The structure and function of platelet integrins

This publication has 11 references indexed in Scilit:

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• A novel vitronectin receptor integrin (αvβx) is responsible for distinct adhesive properties of carcinoma cells
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• Inhibition of platelet adhesion to fibronectin, fibrinogen, and von Willebrand factor substrates by complex gangliosides
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• The function of multiple extracellular matrix receptors in mediating cell adhesion to extracellular matrix: preparation of monoclonal antibodies to the fibronectin receptor that specifically inhibit cell adhesion to fibronectin and react with platelet glycoproteins Ic-IIa.
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• Platelet glycoproteins IIb and IIIa as a calcium channel in liposomes
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• Glycoprotein IIb-IIIa and RGD(S) are not important for fibronectin- dependent platelet adhesion under flow conditions
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• Antibodies to the conserved cytoplasmic domain of the integrin beta 1 subunit react with proteins in vertebrates, invertebrates, and fungi.
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• Glycoprotein Ic-IIa functions as an activation-independent fibronectin receptor on human platelets.
  The Journal of cell biology, 1988