Crystal structure of human trypsin 1: unexpected phosphorylation of Tyr151
about
Hereditary chronic pancreatitisSodium and T1rho MRI for molecular and diagnostic imaging of articular cartilageMutations of human cationic trypsinogen (PRSS1) and chronic pancreatitisHereditary pancreatitis: new insights into acute and chronic pancreatitisChymotrypsin C (caldecrin) promotes degradation of human cationic trypsin: identity with Rinderknecht's enzyme YBiochemical models of hereditary pancreatitisStructural basis for accelerated cleavage of bovine pancreatic trypsin inhibitor (BPTI) by human mesotrypsinNew enzyme lineages by subdomain shufflingProtein structure alignment using a genetic algorithm.A degradation-sensitive anionic trypsinogen (PRSS2) variant protects against chronic pancreatitisHuman mesotrypsin exhibits restricted S1' subsite specificity with a strong preference for small polar side chainsSystematic analysis of the in situ crosstalk of tyrosine modifications reveals no additional natural selection on multiply modified residues.Tyrosine sulfation of human trypsin steers S2' subsite selectivity towards basic amino acids.Protein surface charge of trypsinogen changes its activation pattern.A common African polymorphism abolishes tyrosine sulfation of human anionic trypsinogen (PRSS2).Genetic mechanisms underlying the pathogenesis of tropical calcific pancreatitis.Human trypsinogens in the pancreas and in cancer.Genetic basis of chronic pancreatitis in Asia Pacific region.Direct proton magnetic resonance determination of the pKa of the active center histidine in thiolsubtilisin.Molecular Basis of Enhanced Activity in Factor VIIa-Trypsin Variants Conveys Insights into Tissue Factor-mediated Allosteric Regulation of Factor VIIa ActivityMass spectrometric detection of tyrosine sulfation in human pancreatic trypsinogens, but not in tumor-associated trypsinogen.Human cationic trypsinogen is sulfated on Tyr154.The tetra-aspartate motif in the activation peptide of human cationic trypsinogen is essential for autoactivation control but not for enteropeptidase recognition.Comparative in vitro studies on native and recombinant human cationic trypsins. Cathepsin B is a possible pathological activator of trypsinogen in pancreatitis.Hereditary pancreatitis caused by a novel PRSS1 mutation (Arg-122 --> Cys) that alters autoactivation and autodegradation of cationic trypsinogen.Human cationic trypsinogen. Arg(117) is the reactive site of an inhibitory surface loop that controls spontaneous zymogen activation.Network approach for capturing ligand-induced subtle global changes in protein structures.
P2860
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P2860
Crystal structure of human trypsin 1: unexpected phosphorylation of Tyr151
description
1996 nî lūn-bûn
@nan
1996 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
Crystal structure of human trypsin 1: unexpected phosphorylation of Tyr151
@ast
Crystal structure of human trypsin 1: unexpected phosphorylation of Tyr151
@en
Crystal structure of human trypsin 1: unexpected phosphorylation of Tyr151
@nl
type
label
Crystal structure of human trypsin 1: unexpected phosphorylation of Tyr151
@ast
Crystal structure of human trypsin 1: unexpected phosphorylation of Tyr151
@en
Crystal structure of human trypsin 1: unexpected phosphorylation of Tyr151
@nl
prefLabel
Crystal structure of human trypsin 1: unexpected phosphorylation of Tyr151
@ast
Crystal structure of human trypsin 1: unexpected phosphorylation of Tyr151
@en
Crystal structure of human trypsin 1: unexpected phosphorylation of Tyr151
@nl
P2093
P356
P1476
Crystal structure of human trypsin 1: unexpected phosphorylation of Tyr151
@en
P2093
Fontecilla-Camps JC
Gaboriaud C
Guy-Crotte O
P304
P356
10.1006/JMBI.1996.0376
P407
P577
1996-06-01T00:00:00Z