｆｆｍａｎｎ−ＬａＲｏｃｈｅＡｋｔｉｅｎｇｅｓｅｌｌｓｃｈａｆｔ	ポリペプチド−ポリヌクレオチド複合体、およびエフェクター成分の標的化された送達におけるその使用
KR101928116B1 (ko)	2011-01-31	2018-12-11	노파르티스 아게	신규 헤테로시클릭 유도체
CN103649326B (zh) *	2011-03-08	2016-08-17	宾夕法尼亚大学理事会	用于治疗和诊断用途的抗体样蛋白
AU2012245116A1 (en)	2011-04-20	2013-11-07	Genmab A/S	Bispecific antibodies against HER2 and CD3
AU2012258637B2 (en)	2011-05-24	2017-07-20	Zyngenia, Inc.	Multivalent and monovalent multispecific complexes and their uses
JP2014526891A (ja)	2011-08-17	2014-10-09	ジェネンテック，インコーポレイテッド	ニューレグリン抗体とその使用
HUE044352T2 (hu)	2011-10-14	2019-10-28	Hoffmann La Roche	Pertuzumab, Trastuzumab, Docetaxel és Carboplatin korai stádiumú mellrák kezelésére
WO2013063229A1 (en)	2011-10-25	2013-05-02	The Regents Of The University Of Michigan	Her2 targeting agent treatment in non-her2-amplified cancers having her2 expressing cancer stem cells
JP6059731B2 (ja)	2011-10-28	2017-01-11	ノバルティスアーゲー	新規プリン誘導体および疾患の処置におけるその使用
WO2013078191A1 (en)	2011-11-23	2013-05-30	Medimmune, Llc	Binding molecules specific for her3 and uses thereof
AU2012346540C1 (en)	2011-11-30	2019-07-04	Genentech, Inc.	ErbB3 mutations in cancer
EP2788500A1 (en)	2011-12-09	2014-10-15	F.Hoffmann-La Roche Ag	Identification of non-responders to her2 inhibitors
CA2859376C (en)	2011-12-22	2022-04-19	Genentech, Inc.	Use of ion exchange chromatography for improving downstream chromatography steps for purification of antibodies
TWI593705B (zh)	2011-12-28	2017-08-01	Chugai Pharmaceutical Co Ltd	Humanized anti-epiregulin antibody and cancer therapeutic agent containing the antibody as an active ingredient
KR20140117644A (ko)	2012-01-31	2014-10-07	스미스클라인 비이참 (코르크) 리미티드	암을 치료하는 방법
EP2638916A1 (en)	2012-03-16	2013-09-18	Covagen AG	Novel binding molecules with antitumoral activity
SG11201406079TA (en)	2012-03-27	2014-10-30	Genentech Inc	Diagnosis and treatments relating to her3 inhibitors
NZ799532A (en)	2012-04-20	2023-07-28	Merus Nv	Methods and means for the production of ig-like molecules
KR101505157B1 (ko)	2012-05-08	2015-03-24	주식회사 종근당	항―ＥｒｂＢ２ 항체 변이체
KR20150009540A (ko)	2012-05-16	2015-01-26	노파르티스 아게	Pi-3 키나제 억제제에 대한 투여 요법
CA2889298C (en)	2012-11-30	2024-01-02	Anton Belousov	Identification of patients in need of pd-l1 inhibitor cotherapy
ES2651331T3 (es)	2013-01-10	2018-01-25	Glaxosmithkline Intellectual Property (No. 2) Limited	Inhibidores de la sintasa de ácidos grasos
AR094403A1 (es)	2013-01-11	2015-07-29	Hoffmann La Roche	Terapia de combinación de anticuerpos anti-her3
CA2907181C (en)	2013-03-15	2023-10-17	Viktor Roschke	Multivalent and monovalent multispecific complexes and their uses
CN104628846B (zh)	2013-11-06	2019-12-06	三生国健药业（上海）股份有限公司	重组蛋白质的纯化方法
DK3072907T3 (da) *	2013-11-19	2019-04-01	Remegen Ltd	Anti-her2- antistof og konjugat deraf
CA2931356A1 (en) *	2013-11-27	2015-06-04	Zymeworks Inc.	Bispecific antigen-binding constructs targeting her2
JP2016539149A (ja)	2013-12-06	2016-12-15	ノバルティスアーゲー	アルファ−アイソフォーム選択的ホスファチジルイノシトール３−キナーゼ阻害剤の投薬レジメン
KR20230162159A (ko)	2014-01-31	2023-11-28	다이이찌 산쿄 가부시키가이샤	항-her2 항체-약물 접합체
EP3111222A1 (en)	2014-02-26	2017-01-04	Glaxosmithkline Intellectual Property (No. 2) Limited	Methods of treating cancer patients responding to ezh2 inhibitor gsk126
ES2897765T3 (es)	2014-03-14	2022-03-02	Hoffmann La Roche	Procedimientos y composiciones para la secreción de polipéptidos heterólogos
TW201542594A (zh)	2014-04-11	2015-11-16	Medimmune Llc	雙特異性ｈｅｒ２抗體
SG11201701128YA (en)	2014-09-12	2017-03-30	Genentech Inc	Cysteine engineered antibodies and conjugates
JP6976847B2 (ja)	2014-09-19	2021-12-08	シワコーポレイション	炎症及び自己免疫障害を治療するための抗ａｇｅ抗体
US10385380B2 (en)	2014-10-02	2019-08-20	The Regents Of The University Of California	Personalized protease assay to measure protease activity in neoplasms
US10358502B2 (en)	2014-12-18	2019-07-23	Siwa Corporation	Product and method for treating sarcopenia
US9993535B2 (en)	2014-12-18	2018-06-12	Siwa Corporation	Method and composition for treating sarcopenia
MA41414A (fr)	2015-01-28	2017-12-05	Centre Nat Rech Scient	Protéines de liaison agonistes d' icos
