Results 281 to 290 of about 69,458 (313)
Anti-β2GPI/β2GPI complex promotes thrombosis by activating the P2Y2/MAPKs pathway to increase human neutrophil peptides. [PDF]
Guan X+7 more
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Endothelial function and vascular events in patients with limited cutaneous systemic sclerosis (EFVELSS): a prospective observational study. [PDF]
Jud P+19 more
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VWF proteolysis and high-shear cardiovascular disorders : new diagnosis and therapeutic approaches
Antoine Rauch
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Critical independent regions in the VWF propeptide and mature VWF that enable normal VWF storage
Blood, 2003Von Willebrand factor (VWF) is synthesized in endothelial cells, where it is stored in Weibel-Palade bodies. Administration of 1-desamino-8-D-arginine-vasopressin (DDAVP) to patients with type 1 von Willebrand disease and to healthy individuals causes a rapid increase in plasma VWF levels.
Robert R. Montgomery+2 more
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Uptake of vWF–Anti-vWF Complexes by Platelets in Suspension
Arteriosclerosis, Thrombosis, and Vascular Biology, 1996Efforts to identify the translocation of glycoprotein (GP) Ib/IX receptors, either bound to von Willebrand factor (vWF) or not, from exposed surfaces to interior membranes of thrombin-activated platelets in suspension have been unsuccessful. To observe vWF uptake by platelets, we added an anti-vWF antibody and staphylococcal protein A–gold (to act as a
Marlys D. Krumwiede+3 more
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Thrombosis and Haemostasis, 2000
SummaryWe previously found that two peptides (N- and Q-peptide) selected by phage display for binding to an anti-vWF antibody, were able to inhibit vWF-binding to collagen (1). The sequence of those peptides could be aligned with the sequence in vWF at position 1129-1136 just outside the A3-domain.
Hans Deckmyn+6 more
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SummaryWe previously found that two peptides (N- and Q-peptide) selected by phage display for binding to an anti-vWF antibody, were able to inhibit vWF-binding to collagen (1). The sequence of those peptides could be aligned with the sequence in vWF at position 1129-1136 just outside the A3-domain.
Hans Deckmyn+6 more
openaire +4 more sources
The smaller, the better: VWF in stroke
Blood, 2010In this issue of Blood , Fujioka and colleagues demonstrate that the von Willebrand factor–cleaving protease ADAMTS13 limits brain infarction in a murine model of ischemic stroke.[1][1] Platelet aggregation at sites of vascular injury is essential for normal hemostasis but also causes ...
Bernhard Nieswandt, Guido Stoll
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Thrombosis Research, 2014
Ristocetin cofactor activity of Von Willebrand factor (VWF:RCo) and the ratio VWF:RCo to its antigen VWF:Ag are used as routine screening to estimate VWF function and to detect types of Von Willebrand disease (VWD) caused by loss of high molecular weight multimers. However, the VWF:RCo test is prone to analytic imprecisions due to various reasons.
Geisen, Ulrich+6 more
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Ristocetin cofactor activity of Von Willebrand factor (VWF:RCo) and the ratio VWF:RCo to its antigen VWF:Ag are used as routine screening to estimate VWF function and to detect types of Von Willebrand disease (VWD) caused by loss of high molecular weight multimers. However, the VWF:RCo test is prone to analytic imprecisions due to various reasons.
Geisen, Ulrich+6 more
openaire +4 more sources
Thrombosis and Haemostasis, 1987
SummaryNine monoclonal antibodies (MAb, coded ESvWF 1-5, 7-10) to human von Willebrand’s factor (vWf) have been studied for their labelling characteristics with 125I and their ability to demonstrate vWf multimers by autoradiography after discontinuous SDS electrophoresis on agarose and agarose/acrylamide gels in plasma from normal and von Willebrand’s ...
M S Enayat+4 more
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SummaryNine monoclonal antibodies (MAb, coded ESvWF 1-5, 7-10) to human von Willebrand’s factor (vWf) have been studied for their labelling characteristics with 125I and their ability to demonstrate vWf multimers by autoradiography after discontinuous SDS electrophoresis on agarose and agarose/acrylamide gels in plasma from normal and von Willebrand’s ...
M S Enayat+4 more
openaire +3 more sources