ADAMTS-13 metalloprotease interacts with the endothelial cell-derived ultra-large von Willebrand factor - Wikidata - wikimedia - TriplyDB

ADAMTS-13 metalloprotease interacts with the endothelial cell-derived ultra-large von Willebrand factor

ADAMTS-13 metalloprotease interacts with the endothelial cell-derived ultra-large von Willebrand factor

http://www.wikidata.org/entity/Q24303587

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Binding of ADAMTS13 to von Willebrand factor ADAMTS-12 associates with and degrades cartilage oligomeric matrix protein ADAMTS13 substrate recognition of von Willebrand factor A2 domain A disintegrin-like and metalloprotease (reprolysin-type) with thrombospondin type 1 motif (ADAMTS) superfamily: functions and mechanisms Pathogenesis of thrombotic microangiopathies Hemolytic uremic syndrome-associated Shiga toxins promote endothelial-cell secretion and impair ADAMTS13 cleavage of unusually large von Willebrand factor multimers Cleavage of ultra-large von Willebrand factor by ADAMTS-13 under flow conditions The von Willebrand factor-cleaving protease (ADAMTS-13) and the diagnosis of thrombotic thrombocytopenic purpura (TTP)Cochlin and glaucoma: a mini-review.Essential domains of a disintegrin and metalloprotease with thrombospondin type 1 repeats-13 metalloprotease required for modulation of arterial thrombosis.Carboxyl terminus of ADAMTS13 directly inhibits platelet aggregation and ultra large von Willebrand factor string formation under flow in a free-thiol-dependent manner.Attack of the acronyms: TTP, VWF, ADAMTS-13 and SELDI-TOF-MS.Further characterization of ADAMTS-13 inactivation by thrombin.von Willebrand factor: two sides of a coin.The role of ADAMTS13 in the new pathogenesis of TTP.Enzymatically active ADAMTS13 variants are not inhibited by anti-ADAMTS13 autoantibodies: a novel therapeutic strategy?The pathogenicity of von Willebrand factor in thrombotic thrombocytopenic purpura: reconsideration of treatment with cryopoor plasma.Systemic antithrombotic effects of ADAMTS13.Insights into von Willebrand factor proteolysis: clinical implications.Prospective study on the behaviour of the metalloprotease ADAMTS13 and of von Willebrand factor after bone marrow transplantation.Inhibitory autoantibodies against ADAMTS-13 in patients with thrombotic thrombocytopenic purpura bind ADAMTS-13 protease and may accelerate its clearance in vivo.Thrombotic thrombocytopenic purpura: survival by "giving a dam"An autoantibody epitope comprising residues R660, Y661, and Y665 in the ADAMTS13 spacer domain identifies a binding site for the A2 domain of VWF Thrombotic microangiopathies: multimers, metalloprotease, and beyond.Clinical features of severe acquired ADAMTS13 deficiency in thrombotic thrombocytopenic purpura: the Korean TTP registry experience.Gain-of-function ADAMTS13 variants that are resistant to autoantibodies against ADAMTS13 in patients with acquired thrombotic thrombocytopenic purpura.Antigen and substrate withdrawal in the management of autoimmune thrombotic disorders.Thrombotic thrombocytopenic purpura-what is new?ADAMTS-13 in the Diagnosis and Management of Thrombotic Microangiopathies.VWF excess and ADAMTS13 deficiency: a unifying pathomechanism linking inflammation to thrombosis in DIC, malaria, and TTP.ADAMTS13 and von Willebrand factor interactions.Amino acid residues Arg(659), Arg(660), and Tyr(661) in the spacer domain of ADAMTS13 are critical for cleavage of von Willebrand factor.A model for single-substrate trimolecular enzymatic kinetics.Factor VIII and platelets synergistically accelerate cleavage of von Willebrand factor by ADAMTS13 under fluid shear stress.Why Do We Need ADAMTS13?Exosite interactions contribute to tension-induced cleavage of von Willebrand factor by the antithrombotic ADAMTS13 metalloprotease Recombinant CUB-1 domain polypeptide inhibits the cleavage of ULVWF strings by ADAMTS13 under flow conditions.The cooperative activity between the carboxyl-terminal TSP1 repeats and the CUB domains of ADAMTS13 is crucial for recognition of von Willebrand factor under flow.Cochlin in the eye: functional implications.Spatial and temporal dynamics of the endothelium.

