Results 301 to 310 of about 69,458 (313)
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Oxidative stress on VWF proteolysis
Blood, 2010In this issue of Blood , Chen and colleagues demonstrate that the rate of cleaving VWF by ADAMTS13 is significantly slowed when the residue Met1606 in the VWF A2 domain is oxidized.[1][1] The finding adds a new dimension to the complexity of regulating VWF cleavage and links the rate of ...
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Relevance of Intact Von Willebrand Factor (VWF) Triplet Structure for VWF Function.
Blood, 2010Abstract Abstract 1425 Introduction: The characteristic multimer pattern of plasmatic von Willebrand factor (VWF) results from asymmetric cleavage by the processing metalloprotease ADAMTS13 between Y1605/M1606 within the VWF A2 domain. In normal plasma, characteristic species of various
Christoph Kannicht +4 more
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Blood, 2006
Comment on Lisman et al, page [3753][1] In this issue of Blood , Lisman and colleagues report on the identification of the VWF-binding site within collagen III: of 57 triple-helical peptides spanning the whole triple-helical domain, one single 27-residue collagen III sequence, with an essential 9-
Karen Vanhoorelbeke, Hans Deckmyn
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Comment on Lisman et al, page [3753][1] In this issue of Blood , Lisman and colleagues report on the identification of the VWF-binding site within collagen III: of 57 triple-helical peptides spanning the whole triple-helical domain, one single 27-residue collagen III sequence, with an essential 9-
Karen Vanhoorelbeke, Hans Deckmyn
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Biochemical Pharmacology, 2013
The interactions between collagen, von Willebrand factor (VWF), and glycoprotein Ib (GPIb) are crucial for hemostasis and thrombosis. This axis represents a promising target for the development of new antithrombotic agents. In this study, we investigate the in vivo antithrombotic efficacy of an anti-VWF monoclonal antibody SZ-123 and its potential ...
Shundong Ji +6 more
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The interactions between collagen, von Willebrand factor (VWF), and glycoprotein Ib (GPIb) are crucial for hemostasis and thrombosis. This axis represents a promising target for the development of new antithrombotic agents. In this study, we investigate the in vivo antithrombotic efficacy of an anti-VWF monoclonal antibody SZ-123 and its potential ...
Shundong Ji +6 more
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SHEARiO, fast lane to oxidized VWF
Blood, 2011In this issue of Blood , Fu and coworkers show that shear stress–induced conformational changes in VWF allow the exposure of otherwise buried methionine residues, thereby promoting their susceptibility to oxidation. 1 Methionine oxidation importantly alters the interaction between VWF and platelets and prevents degradation of the protein by ADAMTS13.
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Protein superglue that holds VWF together
Blood, 2014In this issue of Blood , Zhou and Springer report on the structure determination of the von Willebrand factor (VWF) C-terminal cysteine knot domain (CTCK), finally uncovering the structural basis for the super-stable CTCK dimer that underpins platelet adhesion.[1][1] ![Figure][2] VWF is ...
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A Rapid Assay for the vWF Protease [PDF]
Thrombosis and Haemostasis, 2001 David L. Aronson +2 more
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Nature Medicine, 2001
The etiology of thrombotic thrombocytopenic purpura (TTP), a severe blood disorder resulting from increased platelet activation, has been an enigma. The identification of ADAMTS as a protease that cleaves von Willebrand factor and the demonstration of ADAMTS mutations in families with inherited TTP suggest a molecular mechanism for the disease.
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The etiology of thrombotic thrombocytopenic purpura (TTP), a severe blood disorder resulting from increased platelet activation, has been an enigma. The identification of ADAMTS as a protease that cleaves von Willebrand factor and the demonstration of ADAMTS mutations in families with inherited TTP suggest a molecular mechanism for the disease.
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VWF propeptide: a useful marker in VWD
Blood, 2006Comment on Haberichter et al, page [3344][1] Haberichter and colleagues describe a specific subset of patients with type 1 von Willebrand disease in 4 different families and suggest that an increased ratio between the von Willebrand propeptide and von Willebrand factor antigen may indicate a ...
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VWF attributes – impact on thrombus formation
Thrombosis Research, 2008At sites of vascular injury, free-flowing platelets attach to the vessel wall to initiate thrombus formation in areas of high haemodynamic shear stress, a process that is critical for both haemostasis and thrombosis. This reaction is mediated by the binding of the platelet glycoprotein (GP) Iba to the A1 domain of immobilized von Willebrand factor (VWF)
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