about
Porphyromonas gingivalis Virulence Factor Gingipain RgpB Shows a Unique Zymogenic Mechanism for Cysteine PeptidasesThe structure of a thermostable mutant of pro-papain reveals its activation mechanismThe crystal structure of the cysteine protease Xylellain from Xylella fastidiosa reveals an intriguing activation mechanismMutation in the Pro-Peptide Region of a Cysteine Protease Leads to Altered Activity and Specificity-A Structural and Biochemical ApproachRegulatory elements within the prodomain of Falcipain-2, a cysteine protease of the malaria parasite Plasmodium falciparumCathepsin K analysis in a pycnodysostosis cohort: demographic, genotypic and phenotypic features.Multistep autoactivation of asparaginyl endopeptidase in vitro and in vivo.Residue-specific annotation of disorder-to-order transition and cathepsin inhibition of a propeptide-like crammer from D. melanogaster.Cysteine peptidases of mammals: their biological roles and potential effects in the oral cavity and other tissues in health and disease.Clinical and animal research findings in pycnodysostosis and gene mutations of cathepsin K from 1996 to 2011Specialized roles for cysteine cathepsins in health and disease.Role of the C-terminal extension in a bacterial tyrosinase.Computational investigation of conformational variability and allostery in cathepsin K and other related peptidases.C-Terminal extension of a plant cysteine protease modulates proteolytic activity through a partial inhibitory mechanism.The propeptide of cruzipain--a potent selective inhibitor of the trypanosomal enzymes cruzipain and brucipain, and of the human enzyme cathepsin F.An evolutionarily conserved tripartite tryptophan motif stabilizes the prodomains of cathepsin L-like cysteine proteases.The alpha1/2 helical backbone of the prodomains defines the intrinsic inhibitory specificity in the cathepsin L-like cysteine protease subfamily.Characterization of native and recombinant falcipain-2, a principal trophozoite cysteine protease and essential hemoglobinase of Plasmodium falciparum.The crystal structure of a Cys25 -> Ala mutant of human procathepsin S elucidates enzyme-prosequence interactions.Crystal structure of NS-134 in complex with bovine cathepsin B: a two-headed epoxysuccinyl inhibitor extends along the entire active-site cleft.Chondroitin sulfate promotes activation of cathepsin K.The pro-peptide of proNGF: structure formation and intramolecular association with NGF.Folding incompetence of cathepsin L-like cysteine proteases may be compensated by the highly conserved, domain-building N-terminal extension of the proregion.Independent intramolecular mediators of folding, activity, and inhibition for the Plasmodium falciparum cysteine protease falcipain-2.Comprehensive search for cysteine cathepsins in the human genome.Autocatalytic processing of recombinant human procathepsin B is a bimolecular process.
P2860
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P2860
description
1999 nî lūn-bûn
@nan
1999 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
The crystal structure of human procathepsin K
@ast
The crystal structure of human procathepsin K
@en
The crystal structure of human procathepsin K
@nl
type
label
The crystal structure of human procathepsin K
@ast
The crystal structure of human procathepsin K
@en
The crystal structure of human procathepsin K
@nl
prefLabel
The crystal structure of human procathepsin K
@ast
The crystal structure of human procathepsin K
@en
The crystal structure of human procathepsin K
@nl
P2093
P3181
P356
P1433
P1476
The crystal structure of human procathepsin K
@en
P2093
C A Janson
C M Debouck
J M LaLonde
K J D'Alessio
M J Orsini
M S McQueney
P3181
P356
10.1021/BI9822271
P407
P577
1999-01-19T00:00:00Z