P2860

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P2860

ADAMTS-13 metalloprotease interacts with the endothelial cell-derived ultra-large von Willebrand factor

http://www.wikidata.org/entity/Q24303587

description

2003 nî lūn-bûn

@nan

2003 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2003 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2003年の論文

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2003年論文

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2003年論文

@zh-hant

2003年論文

@zh-hk

2003年論文

@zh-mo

2003年論文

@zh-tw

2003年论文

@wuu

name

ADAMTS-13 metalloprotease inte ...... ra-large von Willebrand factor

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ADAMTS-13 metalloprotease inte ...... ra-large von Willebrand factor

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ADAMTS-13 metalloprotease inte ...... ra-large von Willebrand factor

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ADAMTS-13 metalloprotease inte ...... ra-large von Willebrand factor

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type

label

ADAMTS-13 metalloprotease inte ...... ra-large von Willebrand factor

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ADAMTS-13 metalloprotease inte ...... ra-large von Willebrand factor

@en

ADAMTS-13 metalloprotease inte ...... ra-large von Willebrand factor

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ADAMTS-13 metalloprotease inte ...... ra-large von Willebrand factor

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prefLabel

ADAMTS-13 metalloprotease inte ...... ra-large von Willebrand factor

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ADAMTS-13 metalloprotease inte ...... ra-large von Willebrand factor

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ADAMTS-13 metalloprotease inte ...... ra-large von Willebrand factor

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P356

P1433

Journal of Biological Chemistry

P1476

ADAMTS-13 metalloprotease inte ...... ra-large von Willebrand factor

@en

P2093

Aubrey Bernardo

http://www.w3.org/2001/XMLSchema#string

Chalmette Ball

http://www.w3.org/2001/XMLSchema#string

Jing-fei Dong

http://www.w3.org/2001/XMLSchema#string

Joel L Moake

http://www.w3.org/2001/XMLSchema#string

José A López

http://www.w3.org/2001/XMLSchema#string

Kazuo Fujikawa

http://www.w3.org/2001/XMLSchema#string

Leticia Nolasco

http://www.w3.org/2001/XMLSchema#string

Miguel A Cruz

http://www.w3.org/2001/XMLSchema#string

P2860

Biochemistry and genetics of von Willebrand factor

Mapping the glycoprotein Ib-binding site in the von willebrand factor A1 domain

Purification of human von Willebrand factor-cleaving protease and its identification as a new member of the metalloproteinase family

Structure of von Willebrand factor-cleaving protease (ADAMTS13), a metalloprotease involved in thrombotic thrombocytopenic purpura

Inducible secretion of large, biologically potent von Willebrand factor multimers

Von Willebrand factor, ADAMTS13, and thrombotic thrombocytopenic purpura

Partial amino acid sequence of purified von Willebrand factor-cleaving protease.

Mutations in a member of the ADAMTS gene family cause thrombotic thrombocytopenic purpura.

von Willebrand factor cleaving protease (ADAMTS13) is deficient in recurrent and familial thrombotic thrombocytopenic purpura and hemolytic uremic syndrome.

ADAMTS-13 rapidly cleaves newly secreted ultralarge von Willebrand factor multimers on the endothelial surface under flowing conditions.

P304

29633-9

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P31

scholarly article

P356

10.1074/JBC.M301385200

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P407

P433

32

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P478

278

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P577

2003-08-08T00:00:00Z

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P698

12775718

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P921

protease binding

Von Willebrand factor