Jiang et al., 2021 - Google Patents
Differential neuropeptidomes of dense core secretory vesicles (DCSV) produced at intravesicular and extracellular pH conditions by proteolytic processingJiang et al., 2021
View PDF- Document ID
- 2950995191447487231
- Author
- Jiang Z
- Lietz C
- Podvin S
- Yoon M
- Toneff T
- Hook V
- O’Donoghue A
- Publication year
- Publication venue
- ACS chemical neuroscience
External Links
Snippet
Neuropeptides mediate cell–cell signaling in the nervous and endocrine systems. The neuropeptidome is the spectrum of peptides generated from precursors by proteolysis within dense core secretory vesicles (DCSV). DCSV neuropeptides and contents are released to …
- 230000002797 proteolythic 0 title abstract description 100
Classifications
-
- 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
- G01N33/5005—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving human or animal cells
- G01N33/5008—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving human or animal cells for testing or evaluating the effect of chemical or biological compounds, e.g. drugs, cosmetics
- G01N33/502—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving human or animal cells for testing or evaluating the effect of chemical or biological compounds, e.g. drugs, cosmetics for testing non-proliferative effects
-
- 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
- G01N33/6803—General methods of protein analysis not limited to specific proteins or families of proteins
- G01N33/6842—Proteomic analysis of subsets of protein mixtures with reduced complexity, e.g. membrane proteins, phosphoproteins, organelle proteins
-
- 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
- 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
- G01N2500/00—Screening for compounds of potential therapeutic value
Similar Documents
Publication | Publication Date | Title |
---|---|---|
Jiang et al. | Differential neuropeptidomes of dense core secretory vesicles (DCSV) produced at intravesicular and extracellular pH conditions by proteolytic processing | |
Varejão et al. | Molecular mechanisms in SUMO conjugation | |
Clague et al. | Deubiquitylases from genes to organism | |
Hook et al. | Proteases for processing proneuropeptides into peptide neurotransmitters and hormones | |
Marino et al. | Protein termini and their modifications revealed by positional proteomics | |
Mali et al. | Ubiquitin signaling: chemistry comes to the rescue | |
Fricker | Neuropeptides and other bioactive peptides: from discovery to function | |
Fricker | Analysis of mouse brain peptides using mass spectrometry-based peptidomics: implications for novel functions ranging from non-classical neuropeptides to microproteins | |
Hook et al. | Cysteine Cathepsins in the secretory vesicle produce active peptides: Cathepsin L generates peptide neurotransmitters and cathepsin B produces beta-amyloid of Alzheimer's disease | |
Rockel et al. | Proteasomes degrade proteins in focal subdomains of the human cell nucleus | |
Hemming et al. | Identification of β-secretase (BACE1) substrates using quantitative proteomics | |
Douglas Lu et al. | Cathepsin H functions as an aminopeptidase in secretory vesicles for production of enkephalin and galanin peptide neurotransmitters | |
Pauls et al. | Peptidomics and processing of regulatory peptides in the fruit fly Drosophila | |
Funkelstein et al. | Human cathepsin V protease participates in production of enkephalin and NPY neuropeptide neurotransmitters | |
Abid et al. | Identifying receptors for neuropeptides and peptide hormones: challenges and recent progress | |
Beard et al. | Discovery of cellular roles of intramembrane proteases | |
Corbière et al. | Strategies for the identification of bioactive neuropeptides in vertebrates | |
Petrera et al. | Carboxyterminal protein processing in health and disease: key actors and emerging technologies | |
Nolte et al. | Peptidomics of prolyl endopeptidase in the central nervous system | |
Zhang | Smits | |
Mielczarek et al. | Hemorphins—From discovery to functions and pharmacology | |
Podvin et al. | Dysregulation of neuropeptide and tau peptide signatures in human Alzheimer’s disease brain | |
Mamone et al. | Optimized extraction and large-scale proteomics of pig jejunum brush border membranes for use in in vitro digestion models | |
Schmitz et al. | The deubiquitinating enzyme Ubp1 affects sorting of the ATP-binding cassette-transporter Ste6 in the endocytic pathway | |
Bäck et al. | PAM: diverse roles in neuroendocrine cells, cardiomyocytes, and green algae |