Results 201 to 210 of about 13,808 (210)
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2015
ADAMTS13 has been identified as the von Willebrand factor-cleaving protease and is deficient in the disorder thrombotic thrombocytopenic purpura. The identification of vascular endothelium as a site of synthesis and secretion of ADAMTS13 has led to studies of the role of ADAMTS13 in angiogenesis.
Manfai Lee, George M. Rodgers
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ADAMTS13 has been identified as the von Willebrand factor-cleaving protease and is deficient in the disorder thrombotic thrombocytopenic purpura. The identification of vascular endothelium as a site of synthesis and secretion of ADAMTS13 has led to studies of the role of ADAMTS13 in angiogenesis.
Manfai Lee, George M. Rodgers
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Blood, 2010
In this issue of Blood , Kremer Hovinga and colleagues demonstrate that a lower level of initial plasma ADAMTS13 activity (< 10%) is associated with higher risk of relapse in patients with TTP.
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In this issue of Blood , Kremer Hovinga and colleagues demonstrate that a lower level of initial plasma ADAMTS13 activity (< 10%) is associated with higher risk of relapse in patients with TTP.
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ADAMTS13: Structure and Function
2015ADAMTS13, a plasma metalloprotease that cleaves von Willebrand factor (VWF), has been shown to have both antithrombotic and anti-inflammatory activities. Severe deficiency of plasma ADAMTS13 activity is a primary cause of thrombotic thrombocytopenic purpura (TTP), a potentially fatal syndrome, but mild to moderate deficiency of plasma ADAMTS13 activity
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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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