GP1BA protein, human

Known as: Antigen CD42b-Alpha, Glycoprotein Ibalpha, glycoprotein Ib (platelet), alpha polypeptide, human 
Platelet glycoprotein Ib alpha chain (652 aa, ~72 kDa) is encoded by the human GP1BA gene. This protein plays a role in von Willebrand factor binding… (More)
National Institutes of Health

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12 relations
Blood PlateletsCD42 ComplexCD42b AntigenGP1BA gene
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Broader (1)

adhesion receptor

Papers overview

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2010
2010
Abnormal VWF modifies megakaryocytopoiesis: studies of platelets and megakaryocyte cultures from patients with von Willebrand disease type 2B.
von Willebrand factor (VWF) is an essential mediator of platelet adhesion to the vessel wall, but little is known about its role… (More)
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Highly Cited
2008
Highly Cited
2008
Platelet granule secretion continuously prevents intratumor hemorrhage.
Cancer is associated with a prothrombogenic state capable of platelet activation. Platelets, on the other hand, can support… (More)
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2008
2008
Platelet activation by dimeric beta2-glycoprotein I requires signaling via both glycoprotein Ibalpha and apolipoprotein E receptor 2'.
BACKGROUND Dimerization of beta(2)-glycoprotein I (beta(2)-GPI) by autoantibodies is thought to trigger the clinical… (More)
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Highly Cited
2006
Highly Cited
2006
Mechanism of platelet adhesion to von Willebrand factor and microparticle formation under high shear stress.
We describe here the mechanism of platelet adhesion to immobilized von Willebrand factor (VWF) and subsequent formation of… (More)
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Highly Cited
2005
Highly Cited
2005
A novel nanobody that detects the gain-of-function phenotype of von Willebrand factor in ADAMTS13 deficiency and von Willebrand disease type 2B.
Von Willebrand factor (VWF) is unable to interact spontaneously with platelets because this interaction requires a conversion of… (More)
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Highly Cited
2004
Highly Cited
2004
Crystal structure of the wild-type von Willebrand factor A1-glycoprotein Ibalpha complex reveals conformation differences with a complex bearing von Willebrand disease mutations.
The adhesion of platelets to the subendothelium of blood vessels at sites of vascular injury under high shear conditions is… (More)
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Highly Cited
2003
Highly Cited
2003
Crystal structure of the GpIbalpha-thrombin complex essential for platelet aggregation.
Direct interaction between platelet receptor glycoprotein Ibalpha (GpIbalpha) and thrombin is required for platelet aggregation… (More)
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Highly Cited
2002
Highly Cited
2002
Sequential cytoplasmic calcium signals in a 2-stage platelet activation process induced by the glycoprotein Ibalpha mechanoreceptor.
We found that the interaction of platelets with immobilized von Willebrand factor (VWF) under flow induces distinct elevations of… (More)
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Highly Cited
2000
Highly Cited
2000
Platelets adhere to and translocate on von Willebrand factor presented by endothelium in stimulated veins.
With the use of intravital microscopy, a new type of platelet-endothelial interaction in mouse mesenteric venules at low shear… (More)
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Highly Cited
1999
Highly Cited
1999
Activated platelets release two types of membrane vesicles: microvesicles by surface shedding and exosomes derived from exocytosis of multivesicular bodies and alpha-granules.
Platelet activation leads to secretion of granule contents and to the formation of microvesicles by shedding of membranes from… (More)
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