Cleavage of ultralarge multimers of von Willebrand factor by C-terminal-truncated mutants of ADAMTS-13 under flow.
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Pathogenesis of thrombotic microangiopathiesADAMTS13 and von Willebrand factor in thrombotic thrombocytopenic purpuraIncreased ADAMTS-13 proteolytic activity in rat hepatic stellate cells upon activation in vitro and in vivoShear-Induced Unfolding and Enzymatic Cleavage of Full-Length VWF Multimers.Size regulation of von Willebrand factor-mediated platelet thrombi by ADAMTS13 in flowing bloodCarboxyl terminus of ADAMTS13 directly inhibits platelet aggregation and ultra large von Willebrand factor string formation under flow in a free-thiol-dependent manner.A rapid test for the diagnosis of thrombotic thrombocytopenic purpura using surface enhanced laser desorption/ionization time-of-flight (SELDI-TOF)-mass spectrometry.Further characterization of ADAMTS-13 inactivation by thrombin.Insights into von Willebrand factor proteolysis: clinical implications.An IAP retrotransposon in the mouse ADAMTS13 gene creates ADAMTS13 variant proteins that are less effective in cleaving von Willebrand factor multimers.Correction of ADAMTS13 deficiency by in utero gene transfer of lentiviral vector encoding ADAMTS13 genes.Effects of naturally occurring mutations in CUB-1 domain on synthesis, stability, and activity of ADAMTS-13.The distal carboxyl-terminal domains of ADAMTS13 are required for regulation of in vivo thrombus formation.An autoantibody epitope comprising residues R660, Y661, and Y665 in the ADAMTS13 spacer domain identifies a binding site for the A2 domain of VWFA shear-based assay for assessing plasma ADAMTS13 activity and inhibitors in patients with thrombotic thrombocytopenic purpuraHumoral immune response to ADAMTS13 in acquired thrombotic thrombocytopenic purpura.[ADAMTS13, von Willebrand factor specific cleaving protease].Residual plasmatic activity of ADAMTS13 is correlated with phenotype severity in congenital thrombotic thrombocytopenic purpura.von Willebrand factor: more than a regulator of hemostasis and thrombosis.A novel flow-based assay reveals discrepancies in ADAMTS-13 inhibitor assessment as compared with a conventional clinical static assay.Congenital and acquired ADAMTS13 deficiency: Two mechanisms, one patient.Disulfide bond reduction of von Willebrand factor by ADAMTS-13.Amino acid residues Arg(659), Arg(660), and Tyr(661) in the spacer domain of ADAMTS13 are critical for cleavage of von Willebrand factor.Unraveling the scissile bond: how ADAMTS13 recognizes and cleaves von Willebrand factor.Detection of a secreted metalloprotease within the nuclei of liver cellsRecombinant 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.Linker regions and flexibility around the metalloprotease domain account for conformational activation of ADAMTS-13.The proximal carboxyl-terminal domains of ADAMTS13 determine substrate specificity and are all required for cleavage of von Willebrand factor.Structure-function and regulation of ADAMTS-13 protease.A systematic overview of the first pasteurised VWF/FVIII medicinal product, Haemate P/ Humate -P: history and clinical performance.Detection of intracellular ADAMTS13, a secreted zinc-metalloprotease, via flow cytometry.Melanoma-derived IL-1 converts vascular endothelium to a proinflammatory and procoagulatory phenotype via NFκB activation.The ADAMTS13 metalloprotease domain: roles of subsites in enzyme activity and specificity.Apical sorting of ADAMTS13 in vascular endothelial cells and Madin-Darby canine kidney cells depends on the CUB domains and their association with lipid rafts.ADAMTS13 and its variants promote angiogenesis via upregulation of VEGF and VEGFR2.Cysteine residues in CUB-1 domain are critical for ADAMTS13 secretion and stability.Antihemostatic Activity of Human Granzyme B Mediated by Cleavage of von Willebrand Factor
P2860
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P2860
Cleavage of ultralarge multimers of von Willebrand factor by C-terminal-truncated mutants of ADAMTS-13 under flow.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
2005年论文
@zh
2005年论文
@zh-cn
name
Cleavage of ultralarge multime ...... tants of ADAMTS-13 under flow.
@en
Cleavage of ultralarge multime ...... tants of ADAMTS-13 under flow.
@nl
type
label
Cleavage of ultralarge multime ...... tants of ADAMTS-13 under flow.
@en
Cleavage of ultralarge multime ...... tants of ADAMTS-13 under flow.
@nl
prefLabel
Cleavage of ultralarge multime ...... tants of ADAMTS-13 under flow.
@en
Cleavage of ultralarge multime ...... tants of ADAMTS-13 under flow.
@nl
P2093
P2860
P1433
P1476
Cleavage of ultralarge multime ...... tants of ADAMTS-13 under flow.
@en
P2093
Aubrey Bernardo
Huiwei Choi
Jing-Fei Dong
José A López
Kenji Nishio
Yongtao Wang
Zhenyin Tao
P2860
P304
P356
10.1182/BLOOD-2004-11-4188
P407
P577
2005-03-17T00:00:00Z