KR101515535B1 (ko)	2015-01-28	2015-05-06	주식회사 종근당	항―ＥｒｂＢ２ 항체 변이체
AU2016262168B2 (en) *	2015-05-13	2022-06-23	Zymeworks Bc Inc.	Antigen-binding constructs targeting HER2
WO2017025871A1 (en)	2015-08-07	2017-02-16	Glaxosmithkline Intellectual Property Development Limited	Combination therapy comprising anti ctla-4 antibodies
AU2016336959A1 (en) *	2015-10-13	2018-04-12	Siwa Corporation	Anti-age antibodies and methods of use thereof
US20180280370A1 (en)	2015-11-02	2018-10-04	Novartis Ag	Dosage regimen for a phosphatidylinositol 3-kinase inhibitor
CN106729743B (zh)	2015-11-23	2021-09-21	四川科伦博泰生物医药股份有限公司	抗ErbB2抗体-药物偶联物及其组合物、制备方法和应用
CN108884161A (zh)	2015-12-01	2018-11-23	葛兰素史密斯克莱知识产权发展有限公司	联合治疗及其用途和方法
EA201891178A1 (ru)	2015-12-14	2019-01-31	Макродженикс, Инк.	Биспецифичные молекулы, обладающие иммунореактивностью в отношении pd-1 и ctla-4, и способы их применения
CN105646704B (zh) *	2015-12-28	2019-11-15	广西医科大学	抗p185erbB2人鼠嵌合抗体ChAb26、乳腺特异性表达载体、转基因FVB小鼠及其制备方法
KR20230074837A (ko)	2016-02-19	2023-05-31	시와 코퍼레이션	고급 당화 최종 산물(age)에 대한 항체를 사용하여 암을 치료하고, 전이성 암 세포를 사멸시키고, 암 전이를 예방하기 위한 방법 및 조성물
EP3429623A1 (en) *	2016-03-15	2019-01-23	Merrimack Pharmaceuticals, Inc.	Methods for treating er+, her2-, hrg+ breast cancer using combination therapies comprising an anti-erbb3 antibody
WO2017181116A1 (en)	2016-04-15	2017-10-19	Siwa Corporation	Anti-age antibodies for treating neurodegenerative disorders
EP3454863A1 (en)	2016-05-10	2019-03-20	INSERM (Institut National de la Santé et de la Recherche Médicale)	Combinations therapies for the treatment of cancer
EP3455260B1 (en) *	2016-05-12	2022-07-06	Agency for Science, Technology and Research	Anti-erbb-2 antibodies and uses thereof
JP2019518763A (ja)	2016-06-23	2019-07-04	シワコーポレーション	様々な疾患及び障害の治療において使用するためのワクチン
WO2018060833A1 (en)	2016-09-27	2018-04-05	Novartis Ag	Dosage regimen for alpha-isoform selective phosphatidylinositol 3-kinase inhibitor alpelisib
KR20230158641A (ko)	2016-10-07	2023-11-20	다이이찌 산쿄 가부시키가이샤	항 her2 항체-약물 콘주게이트 투여에 의한 내성암의 치료
CN110049779A (zh)	2016-12-12	2019-07-23	第一三共株式会社	抗体-药物缀合物和免疫检查点抑制剂的组合
US10961321B1 (en)	2017-01-06	2021-03-30	Siwa Corporation	Methods and compositions for treating pain associated with inflammation
US10925937B1 (en)	2017-01-06	2021-02-23	Siwa Corporation	Vaccines for use in treating juvenile disorders associated with inflammation
US10858449B1 (en)	2017-01-06	2020-12-08	Siwa Corporation	Methods and compositions for treating osteoarthritis
US10995151B1 (en)	2017-01-06	2021-05-04	Siwa Corporation	Methods and compositions for treating disease-related cachexia
US11390685B2 (en)	2017-01-06	2022-07-19	Biosion, Inc.	ErbB2 antibodies and uses therefore
CA3053803A1 (en)	2017-02-24	2018-08-30	Macrogenics, Inc.	Bispecific binding molecules that are capable of binding cd137 and tumor antigens, and uses thereof
WO2018160138A1 (en)	2017-03-02	2018-09-07	Aslan Pharmaceuticals Pte Ltd	Dhodh inhibitor for treating haematological cancer
WO2018160654A2 (en)	2017-03-02	2018-09-07	Genentech, Inc.	Adjuvant treatment of her2-positive breast cancer
CA3056248A1 (en)	2017-03-22	2018-09-27	Genentech, Inc.	Optimized antibody compositions for treatment of ocular disorders
US10919957B2 (en)	2017-04-13	2021-02-16	Siwa Corporation	Humanized monoclonal advanced glycation end-product antibody
WO2018222135A1 (en)	2017-06-02	2018-12-06	Aslan Pharmaceuticals Pte Ltd	Cancer therapy
CN107417791B (zh) *	2017-08-17	2020-09-22	合肥瀚科迈博生物技术有限公司	抗人ErbB2双特异性抗体、其制备方法及用途
CN118767159A (zh)	2017-08-23	2024-10-15	第一三共株式会社	抗体-药物缀合物制剂及其冻干
CN117838881A (zh)	2017-08-31	2024-04-09	第一三共株式会社	制备抗体-药物缀合物的新方法
EP3677589A4 (en)	2017-08-31	2021-04-21	Daiichi Sankyo Company, Limited	IMPROVED PROCESS FOR PREPARING ANTIBODY-ACTIVE CONJUGATE
CN107789631B (zh) *	2017-11-03	2021-03-16	合肥瀚科迈博生物技术有限公司	抗人ErbB2双表位抗体-药物偶联物及其应用
RU2020122822A (ru)	2017-12-12	2022-01-13	Макродженикс, Инк.	Биспецифичные связывающие cd16 молекулы и их применение при лечении заболеваний
