Epinette et al., 2012 - Google Patents
A selective reversible azapeptide inhibitor of human neutrophil proteinase 3 derived from a high affinity FRET substrateEpinette et al., 2012
View PDF- Document ID
- 1231908432421690892
- Author
- Epinette C
- Croix C
- Jaquillard L
- Marchand-Adam S
- Kellenberger C
- Lalmanach G
- Cadene M
- Viaud-Massuard M
- Gauthier F
- Korkmaz B
- Publication year
- Publication venue
- Biochemical pharmacology
External Links
Snippet
The biological functions of human neutrophil proteinase 3 (PR3) remain unclear because of its close structural resemblance to neutrophil elastase and its apparent functional redundancy with the latter. Thus, all natural inhibitors of PR3 preferentially target neutrophil …
- 230000002401 inhibitory effect 0 title abstract description 99
Classifications
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2333/00—Assays involving biological materials from specific organisms or of a specific nature
- G01N2333/90—Enzymes; Proenzymes
- G01N2333/914—Hydrolases (3)
- G01N2333/948—Hydrolases (3) acting on peptide bonds (3.4)
- G01N2333/95—Proteinases, i.e. endopeptidases (3.4.21-3.4.99)
- G01N2333/964—Proteinases, i.e. endopeptidases (3.4.21-3.4.99) derived from animal tissue
- G01N2333/96425—Proteinases, i.e. endopeptidases (3.4.21-3.4.99) derived from animal tissue from mammals
- G01N2333/96427—Proteinases, i.e. endopeptidases (3.4.21-3.4.99) derived from animal tissue from mammals in general
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/81—Protease inhibitors
- C07K14/8107—Endopeptidase (E.C. 3.4.21-99) inhibitors
- C07K14/8146—Metalloprotease (E.C. 3.4.24) inhibitors, e.g. tissue inhibitor of metallo proteinase, TIMP
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/81—Protease inhibitors
- C07K14/8107—Endopeptidase (E.C. 3.4.21-99) inhibitors
- C07K14/811—Serine protease (E.C. 3.4.21) inhibitors
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES OR MICRO-ORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
- C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or micro-organisms; Compositions therefor; Processes of preparing such compositions
- C12Q1/34—Measuring or testing processes involving enzymes, nucleic acids or micro-organisms; Compositions therefor; Processes of preparing such compositions involving hydrolase
- C12Q1/37—Measuring or testing processes involving enzymes, nucleic acids or micro-organisms; Compositions therefor; Processes of preparing such compositions involving hydrolase involving peptidase or proteinase
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by the preceding groups
- G01N33/48—Investigating or analysing materials by specific methods not covered by the preceding groups biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/68—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K7/00—Peptides having 5 to 20 amino acids in a fully defined sequence; Derivatives thereof
- C07K7/04—Linear peptides containing only normal peptide links
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICRO-ORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING OR MAINTAINING MICRO-ORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
Similar Documents
Publication | Publication Date | Title |
---|---|---|
Epinette et al. | A selective reversible azapeptide inhibitor of human neutrophil proteinase 3 derived from a high affinity FRET substrate | |
Fittler et al. | Potent inhibitors of human matriptase‐1 based on the scaffold of sunflower trypsin inhibitor | |
Korkmaz et al. | Design and use of highly specific substrates of neutrophil elastase and proteinase 3 | |
Rut et al. | Engineered unnatural ubiquitin for optimal detection of deubiquitinating enzymes | |
Avrutina et al. | Between two worlds: a comparative study on in vitro and in silico inhibition of trypsin and matriptase by redox-stable SFTI-1 variants at near physiological pH | |
Jendrny et al. | Inhibition of kallikrein‐related peptidases 7 and 5 by grafting serpin reactive‐center loop sequences onto sunflower trypsin inhibitor‐1 (SFTI‐1) | |
Drag et al. | Activity profiling of human deSUMOylating enzymes (SENPs) with synthetic substrates suggests an unexpected specificity of two newly characterized members of the family | |
Cadicamo et al. | Design, synthesis, inhibition studies, and molecular modeling of pepstatin analogues addressing different secreted aspartic proteinases of Candida albicans | |
Chang et al. | Identification of a 4-mer peptide inhibitor that effectively blocks the polymerization of pathogenic Z α1-antitrypsin | |
Popow-Stellmaszyk et al. | A new proteinase 3 substrate with improved selectivity over human neutrophil elastase | |
Praveen et al. | Nonspecific cytotoxic cells of teleosts are armed with multiple granzymes and other components of the granule exocytosis pathway | |
Groborz et al. | Internally quenched fluorogenic substrates with unnatural amino acids for cathepsin G investigation | |
Chen et al. | Cloning and characterization of a novel Kunitz-type inhibitor from scorpion with unique cysteine framework | |
Kreutzmann et al. | Recombinant production, purification and biochemical characterization of domain 6 of LEKTI: a temporary Kazal-type-related serine proteinase inhibitor | |
Benkova et al. | Evaluation of recombinant caspase specificity by competitive substrates | |
Liu et al. | Functional characterization of a new non-Kunitz serine protease inhibitor from the scorpion Lychas mucronatus | |
Jégot et al. | A substrate‐based approach to convert SerpinB1 into a specific inhibitor of proteinase 3, the Wegener's granulomatosis autoantigen | |
Motoyama et al. | Identification of dermcidin in human gestational tissue and characterization of its proteolytic activity | |
Lütticke et al. | E. coli LoiP (YggG), a metalloprotease hydrolyzing Phe–Phe bonds | |
Öhlknecht et al. | Enhancing the promiscuity of a member of the Caspase protease family by rational design | |
Hempel et al. | Structural relationships among class I isozymes of human liver alcohol dehydrogenase | |
Lobov et al. | Structural bases of the redox-dependent conformational switch in the serpin PAI-2 | |
McGouran et al. | Fluorescence-based active site probes for profiling deubiquitinating enzymes | |
Łęgowska et al. | Ultrasensitive internally quenched substrates of human cathepsin L | |
Kumarathasan et al. | An automated high-performance liquid chromatography fluorescence method for the analyses of endothelins in plasma samples |