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ADAMTS13: origins, applications, and prospects
Transfusion, 2018ADAMTS13 is an enzyme that acts by cleaving prothrombotic von Willebrand factor (VWF) multimers from the vasculature in a highly regulated manner. In pathologic states such as thrombotic thrombocytopenic purpura (TTP) and other thrombotic microangiopathies (TMAs), VWF can bind to the endothelium and form large multimers. As the anchored VWF chains grow,
William E. Plautz +5 more
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Blood, 2009
In mice, a long form and a short form of the VWF-cleaving protease ADAMTS13 have been identified, the latter lacking the 4 distal carboxyl-terminal domains. While these are not strictly required for regulating normal size distribution of VWF multimers, in this issue of Blood, Banno and colleagues reveal the role of these domains in down-regulating ...
Karen, Vanhoorelbeke +2 more
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In mice, a long form and a short form of the VWF-cleaving protease ADAMTS13 have been identified, the latter lacking the 4 distal carboxyl-terminal domains. While these are not strictly required for regulating normal size distribution of VWF multimers, in this issue of Blood, Banno and colleagues reveal the role of these domains in down-regulating ...
Karen, Vanhoorelbeke +2 more
openaire +2 more sources
Structural and functional correlation of ADAMTS13
Current Opinion in Hematology, 2007ADAMTS13 represents a landmark in a journey that began over 80 years ago with a single clinical case. Thrombotic thrombocytopenic purpura exemplifies how von Willebrand factor can be responsible for life-threatening thrombosis. This review summarizes recent progress on ADAMTS13, which prevents this deadly event.Recent advances are summarized in four ...
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A-175 Distribution of ADAMTS13 Inhibitor Levels as a Function of ADAMTS13 Activity
Clinical ChemistryAbstract Background Thrombotic thrombocytopenic purpura (TTP) is diagnosed clinicopathologically that includes the finding of abnormally low ADAMTS13 activity (<0.1 IU/mL [10%]) in the context of appropriate laboratory and clinical findings.
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International review of thrombosis
ADAMTS13, encoded on chromosome 9q34, is a member of the ADAMTS (a disintegrin and metalloprotease with thrombospondin type 1 motif) metalloprotease family, containing the common domain structure of (from the amino terminus) signal peptide, propeptide, reprolysin type metalloprotease, thrombospondin type 1 motif, cysteine-rich region, and spacer domain.
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ADAMTS13, encoded on chromosome 9q34, is a member of the ADAMTS (a disintegrin and metalloprotease with thrombospondin type 1 motif) metalloprotease family, containing the common domain structure of (from the amino terminus) signal peptide, propeptide, reprolysin type metalloprotease, thrombospondin type 1 motif, cysteine-rich region, and spacer domain.
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