US11518801B1 (en)	2017-12-22	2022-12-06	Siwa Corporation	Methods and compositions for treating diabetes and diabetic complications
WO2019160904A1 (en)	2018-02-15	2019-08-22	Macrogenics, Inc.	Variant cd3-binding domains and their use in combination therapies for the treatment of disease
EP3560945A1 (en)	2018-04-27	2019-10-30	F. Hoffmann-La Roche AG	Methods for purification of polypeptides using polysorbates
SG11202011243XA (en)	2018-05-28	2020-12-30	Daiichi Sankyo Co Ltd	Treatment of her2-mutated cancer by administering anti-her2 antibody-drug conjugate
CN118512453A (zh)	2018-07-23	2024-08-20	特雷维治疗股份有限公司	慢性咳嗽、呼吸急促和呼吸困难的治疗
US20210283269A1 (en)	2018-07-25	2021-09-16	Daiichi Sankyo Company, Limited	Effective method for manufacturing antibody-drug conjugate
US20210169852A1 (en)	2018-07-27	2021-06-10	Daiichi Sankyo Company, Limited	Protein recognizing drug moiety of antibody-drug conjugate
AU2019315177A1 (en)	2018-07-31	2021-02-25	Daiichi Sankyo Company, Limited	Treatment of metastatic brain tumor by administration of antibody-drug conjugate
CA3108754A1 (en)	2018-08-06	2020-02-13	Daiichi Sankyo Company, Limited	Combination of antibody-drug conjugate and tubulin inhibitor
US20210340628A1 (en)	2018-08-23	2021-11-04	Daiichi Sankyo Company, Limited	Sensitivity marker for antibody-drug conjugate
AU2019349934A1 (en)	2018-09-25	2021-05-13	Absci Corporation	Protein purification methods
WO2020084503A1 (en)	2018-10-26	2020-04-30	Cadila Healthcare Limited	A composition comprising antibody with reduced level of basic variants thereof
TW202034959A (zh)	2018-12-11	2020-10-01	日商第一三共股份有限公司	抗體-藥物結合物與parp抑制劑之組合
EP3903828A4 (en)	2018-12-21	2022-10-05	Daiichi Sankyo Company, Limited	COMBINATION OF AN ANTIBODY-DRUG CONJUGATE AND A KINASE INHIBITOR
WO2020160365A1 (en)	2019-02-01	2020-08-06	Glaxosmithkline Intellectual Property Development Limited	Belantamab mafodotin in combination with pembrolizumab for treating cancer
EP3946457A1 (en)	2019-04-01	2022-02-09	Genentech, Inc.	Compositions and methods for stabilizing protein-containing formulations
CN112007169B (zh) *	2019-05-30	2022-03-08	湖南大学	一种核酸适配体药物偶联物及其制备方法和用途
CN110205302B (zh) *	2019-06-24	2021-03-23	扬州大学	一株分泌抗麦考酚酸单克隆抗体的细胞株、其单克隆抗体及其应用
KR20220026585A (ko)	2019-06-26	2022-03-04	글락소스미스클라인 인털렉츄얼 프로퍼티 디벨로프먼트 리미티드	Il1rap 결합 단백질
CN110551214A (zh) *	2019-08-27	2019-12-10	杨澜	一种人源化抗Periostin单克隆抗体、及其制备方法和应用
JP2023512023A (ja)	2020-01-28	2023-03-23	グラクソスミスクライン、インテレクチュアル、プロパティー、ディベロップメント、リミテッド	併用療法及びその使用及び方法
EP4171650A1 (en)	2020-06-24	2023-05-03	AstraZeneca UK Limited	Combination of antibody-drug conjugate and atr inhibitor
WO2021260583A1 (en)	2020-06-24	2021-12-30	Astrazeneca Uk Limited	Combination of antibody-drug conjugate and dna-pk inhibitor
CN116615248A (zh)	2020-06-24	2023-08-18	阿斯利康(英国)有限公司	抗体-药物缀合物和cdk9抑制剂的组合
WO2021260582A1 (en)	2020-06-24	2021-12-30	Astrazeneca Uk Limited	Combination of antibody-drug conjugate and aurora b inhibitor
CN116194109A (zh)	2020-06-24	2023-05-30	阿斯利康(英国)有限公司	抗体-药物缀合物和atm抑制剂的组合
BR112023000982A2 (pt)	2020-07-20	2023-03-28	Daiichi Sankyo Co Ltd	Composição farmacêutica, e, método de tratamento
BR112023006337A2 (pt)	2020-10-09	2023-05-09	Astrazeneca Uk Ltd	Produto farmacêutico, uso de um conjugado anticorpo anti-her2-fármaco ou um inibidor seletivo de parp1, e, método de tratamento do câncer
KR20230106645A (ko)	2020-11-11	2023-07-13	다이이찌 산쿄 가부시키가이샤	항체-약물 콘주게이트와 항 SIRPα 항체의 조합
JPWO2023100829A1 (da)	2021-11-30	2023-06-08
TW202333800A (zh)	2021-12-28	2023-09-01	英商阿斯特捷利康英國股份有限公司	抗體-藥物結合物及rasg12c抑制劑之組合
JPWO2023153442A1 (da)	2022-02-09	2023-08-17
AU2023262308A1 (en)	2022-04-27	2024-10-03	Astrazeneca Uk Limited	Combination of antibody-drug conjugate with ezh1 and/or ezh2 inhibitor
WO2023218378A1 (en)	2022-05-11	2023-11-16	Daiichi Sankyo Company, Limited	Combination of an antibody specific for a tumor antigen and a cd47 inhibitor
WO2024023750A1 (en)	2022-07-28	2024-02-01	Astrazeneca Uk Limited	Combination of antibody-drug conjugate and bispecific checkpoint inhibitor
CN117224689B (zh) *	2023-11-16	2024-02-23	上海复宏汉霖生物技术股份有限公司	联合抗her2抗体和化疗剂治疗胃癌的用途

