Zobrazeno 1 - 10
of 13
pro vyhledávání: '"M J, IJsseldijk"'
Publikováno v:
Blood. 79:928-935
The adhesion of platelets to purified laminin under flow conditions was investigated. Adhesion to laminin was strongly dependent on the presence of divalent cations. In the absence of cations platelet adhesion (8% coverage in 5 minutes) was maximal a
Publikováno v:
Thrombosis and haemostasis. 85(4)
We studied the role of fibrinogen in platelet thrombus formation under flow on adhesive proteins using afibrinogenemic blood (LMWH anticoagulated) in a perfusion system. Perfusions with afibrinogenemic blood showed strong increased surface coverage a
Autor:
M, Roest, J J, Sixma, Y P, Wu, M J, Ijsseldijk, M, Tempelman, P J, Slootweg, P G, de Groot, G H, van Zanten
Publikováno v:
Blood. 96(4)
Platelet thrombus formation on collagen is initiated by platelet GPIb interaction with von Willebrand factor (vWF) bound to collagen, followed by firm attachment of the platelet to collagen by the integrin alpha(2)beta(1). Platelet and plasma vWF lev
Autor:
M W, Verkleij, M J, IJsseldijk, G J, Heijnen-Snyder, E G, Huizinga, L F, Morton, C G, Knight, J J, Sixma, P G, de Groot, M J, Barnes
Publikováno v:
Thrombosis and haemostasis. 82(3)
Seven overlapping peptides derived from the bovine alpha1(III)CB4 fragment of collagen III support static platelet adhesion, and an integrin alpha2beta1-recognition site has been assigned within this fragment to residues 522-528 of the collagen alpha
Autor:
H, Lankhof, C, Damas, M E, Schiphorst, M J, Ijsseldijk, M, Bracke, M, Furlan, P G, de Groot, J J, Sixma, T, Vink
Publikováno v:
Thrombosis and haemostasis. 81(6)
Type 2A von Willebrand Disease (vWD) is characterized by the absence of high molecular weight von Willebrand factor (VWF) multimers in plasma which is caused by enhanced extracellular proteolysis or defective intracellular transport. We identified in
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 96
Autor:
H, Lankhof, C, Damas, M E, Schiphorst, M J, Ijsseldijk, M, Bracke, M, Furlan, H M, Tsai, P G, de Groot, J J, Sixma, T, Vink
Publikováno v:
Thrombosis and haemostasis. 77(5)
von Willebrand factor (vWF) is a complex multimeric plasma glycoprotein, that plays a critical role in the mediation of platelet adhesion to the damaged vascular wall, and functions as a carrier protein for factor VIII. vWF has a domain structure con
Autor:
H, Lankhof, C, Damas, M E, Schiphorst, M J, IJsseldijk, M, Bracke, J J, Sixma, T, Vink, P G, de Groot
Publikováno v:
Blood. 89(8)
Type 2B von Willebrand disease (vWD) is characterized by the absence of the very high molecular weight von Willebrand factor (vWF) multimers from plasma, which is caused by spontaneous binding to platelet receptor glycoprotein Ib (GPIb). We studied t
Autor:
H, Lankhof, M, van Hoeij, M E, Schiphorst, M, Bracke, Y P, Wu, M J, Ijsseldijk, T, Vink, P G, de Groot, J J, Sixma
Publikováno v:
Thrombosis and haemostasis. 75(6)
von Willebrand factor (vWF) mediates platelet adhesion at sites of vascular damage. It acts as a bridge between receptors on platelets and collagens present in the connective tissue. Two collagen binding sites have been identified on the A1 and A3 do
Publikováno v:
Blood. 86(9)
We describe glycoprotein (GP) Ib as a mediator of adhesion to fibronectin, specifically in flow. A monoclonal antibody (MoAb) directed to the von Willebrand factor (vWF)-binding site on this receptor or the absence of this receptor on the platelet me