Essential role of the disintegrin-like domain in ADAMTS13 function.
about
Evolutionary divergence and functions of the ADAM and ADAMTS gene familiesPathophysiology of thrombotic thrombocytopenic purpuraA disintegrin-like and metalloprotease (reprolysin-type) with thrombospondin type 1 motif (ADAMTS) superfamily: functions and mechanismsADAM and ADAMTS Family Proteins and Snake Venom Metalloproteinases: A Structural OverviewStructural basis of type 2A von Willebrand disease investigated by molecular dynamics simulations and experimentsAn autoantibody epitope comprising residues R660, Y661, and Y665 in the ADAMTS13 spacer domain identifies a binding site for the A2 domain of VWFResidues Arg568 and Phe592 contribute to an antigenic surface for anti-ADAMTS13 antibodies in the spacer domainResidual plasmatic activity of ADAMTS13 is correlated with phenotype severity in congenital thrombotic thrombocytopenic purpura.Conformational activation of ADAMTS13.ADAMTS13 and von Willebrand factor interactions.A model for the conformational activation of the structurally quiescent metalloprotease ADAMTS13 by von Willebrand factor.Amino acid residues Arg(659), Arg(660), and Tyr(661) in the spacer domain of ADAMTS13 are critical for cleavage of von Willebrand factor.ADAM and ADAMTS family proteins and their role in the colorectal cancer etiopathogenesis.The importance of vicinal cysteines, C1669 and C1670, for von Willebrand factor A2 domain functionUnraveling the scissile bond: how ADAMTS13 recognizes and cleaves von Willebrand factor.Mechanism of von Willebrand factor scissile bond cleavage by a disintegrin and metalloproteinase with a thrombospondin type 1 motif, member 13 (ADAMTS13).The role of the ADAMTS13 cysteine-rich domain in VWF binding and proteolysis.A novel binding site for ADAMTS13 constitutively exposed on the surface of globular VWF.Rearranging exosites in noncatalytic domains can redirect the substrate specificity of ADAMTS proteases.Structure-function and regulation of ADAMTS-13 protease.Crystal structures of the noncatalytic domains of ADAMTS13 reveal multiple discontinuous exosites for von Willebrand factor.The ADAMTS13 metalloprotease domain: roles of subsites in enzyme activity and specificity.ADAMTS13, lucky to have a hydrophobic pocket.Conformational quiescence of ADAMTS-13 prevents proteolytic promiscuity.A common mechanism by which type 2A von Willebrand disease mutations enhance ADAMTS13 proteolysis revealed with a von Willebrand factor A2 domain FRET construct.High throughput protease profiling comprehensively defines active site specificity for thrombin and ADAMTS13.ADAMTS-13 and von Willebrand factor: a dynamic duo.
P2860
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P2860
Essential role of the disintegrin-like domain in ADAMTS13 function.
description
2009 nî lūn-bûn
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2009年の論文
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2009年学术文章
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2009年学术文章
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2009年学术文章
@zh-cn
2009年学术文章
@zh-hans
2009年学术文章
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2009年学术文章
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2009年學術文章
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2009年學術文章
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name
Essential role of the disintegrin-like domain in ADAMTS13 function.
@en
Essential role of the disintegrin-like domain in ADAMTS13 function.
@nl
type
label
Essential role of the disintegrin-like domain in ADAMTS13 function.
@en
Essential role of the disintegrin-like domain in ADAMTS13 function.
@nl
prefLabel
Essential role of the disintegrin-like domain in ADAMTS13 function.
@en
Essential role of the disintegrin-like domain in ADAMTS13 function.
@nl
P2093
P1433
P1476
Essential role of the disintegrin-like domain in ADAMTS13 function
@en
P2093
Ajoy Bardhan
David A Lane
Nalisha Ramroop
P304
P356
10.1182/BLOOD-2008-11-187914
P407
P577
2009-02-20T00:00:00Z