Family Cites Families (105)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US3773919A (en)	1969-10-23	1973-11-20	Du Pont	Polylactide-drug mixtures
CU22545A1 (es)	1994-11-18	1999-03-31	Centro Inmunologia Molecular	Obtención de un anticuerpo quimérico y humanizado contra el receptor del factor de crecimiento epidérmico para uso diagnóstico y terapéutico
USRE30985E (en)	1978-01-01	1982-06-29		Serum-free cell culture media
FR2413974A1 (fr)	1978-01-06	1979-08-03	David Bernard	Sechoir pour feuilles imprimees par serigraphie
US4275149A (en)	1978-11-24	1981-06-23	Syva Company	Macromolecular environment control in specific receptor assays
US4318980A (en)	1978-04-10	1982-03-09	Miles Laboratories, Inc.	Heterogenous specific binding assay employing a cycling reactant as label
WO1981001145A1 (en)	1979-10-18	1981-04-30	Univ Illinois	Hydrolytic enzyme-activatible pro-drugs
US4419446A (en)	1980-12-31	1983-12-06	The United States Of America As Represented By The Department Of Health And Human Services	Recombinant DNA process utilizing a papilloma virus DNA as a vector
US4485045A (en)	1981-07-06	1984-11-27	Research Corporation	Synthetic phosphatidyl cholines useful in forming liposomes
NZ201705A (en)	1981-08-31	1986-03-14	Genentech Inc	Recombinant dna method for production of hepatitis b surface antigen in yeast
US4601978A (en)	1982-11-24	1986-07-22	The Regents Of The University Of California	Mammalian metallothionein promoter system
US4560655A (en)	1982-12-16	1985-12-24	Immunex Corporation	Serum-free cell culture medium and process for making same
US4657866A (en)	1982-12-21	1987-04-14	Sudhir Kumar	Serum-free, synthetic, completely chemically defined tissue culture media
US4816567A (en)	1983-04-08	1989-03-28	Genentech, Inc.	Recombinant immunoglobin preparations
DD266710A3 (de)	1983-06-06	1989-04-12	Ve Forschungszentrum Biotechnologie	Verfahren zur biotechnischen Herstellung van alkalischer Phosphatase
US4544545A (en)	1983-06-20	1985-10-01	Trustees University Of Massachusetts	Liposomes containing modified cholesterol for organ targeting
US4767704A (en)	1983-10-07	1988-08-30	Columbia University In The City Of New York	Protein-free culture medium
WO1985003357A1 (en)	1984-01-30	1985-08-01	Icrf Patents Ltd.	Improvements relating to growth factors
US4943533A (en)	1984-03-01	1990-07-24	The Regents Of The University Of California	Hybrid cell lines that produce monoclonal antibodies to epidermal growth factor receptor
US4965199A (en)	1984-04-20	1990-10-23	Genentech, Inc.	Preparation of functional human factor VIII in mammalian cells using methotrexate based selection
US4879231A (en)	1984-10-30	1989-11-07	Phillips Petroleum Company	Transformation of yeasts of the genus pichia
US4737456A (en)	1985-05-09	1988-04-12	Syntex (U.S.A.) Inc.	Reducing interference in ligand-receptor binding assays
GB8516415D0 (en)	1985-06-28	1985-07-31	Celltech Ltd	Culture of animal cells
US4676980A (en)	1985-09-23	1987-06-30	The United States Of America As Represented By The Secretary Of The Department Of Health And Human Services	Target specific cross-linked heteroantibodies
US4927762A (en)	1986-04-01	1990-05-22	Cell Enterprises, Inc.	Cell culture medium with antioxidant
GB8610600D0 (en)	1986-04-30	1986-06-04	Novo Industri As	Transformation of trichoderma
US5401638A (en)	1986-06-04	1995-03-28	Oncogene Science, Inc.	Detection and quantification of neu related proteins in the biological fluids of humans
US5567610A (en)	1986-09-04	1996-10-22	Bioinvent International Ab	Method of producing human monoclonal antibodies and kit therefor
US4968603A (en)	1986-12-31	1990-11-06	The Regents Of The University Of California	Determination of status in neoplastic disease
IL85035A0 (en)	1987-01-08	1988-06-30	Int Genetic Eng	Polynucleotide molecule,a chimeric antibody with specificity for human b cell surface antigen,a process for the preparation and methods utilizing the same
GB8705477D0 (en)	1987-03-09	1987-04-15	Carlton Med Prod	Drug delivery systems
US4975278A (en)	1988-02-26	1990-12-04	Bristol-Myers Company	Antibody-enzyme conjugates in combination with prodrugs for the delivery of cytotoxic agents to tumor cells
US5283187A (en)	1987-11-17	1994-02-01	Brown University Research Foundation	Cell culture-containing tubular capsule produced by co-extrusion
US4892538A (en)	1987-11-17	1990-01-09	Brown University Research Foundation	In vivo delivery of neurotransmitters by implanted, encapsulated cells
