Clifford C. Reynolds

Identification of two proteins (actin-binding protein and P235) that are hydrolyzed by endogenous Ca2+-dependent protease during platelet aggregation.

On the role of the platelet membrane skeleton in mediating signal transduction : association of GP IIb-IIIa, pp60c-src, pp62c-yes, and the P21ras GTPase-activating protein with the membrane skeleton

Evidence that agonist-induced activation of calpain causes the shedding of procoagulant-containing microvesicles from the membrane of aggregating platelets.

Efficient plasma membrane expression of a functional platelet glycoprotein Ib-IX complex requires the presence of its three subunits.

Calcium-dependent proteolysis occurs during platelet aggregation.

Treatment of Bovine Nasal Cartilage Proteoglycan with Chondroitinases from Flavobacterium heparinum and Proteus vulgaris

Spectrin is associated with membrane-bound actin filaments in platelets and is hydrolyzed by the Ca2+-dependent protease during platelet activation

Platelet glycoprotein Ib beta is phosphorylated on serine 166 by cyclic AMP-dependent protein kinase.

The role of calpain in stimulus-response coupling : evidence that calpain mediates agonist-induced expression of procoagulant activity in platelets

Identification of glycoprotein Ib beta as one of the major proteins phosphorylated during exposure of intact platelets to agents that activate cyclic AMP-dependent protein kinase.