Modulation of the Affinity of Integrin α IIb β 3 (GPIIb-IIIa) by the Cytoplasmic Domain of α IIb
Author:
Affiliation:
1. Committee on Vascular Biology, Scripps Research Institute, La Jolla, CA 92037.
2. University of Pennsylvania Cancer Center, Philadelphia, PA 19104.
Publisher
American Association for the Advancement of Science (AAAS)
Subject
Multidisciplinary
Reference30 articles.
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3. BRASS, L.F., REGULATION OF THE PHOSPHOINOSITIDE HYDROLYSIS PATHWAY IN THROMBIN-STIMULATED PLATELETS BY A PERTUSSIS TOXIN-SENSITIVE GUANINE NUCLEOTIDE-BINDING PROTEIN - EVALUATION OF ITS CONTRIBUTION TO PLATELET ACTIVATION AND COMPARISONS WITH THE ADENYLATE-CYCLASE INHIBITORY PROTEIN, GI, JOURNAL OF BIOLOGICAL CHEMISTRY 261: 6838 (1986).
4. COLLER, B.S., A MURINE MONOCLONAL-ANTIBODY THAT COMPLETELY BLOCKS THE BINDING OF FIBRINOGEN TO PLATELETS PRODUCES A THROMBASTHENIC-LIKE STATE IN NORMAL PLATELETS AND BINDS TO GLYCOPROTEINS-IIB AND OR GLYCOPROTEIN-IIIA, JOURNAL OF CLINICAL INVESTIGATION 72: 325 (1983).
5. T-cell receptor cross-linking transiently stimulates adhesiveness through LFA-1
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