US5824311A (en)	1987-11-30	1998-10-20	Trustees Of The University Of Pennsylvania	Treatment of tumors with monoclonal antibodies against oncogene antigens
US5720937A (en) *	1988-01-12	1998-02-24	Genentech, Inc.	In vivo tumor detection assay
WO1989006692A1 (en) *	1988-01-12	1989-07-27	Genentech, Inc.	Method of treating tumor cells by inhibiting growth factor receptor function
WO1990003430A1 (en)	1988-09-23	1990-04-05	Cetus Corporation	Cell culture medium for enhanced cell growth, culture longevity and product expression
GB8823869D0 (en)	1988-10-12	1988-11-16	Medical Res Council	Production of antibodies
US5175384A (en)	1988-12-05	1992-12-29	Genpharm International	Transgenic mice depleted in mature t-cells and methods for making transgenic mice
FR2646437B1 (fr)	1989-04-28	1991-08-30	Transgene Sa	Nouvelles sequences d'adn, leur application en tant que sequence codant pour un peptide signal pour la secretion de proteines matures par des levures recombinantes, cassettes d'expression, levures transformees et procede de preparation de proteines correspondant
EP0474727B1 (en)	1989-05-19	1997-07-23	Genentech, Inc.	Her2 extracellular domain
EP0402226A1 (en)	1989-06-06	1990-12-12	Institut National De La Recherche Agronomique	Transformation vectors for yeast yarrowia
DE3920358A1 (de)	1989-06-22	1991-01-17	Behringwerke Ag	Bispezifische und oligospezifische, mono- und oligovalente antikoerperkonstrukte, ihre herstellung und verwendung
ATE144793T1 (de)	1989-06-29	1996-11-15	Medarex Inc	Bispezifische reagenzien für die aids-therapie
ATE135373T1 (de)	1989-09-08	1996-03-15	Univ Johns Hopkins	Modifikationen der struktur des egf-rezeptor-gens in menschlichen glioma
DE68926248T2 (de)	1989-09-29	1996-12-19	Oncogene Science Inc	p100 "neu" menschlisches Protein and Verwendung dieses Proteins zum Nachweis von preneoplasmatischen- oder neoplasmatischen beim Menschen
US5013556A (en)	1989-10-20	1991-05-07	Liposome Technology, Inc.	Liposomes with enhanced circulation time
CA2026147C (en) *	1989-10-25	2006-02-07	Ravi J. Chari	Cytotoxic agents comprising maytansinoids and their therapeutic use
US5208020A (en)	1989-10-25	1993-05-04	Immunogen Inc.	Cytotoxic agents comprising maytansinoids and their therapeutic use
US5183884A (en)	1989-12-01	1993-02-02	United States Of America	Dna segment encoding a gene for a receptor related to the epidermal growth factor receptor
US5229275A (en)	1990-04-26	1993-07-20	Akzo N.V.	In-vitro method for producing antigen-specific human monoclonal antibodies
US5122469A (en)	1990-10-03	1992-06-16	Genentech, Inc.	Method for culturing Chinese hamster ovary cells to improve production of recombinant proteins
US5571894A (en)	1991-02-05	1996-11-05	Ciba-Geigy Corporation	Recombinant antibodies specific for a growth factor receptor
EP0586505A1 (en)	1991-05-14	1994-03-16	Repligen Corporation	Heteroconjugate antibodies for treatment of hiv infection
IL101943A0 (en)	1991-05-24	1992-12-30	Genentech Inc	Structure,production and use of heregulin
EP0940468A1 (en)	1991-06-14	1999-09-08	Genentech, Inc.	Humanized antibody variable domain
US5264586A (en)	1991-07-17	1993-11-23	The Scripps Research Institute	Analogs of calicheamicin gamma1I, method of making and using the same
US5565332A (en)	1991-09-23	1996-10-15	Medical Research Council	Production of chimeric antibodies - a combinatorial approach
WO1994000136A1 (en)	1992-06-30	1994-01-06	Oncologix, Inc.	A COMBINATION OF ANTI-erbB-2 MONOCLONAL ANTIBODIES AND METHOD OF USING
US5587458A (en)	1991-10-07	1996-12-24	Aronex Pharmaceuticals, Inc.	Anti-erbB-2 antibodies, combinations thereof, and therapeutic and diagnostic uses thereof
WO1993008829A1 (en)	1991-11-04	1993-05-13	The Regents Of The University Of California	Compositions that mediate killing of hiv-infected cells
EP0617706B1 (en)	1991-11-25	2001-10-17	Enzon, Inc.	Multivalent antigen-binding proteins
EP0625200B1 (en)	1992-02-06	2005-05-11	Chiron Corporation	Biosynthetic binding protein for cancer marker
DE69333082T2 (de)	1992-02-11	2004-05-06	Cell Genesys, Inc., Foster City	Erzielen von homozygotem durch zielgerichtete genetische ereignisse
US5573905A (en)	1992-03-30	1996-11-12	The Scripps Research Institute	Encoded combinatorial chemical libraries
AU4025193A (en)	1992-04-08	1993-11-18	Cetus Oncology Corporation	Humanized C-erbB-2 specific antibodies
ZA932522B (en)	1992-04-10	1993-12-20	Res Dev Foundation	Immunotoxins directed against c-erbB-2(HER/neu) related surface antigens
