Blocking the proteolytic activity of zymogen matriptase with antibody-based inhibitors.
TTSP
cancer therapy
enzyme inhibitor
enzyme kinetics
epitope mapping
matriptase
multi-domain protein
serine protease
surface plasmon resonance (SPR)
zymogen
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
04 01 2019
04 01 2019
Historique:
received:
27
05
2018
revised:
04
11
2018
pubmed:
10
11
2018
medline:
10
4
2019
entrez:
10
11
2018
Statut:
ppublish
Résumé
Matriptase is a member of the type-II transmembrane serine protease (TTSP) family and plays a crucial role in the development and maintenance of epithelial tissues. As all chymotrypsin-like serine proteases, matriptase is synthesized as a zymogen (proform), requiring a cleavage event for full activity. Recent studies suggest that the zymogen of matriptase possesses enough catalytic activity to not only facilitate autoactivation, but also carry out its
Identifiants
pubmed: 30409910
pii: S0021-9258(20)36900-3
doi: 10.1074/jbc.RA118.004126
pmc: PMC6322904
pii:
doi:
Substances chimiques
Antibodies, Monoclonal
0
Enzyme Precursors
0
Protease Inhibitors
0
Serine Endopeptidases
EC 3.4.21.-
matriptase
EC 3.4.21.-
Banques de données
PDB
['5LYO', '4ISN']
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
314-326Informations de copyright
© 2019 Tamberg et al.
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