Molecular characterization of the human platelet integrin GPIIb/IIIa and its constituent glycoproteins
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Summary
Human platelet plasma membrane glycoproteins IIb (GPIIb) and IIIa (GPIIIa) form a Ca2+-dependent heterodimer, the integrin GPIIb/IIIa, which serves as the receptor for fibrinogen and other adhesive proteins at the surface of activated platelets.
- Type
- article
- Published
- 2004-01-01
- Cited by
- 7
- References
- 40
- OpenAlex
- https://openalex.org/W2009656549
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:34162430
Keywords
Chemistry, Molecular mass, Glycoprotein, Platelet, Platelet membrane glycoprotein
References
- New isolation procedure and further biochemical characterization of glycoproteins IIb and IIIa from human platelet plasma membrane.
- Related binding mechanisms for fibrinogen, fibronectin, von Willebrand factor, and thrombospondin on thrombin-stimulated human platelets.
- Complete localization of the intrachain disulphide bonds and the N-glycosylation points in the alpha-subunit of human platelet glycoprotein IIb.
- Exposure of binding sites for vitronectin on platelets following stimulation.
- Purification of glycoproteins IIb and III from human platelet plasma membranes and characterization of a calcium-dependent glycoprotein IIb-III complex.
- Structure of human platelet membrane glycoproteins IIb and IIIa as determined by electron microscopy.
- Synthetic peptides derived from fibrinogen and fibronectin change the conformation of purified platelet glycoprotein IIb-IIIa.
- Electron microscopy and structural model of human fibronectin receptor.
- Identification of the fibrinogen receptor on human platelets by photoaffinity labeling.
- The ligand binding site of the platelet integrin receptor GPIIb-IIIa is proximal to the second calcium binding domain of its alpha subunit.
- The genomic organization of platelet glycoprotein IIIa.
- The binding of detergents to lipophilic and hydrophilic proteins.
- The size and detergent binding of membrane proteins.
- The binding of deoxycholate and Triton X-100 to proteins.
- Membrane protein molecular weight determined by low-angle laser light-scattering photometry coupled with high-performance gel chromatography.
- The platelet membrane glycoprotein IIb-IIIa complex.
- Organization of the gene for platelet glycoprotein IIb.
- Highly reactive impurities in Triton X-100 and Brij 35: partial characterization and removal.
- Molecular weight, shape and structure of mixed micelles of Triton X-100 and sphingomyelin.
- New perspectives in cell adhesion: RGD and integrins.
Cited by
- Purification, analysis, and crystal structure of integrins.
- Three-dimensional Model of Human Platelet Integrin αIIbβ3 in Solution Obtained by Small Angle Neutron Scattering*
- Calcium and temperature regulation of the stability of the human platelet integrin GPIIb/IIIa in solution: an analytical ultracentrifugation study
- High glucose removes natural anti-α-galactoside and anti-β-glucoside antibody immune complexes adhering to surface O-glycoproteins of normal platelets and enhances platelet aggregation
- Modeling the a I I b & integrin solution conformation
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