EP0646178A1 (en)	1992-06-04	1995-04-05	The Regents Of The University Of California	expression cassette with regularoty regions functional in the mammmlian host
EP0656064B1 (en)	1992-08-17	1997-03-05	Genentech, Inc.	Bispecific immunoadhesins
FR2697752B1 (fr) *	1992-11-10	1995-04-14	Rhone Poulenc Rorer Sa	Compositions antitumorales contenant des dérivés du taxane.
RU2139731C1 (ru)	1992-11-13	1999-10-20	Айдек Фармасьютикалс Корпорейшн (US	Способ лечения, антитела, гибридома
CA2103323A1 (en)	1992-11-24	1994-05-25	Gregory D. Plowman	Her4 human receptor tyrosine kinase
DK0616812T3 (da)	1993-03-24	2000-04-25	Berlex Biosciences	Kombination af antihormonforbindelser og bindingsmolekyler til behandling af cancer
WO1994022478A1 (en)	1993-03-30	1994-10-13	The Trustees Of The University Of Pennsylvania	PREVENTION OF TUMORS WITH MONOCLONAL ANTIBODIES AGAINST $i(NEU)
AU697142B2 (en)	1993-11-23	1998-10-01	Genentech Inc.	Protein tyrosine kinases named Rse
ES2166368T3 (es)	1993-12-24	2002-04-16	Merck Patent Gmbh	Inmunoconjugados.
US5773001A (en)	1994-06-03	1998-06-30	American Cyanamid Company	Conjugates of methyltrithio antitumor agents and intermediates for their synthesis
US5910486A (en)	1994-09-06	1999-06-08	Uab Research Foundation	Methods for modulating protein function in cells using, intracellular antibody homologues
US6214388B1 (en)	1994-11-09	2001-04-10	The Regents Of The University Of California	Immunoliposomes that optimize internalization into target cells
WO1996016673A1 (en)	1994-12-02	1996-06-06	Chiron Corporation	Method of promoting an immune response with a bispecific antibody
US5731168A (en)	1995-03-01	1998-03-24	Genentech, Inc.	Method for making heteromultimeric polypeptides
US5641870A (en)	1995-04-20	1997-06-24	Genentech, Inc.	Low pH hydrophobic interaction chromatography for antibody purification
US5739277A (en)	1995-04-14	1998-04-14	Genentech Inc.	Altered polypeptides with increased half-life
US5837234A (en)	1995-06-07	1998-11-17	Cytotherapeutics, Inc.	Bioartificial organ containing cells encapsulated in a permselective polyether suflfone membrane
US5714586A (en)	1995-06-07	1998-02-03	American Cyanamid Company	Methods for the preparation of monomeric calicheamicin derivative/carrier conjugates
CA2222231A1 (en)	1995-06-07	1996-12-19	Imclone Systems Incorporated	Antibody and antibody fragments for inhibiting the growth of tumors
US5712374A (en)	1995-06-07	1998-01-27	American Cyanamid Company	Method for the preparation of substantiallly monomeric calicheamicin derivative/carrier conjugates
EP0873363B1 (en)	1995-06-14	2010-10-06	The Regents of The University of California	High affinity human antibodies to tumor antigens
CN1151842C (zh)	1995-07-27	2004-06-02	基因技术股份有限公司	稳定等渗的冻干蛋白制剂
US5783186A (en)	1995-12-05	1998-07-21	Amgen Inc.	Antibody-induced apoptosis
US5922845A (en)	1996-07-11	1999-07-13	Medarex, Inc.	Therapeutic multispecific compounds comprised of anti-Fcα receptor antibodies
WO1998002541A1 (en) *	1996-07-12	1998-01-22	Genentech, Inc.	Gamma-heregulin
DE69739181D1 (de) *	1996-08-12	2009-02-05	Celgene Corp	Neue immunotherapeutische Mittel und deren Verwendung in der Reduzierung von Cytokinenspiegel
JP2001504326A (ja) *	1996-10-18	2001-04-03	ジェネンテックインコーポレーテッド	抗ＥｒｂＢ２抗体
US5994071A (en)	1997-04-04	1999-11-30	Albany Medical College	Assessment of prostate cancer
US6235883B1 (en)	1997-05-05	2001-05-22	Abgenix, Inc.	Human monoclonal antibodies to epidermal growth factor receptor
AU9805398A (en)	1997-10-15	1999-05-03	Children's Medical Center Corporation	Novel human egf receptors and use thereof
ZA9811162B (en) *	1997-12-12	2000-06-07	Genentech Inc	Treatment with anti-ERBB2 antibodies.
US6316462B1 (en) *	1999-04-09	2001-11-13	Schering Corporation	Methods of inducing cancer cell death and tumor regression
DK1187632T3 (da) *	1999-05-14	2009-04-06	Genentech Inc	Behandling med anti-ErbB2-antistoffer
CA2370466C (en) *	1999-06-25	2011-02-08	Sharon Erickson	Methods of treatment using anti-erbb antibody-maytansinoid conjugates
CH694589A5 (de) *	1999-06-25	2005-04-15	Genentech Inc	Humanisierte Anti-ErbB2-Antikörper und Behandlung mit Anti-ErbB2-Antikörpern.
PT1189634E (pt) *	1999-06-25	2007-06-06	Genentech Inc	Tratamento de cancro da próstata com anticorpos anti-erbb2.
IL148114A0 (en) *	1999-08-27	2002-09-12	Genentech Inc	DOSAGES FOR TREATMENT WITH ANTI-ErbB2 ANTIBODIES

