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Barry S. Coller

Researcher at State University of New York System

Publications -  22
Citations -  1396

Barry S. Coller is an academic researcher from State University of New York System. The author has contributed to research in topics: Platelet & Platelet membrane glycoprotein. The author has an hindex of 13, co-authored 22 publications receiving 1384 citations.

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Platelets and thrombolytic therapy.

TL;DR: It is worthwhile to review the complex interrelations between platelets and fibrinolysis, with emphasis on the therapeutic potential (and risks) of combining thrombolytic therapy.
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Collagen-platelet interactions: evidence for a direct interaction of collagen with platelet GPIa/IIa and an indirect interaction with platelet GPIIb/IIIa mediated by adhesive proteins

TL;DR: A murine monoclonal antibody (6F1) is produced that blocks the interaction between platelets and collagen in the presence of Mg++, supporting a model wherein collagen can directly interact with GPIa/IIa and can indirectly interact with GPIIb/IIIa via intermediary adhesive proteins.
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Platelet vitronectin receptor expression differentiates Iraqi-Jewish from Arab patients with Glanzmann thrombasthenia in Israel

TL;DR: These studies define further the heterogeneity of the molecular basis of Glanzmann thrombasthenia; they also have more widespread implications for understanding the synthesis and function of the beta 3 family of integrin receptors.
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Antiplatelet agents in the prevention and therapy of thrombosis.

TL;DR: Advances in understanding of platelet physiology provide crucial information for the rational design of newer agents that can neutralize thrombin and block the platelet receptor most important in platelet aggregation (GPIIb/IIIa).
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Platelet fibrinogen and vitronectin in Glanzmann thrombasthenia: evidence consistent with specific roles for glycoprotein IIb/IIIA and alpha v beta 3 integrins in platelet protein trafficking [see comments]

TL;DR: Analysis of platelets from two groups of Glanzmann thrombasthenic patients suggests that in addition to their recognized roles in cell adhesion and in the interaction of cells with extracellular proteins, integrin receptors may be important in protein trafficking into, and perhaps out of, platelets.