The influence of residue 190 in the S1 site of trypsin-like serine proteases on substrate selectivity is universally conserved.
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Crystal structure of the catalytic domain of DESC1, a new member of the type II transmembrane serine proteinase familyStructural basis for elastolytic substrate specificity in rodent alpha-chymasesIsolation, Cloning and Structural Characterisation of Boophilin, a Multifunctional Kunitz-Type Proteinase Inhibitor from the Cattle TickActive site conformational changes of prostasin provide a new mechanism of protease regulation by divalent cationsSmall Peptides Blocking Inhibition of Factor Xa and Tissue Factor-Factor VIIa by Tissue Factor Pathway Inhibitor (TFPI)Structure-function analyses of human kallikrein-related peptidase 2 establish the 99-loop as master regulator of activity.Natural and synthetic inhibitors of kallikrein-related peptidases (KLKs).Do-it-yourself histidine-tagged bovine enterokinase: a handy member of the protein engineer's toolbox.The effect of cations on the amidase activity of human tissue kallikrein: 1-linear competitive inhibition by sodium, potassium, calcium and magnesium. 2-linear mixed inhibition by aluminium.Structural determinants of specificity and regulation of activity in the allosteric loop network of human KLK8/neuropsin.
P2860
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P2860
The influence of residue 190 in the S1 site of trypsin-like serine proteases on substrate selectivity is universally conserved.
description
2002 nî lūn-bûn
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2002年の論文
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2002年学术文章
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2002年学术文章
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name
The influence of residue 190 i ...... vity is universally conserved.
@en
The influence of residue 190 i ...... vity is universally conserved.
@nl
type
label
The influence of residue 190 i ...... vity is universally conserved.
@en
The influence of residue 190 i ...... vity is universally conserved.
@nl
prefLabel
The influence of residue 190 i ...... vity is universally conserved.
@en
The influence of residue 190 i ...... vity is universally conserved.
@nl
P2093
P2860
P50
P1433
P1476
The influence of residue 190 i ...... vity is universally conserved.
@en
P2093
Erhard Kopetzki
Katrin Sichler
Robert Huber
P2860
P304
P356
10.1016/S0014-5793(02)03495-6
P407
P577
2002-10-01T00:00:00Z