2000
- 2000-06-23 CH CH02367/01A patent/CH694589A5/de not_active IP Right Cessation
- 2000-06-23 GB GB0200506A patent/GB2368796B/en not_active Expired - Lifetime
- 2000-06-23 BR BR122014028365A patent/BR122014028365B8/pt active IP Right Grant
- 2000-06-23 CN CNA2007101411114A patent/CN101121750A/zh active Pending
- 2000-06-23 SI SI200031080T patent/SI2283867T1/sl unknown
- 2000-06-23 PT PT00943115T patent/PT1189641E/pt unknown
- 2000-06-23 NZ NZ531426A patent/NZ531426A/en not_active IP Right Cessation
- 2000-06-23 DE DE60042648T patent/DE60042648D1/de not_active Expired - Lifetime
- 2000-06-23 EP EP09007811A patent/EP2112167A3/en not_active Withdrawn
- 2000-06-23 ES ES00943115T patent/ES2329437T3/es not_active Expired - Lifetime
- 2000-06-23 MX MXPA01013458A patent/MXPA01013458A/es active IP Right Grant
- 2000-06-23 AU AU57632/00A patent/AU784045B2/en active Active
- 2000-06-23 KR KR1020077020771A patent/KR100797308B1/ko active IP Right Review Request
- 2000-06-23 BR BRPI0012198A patent/BRPI0012198B8/pt not_active IP Right Cessation
- 2000-06-23 CN CN200910126199.1A patent/CN101518653B/zh not_active Expired - Lifetime
- 2000-06-23 CN CN2007101411129A patent/CN101121021B/zh not_active Expired - Lifetime
- 2000-06-23 CN CNB008118981A patent/CN100340575C/zh not_active Expired - Lifetime
- 2000-06-23 CA CA002376596A patent/CA2376596C/en not_active Expired - Lifetime
- 2000-06-23 HU HU0201695A patent/HU226742B1/hu active Protection Beyond IP Right Term
- 2000-06-23 GE GEAP200011523A patent/GEP20104998B/en unknown
- 2000-06-23 DE DE10084743T patent/DE10084743T1/de not_active Withdrawn
- 2000-06-23 PL PL352321A patent/PL204629B1/pl unknown
- 2000-06-23 CA CA2727172A patent/CA2727172A1/en not_active Abandoned
- 2000-06-23 DK DK00943115.6T patent/DK1189641T5/da active
- 2000-06-23 KR KR1020017016490A patent/KR100850389B1/ko active Protection Beyond IP Right Term
- 2000-06-23 AR ARP000103157A patent/AR024464A1/es active IP Right Grant
- 2000-06-23 NZ NZ516830A patent/NZ516830A/en not_active IP Right Cessation
- 2000-06-23 AT AT0911000A patent/AT500848B1/de not_active IP Right Cessation
- 2000-06-23 SI SI200031040T patent/SI1189641T1/sl unknown
- 2000-06-23 CZ CZ20014596A patent/CZ299702B6/cs unknown
- 2000-06-23 EP EP00943115A patent/EP1189641B1/en not_active Expired - Lifetime
- 2000-06-23 TR TR2001/03756T patent/TR200103756T2/xx unknown
- 2000-06-23 IL IL14695400A patent/IL146954A0/xx unknown
- 2000-06-23 PL PL384502A patent/PL203326B1/pl unknown
- 2000-06-23 WO PCT/US2000/017366 patent/WO2001000245A2/en active IP Right Grant
- 2000-06-23 SI SI200031088T patent/SI2283866T1/sl unknown
- 2000-06-23 RU RU2002100905/15A patent/RU2270029C2/ru active Protection Beyond IP Right Term
- 2000-06-23 AT AT00943115T patent/ATE437655T1/de active
- 2000-06-23 JP JP2001505952A patent/JP4283474B2/ja not_active Expired - Lifetime
2001
- 2001-11-28 ZA ZA200109786A patent/ZA200109786B/en unknown
- 2001-12-06 IL IL146954A patent/IL146954A/en active Protection Beyond IP Right Term
- 2001-12-13 ZA ZA200110263A patent/ZA200110263B/xx unknown
- 2001-12-21 NO NO20016329A patent/NO328377B1/no not_active IP Right Cessation
2002
- 2002-08-08 HK HK02105805.2A patent/HK1044888A1/xx not_active IP Right Cessation
2005
- 2005-10-25 RU RU2005132788/15A patent/RU2430739C9/ru active
- 2005-12-07 AU AU2005242195A patent/AU2005242195B2/en not_active Expired
2008
- 2008-12-26 JP JP2008333670A patent/JP2009142280A/ja not_active Withdrawn
2009
- 2009-03-03 IL IL197359A patent/IL197359A0/en unknown
- 2009-05-05 NO NO20091792A patent/NO336040B1/no not_active IP Right Cessation
- 2009-10-20 CY CY20091101084T patent/CY1109525T1/el unknown
2013
- 2013-03-07 LU LU92164C patent/LU92164I2/fr unknown
- 2013-03-08 BE BE2013C020C patent/BE2013C020I2/fr unknown
- 2013-03-08 FR FR13C0016C patent/FR13C0016I2/fr active Active
- 2013-03-11 CY CY2013010C patent/CY2013010I1/el unknown
- 2013-03-12 NO NO2013005C patent/NO2013005I1/no not_active IP Right Cessation

