Structural basis for the autoprocessing of zinc metalloproteases in the thermolysin family
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Structural Insights into the Activation and Inhibition of Histo-Aspartic Protease from Plasmodium falciparumStructure of Gentlyase, the neutral metalloprotease ofPaenibacillus polymyxaA Novel Family of Soluble Minimal Scaffolds Provides Structural Insight into the Catalytic Domains of Integral Membrane MetallopeptidasesA functional and structural study of the major metalloprotease secreted by the pathogenic fungus Aspergillus fumigatusStructural evidence of intramolecular propeptide inhibition of the aspzincin metalloendopeptidase AsaP1Bacillus licheniformis BlaR1 L3 loop is a zinc metalloprotease activated by self-proteolysis.Role of YpeB in cortex hydrolysis during germination of Bacillus anthracis spores.Aureolysin of Staphylococcus warneri M accelerates its proteolytic cascade, and participates in biofilm formation.Identification of a chitinase-modifying protein from Fusarium verticillioides: truncation of a host resistance protein by a fungalysin metalloproteaseA comprehensive alanine-scanning mutagenesis study reveals roles for salt bridges in the structure and activity of Pseudomonas aeruginosa elastase.Evidence for Cleavage of the Metalloprotease Vsm from Vibrio splendidus Strain JZ6 by an M20 Peptidase (PepT-like Protein) at Low Temperature.The role of calcium ions in the stability and instability of a thermolysin-like protease.Extracellular metalloproteases from bacteria.The metalloprotease of Listeria monocytogenes is regulated by pH.C-terminal domains of bacterial proteases: structure, function and the biotechnological applications.A novel mechanism of latency in matrix metalloproteinases.A sporulation-specific, sigF-dependent protein, SspA, affects septum positioning in Streptomyces coelicolor.Preparation and functional evaluation of collagen oligopeptide-rich hydrolysate from fish skin with the serine collagenolytic protease from Pseudoalteromonas sp. SM9913.Leptospira interrogans thermolysin refolded at high pressure and alkaline pH displays proteolytic activity against complement C3.
P2860
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P2860
Structural basis for the autoprocessing of zinc metalloproteases in the thermolysin family
description
2010 nî lūn-bûn
@nan
2010 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2010年の論文
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2010年学术文章
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2010年学术文章
@zh-cn
2010年学术文章
@zh-hans
2010年学术文章
@zh-my
2010年学术文章
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2010年學術文章
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name
Structural basis for the autop ...... ases in the thermolysin family
@ast
Structural basis for the autop ...... ases in the thermolysin family
@en
Structural basis for the autop ...... ases in the thermolysin family
@nl
type
label
Structural basis for the autop ...... ases in the thermolysin family
@ast
Structural basis for the autop ...... ases in the thermolysin family
@en
Structural basis for the autop ...... ases in the thermolysin family
@nl
prefLabel
Structural basis for the autop ...... ases in the thermolysin family
@ast
Structural basis for the autop ...... ases in the thermolysin family
@en
Structural basis for the autop ...... ases in the thermolysin family
@nl
P2093
P2860
P3181
P356
P1476
Structural basis for the autop ...... ases in the thermolysin family
@en
P2093
Bai-Cheng Zhou
Bin-Bin Xie
Jia-Wei Wu
Lu-Hua Lai
Xiu-Lan Chen
Yu-Zhong Zhang
P2860
P304
P3181
P356
10.1073/PNAS.1005681107
P407
P577
2010-10-12T00:00:00Z