Proenzyme Structure and Activation of Astacin Metallopeptidase
about
The structure of the catalytic domain of Tannerella forsythia karilysin reveals it is a bacterial xenologue of animal matrix metalloproteinasesStructure, function and latency regulation of a bacterial enterotoxin potentially derived from a mammalian adamalysin/ADAM xenologCrystal Structures of Archaemetzincin Reveal a Moldable Substrate-Binding SiteStructural basis for the sheddase function of human meprin metalloproteinase at the plasma membraneStructural Basis for Activity Regulation and Substrate Preference of Clostridial Collagenases G, H, and TA Novel Family of Soluble Minimal Scaffolds Provides Structural Insight into the Catalytic Domains of Integral Membrane MetallopeptidasesCrystal structure of the human COP9 signalosomeStructural evidence of intramolecular propeptide inhibition of the aspzincin metalloendopeptidase AsaP1Plectreurys tristis venome: A proteomic and transcriptomic analysisIdentification of a mutation causing deficient BMP1/mTLD proteolytic activity in autosomal recessive osteogenesis imperfecta.The Drosophila melanogaster seminal fluid protease "seminase" regulates proteolytic and post-mating reproductive processes.A highly conserved, inhibitable astacin metalloprotease from Teladorsagia circumcincta is required for cuticle formation and nematode developmentA Unique Egg Cortical Granule Localization Motif Is Required for Ovastacin Sequestration to Prevent Premature ZP2 Cleavage and Ensure Female Fertility in Mice.A Drosophila protease cascade member, seminal metalloprotease-1, is activated stepwise by male factors and requires female factors for full activity.Domain structure and function of matrix metalloprotease 23 (MMP23): role in potassium channel trafficking.Architecture and function of metallopeptidase catalytic domains.Handling Metalloproteinases.De novo metatranscriptome assembly and coral gene expression profile of Montipora capitata with growth anomaly.A novel mechanism of latency in matrix metalloproteinases.Sizzled is unique among secreted frizzled-related proteins for its ability to specifically inhibit bone morphogenetic protein-1 (BMP-1)/tolloid-like proteinases.Inhibitory zinc sites in enzymes.Physicochemical properties of the modeled structure of astacin metalloprotease moulting enzyme NAS-36 and mapping the druggable allosteric space of Heamonchus contortus, Brugia malayi and Ceanorhabditis elegans via molecular dynamics simulation.A novel secreted metzincin metalloproteinase from Bacillus intermedius.Intracellular activation of ovastacin mediates pre-fertilization hardening of the zona pellucida.Myroilysin Is a New Bacterial Member of the M12A Family of Metzincin Metallopeptidases and Is Activated by a Cysteine Switch Mechanism.
P2860
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P2860
Proenzyme Structure and Activation of Astacin Metallopeptidase
description
2010 nî lūn-bûn
@nan
2010 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2010年の論文
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2010年学术文章
@wuu
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
@zh-sg
2010年學術文章
@yue
name
Proenzyme Structure and Activation of Astacin Metallopeptidase
@ast
Proenzyme Structure and Activation of Astacin Metallopeptidase
@en
Proenzyme Structure and Activation of Astacin Metallopeptidase
@nl
type
label
Proenzyme Structure and Activation of Astacin Metallopeptidase
@ast
Proenzyme Structure and Activation of Astacin Metallopeptidase
@en
Proenzyme Structure and Activation of Astacin Metallopeptidase
@nl
prefLabel
Proenzyme Structure and Activation of Astacin Metallopeptidase
@ast
Proenzyme Structure and Activation of Astacin Metallopeptidase
@en
Proenzyme Structure and Activation of Astacin Metallopeptidase
@nl
P2093
P2860
P356
P1476
Proenzyme Structure and Activation of Astacin Metallopeptidase
@en
P2093
F Xavier Gomis-Rüth
Irene Yiallouros
Reinhild Kappelhoff
Steffen Bissdorf
Tibisay Guevara
Walter Stöcker
P2860
P304
P356
10.1074/JBC.M109.097436
P407
P577
2010-04-30T00:00:00Z