Also Published As

Publication number	Publication date
DK1189641T5 (da)	2011-04-11
NZ516830A (en)	2004-07-30
HUP0201695A3 (en)	2005-06-28
NO20016329L (no)	2002-02-25
GB2368796A (en)	2002-05-15
BR122014028365B1 (pt)	2020-01-28
BRPI0012198B1 (pt)	2016-12-20
NO336040B1 (no)	2015-04-27
JP2003503366A (ja)	2003-01-28
CN101518653A (zh)	2009-09-02
KR100850389B1 (ko)	2008-08-04
BE2013C020I2 (da)	2019-08-21
RU2270029C2 (ru)	2006-02-20
AU784045B2 (en)	2006-01-19
AU2005242195A1 (en)	2006-01-12
CH694589A5 (de)	2005-04-15
CN101121750A (zh)	2008-02-13
CN1370082A (zh)	2002-09-18
ZA200110263B (en)	2003-02-26
CY1109525T1 (el)	2014-08-13
TR200103756T2 (tr)	2002-06-21
IL146954A0 (en)	2002-08-14
BR122014028365B8 (pt)	2021-07-06
JP4283474B2 (ja)	2009-06-24
KR100797308B1 (ko)	2008-01-23
AU5763200A (en)	2001-01-31
AT500848B1 (de)	2008-01-15
EP1189641B1 (en)	2009-07-29
FR13C0016I1 (da)	2013-04-12
NO20016329D0 (no)	2001-12-21
PL352321A1 (en)	2003-08-11
IL197359A0 (en)	2011-07-31
BRPI0012198B8 (pt)	2021-05-25
HK1044888A1 (en)	2002-11-08
HUP0201695A2 (en)	2002-09-28
GB0200506D0 (en)	2002-02-27
JP2009142280A (ja)	2009-07-02
CZ299702B6 (cs)	2008-10-22
GEP20104998B (en)	2010-06-10
GB2368796B (en)	2004-08-04
CA2376596C (en)	2009-10-06
CN101518653B (zh)	2015-08-19
NZ531426A (en)	2005-10-28
WO2001000245A2 (en)	2001-01-04
CN100340575C (zh)	2007-10-03
EP2112167A3 (en)	2010-12-22
AR024464A1 (es)	2002-10-02
FR13C0016I2 (fr)	2014-05-16
RU2430739C2 (ru)	2011-10-10
NO20091792L (no)	2002-02-25
PL203326B1 (pl)	2009-09-30
WO2001000245A3 (en)	2001-10-25
CY2013010I2 (el)	2015-08-05
HU226742B1 (en)	2009-08-28
PL204629B1 (pl)	2010-01-29
LU92164I2 (fr)	2013-05-07
DE60042648D1 (de)	2009-09-10
KR20020068264A (ko)	2002-08-27
CN101121021A (zh)	2008-02-13
AT500848A1 (de)	2006-04-15
CY2013010I1 (el)	2015-08-05
PT1189641E (pt)	2009-11-04
ATE437655T1 (de)	2009-08-15
SI2283866T1 (sl)	2015-07-31
DE10084743T1 (de)	2002-08-14
CN101121021B (zh)	2011-12-07
SI2283867T1 (sl)	2014-07-31
CA2376596A1 (en)	2001-01-04
NO2013005I1 (no)	2013-04-02
NO2013005I2 (no)	2013-03-12
MXPA01013458A (es)	2002-07-30
EP2112167A2 (en)	2009-10-28
KR20070094993A (ko)	2007-09-27
RU2430739C9 (ru)	2015-12-20
DK1189641T3 (da)	2009-11-16
IL146954A (en)	2009-09-22
AU2005242195B2 (en)	2009-06-11
SI1189641T1 (sl)	2009-12-31
RU2005132788A (ru)	2007-04-27
CA2727172A1 (en)	2001-01-04
BR0012198A (pt)	2002-04-02
ES2329437T3 (es)	2009-11-26
EP1189641A2 (en)	2002-03-27
CZ20014596A3 (cs)	2003-02-12
ZA200109786B (en)	2002-11-28

Publication	Publication Date	Title
AU784045B2 (en)	2006-01-19	Humanized anti-ErbB2 antibodies and treatment with anti-ErbB2 antibodies
US7485302B2 (en)	2009-02-03	Treatment with anti-ErbB2 antibodies and chemotherapeutic agents
US7041292B1 (en)	2006-05-09	Treating prostate cancer with anti-ErbB2 antibodies
US20070269429A1 (en)	2007-11-22	Treatment with anti-erbb2 antibodies
US20070184055A1 (en)	2007-08-09	Treatment with anti-erbb2 antibodies
JP2003503361A (ja)	2003-01-28	抗ＥｒｂＢ２抗体を用いる前立腺癌の処置

Legal Events

Date	Code	Title	Description
2013-04-02	SPCF	Filing of supplementary protection certificate	Free format text: PRODUCT NAME: PERTUZUMAB; REG. NO/DATE: EU/1/13/813/001 20130304 Spc suppl protection certif: 2013005 Filing date: 20130312
2016-10-24	SPCG	Granted supplementary protection certificate	Free format text: PRODUCT NAME: PERTUZUMAB; REG. NO/DATE: EU/1/13/813/001 20130304 Spc suppl protection certif: 2013005 Filing date: 20130312
2020-07-13	MK1K	Patent expired

Date

Code

Title

Description

2013-04-02

SPCF

Filing of supplementary protection certificate

Free format text: PRODUCT NAME: PERTUZUMAB; REG. NO/DATE: EU/1/13/813/001 20130304

Spc suppl protection certif: 2013005

Filing date: 20130312

2016-10-24

SPCG

Granted supplementary protection certificate