Publications by authors named "John J Dumas"
Article Synopsis
- The study investigates how platelets stick to blood vessel injuries, focusing on the interaction between GpIbalpha (a platelet receptor) and the A1 domain of von Willebrand factor (VWF) under high shear conditions.
- A 2.6-A crystal structure reveals differences in the binding interfaces of wild-type and mutant complexes, particularly highlighting how mutations can alter binding strength.
- These findings enhance our understanding of how specific mutations related to von Willebrand Disease affect platelet adhesion, which could have implications for treating related blood disorders.
Direct interaction between platelet receptor glycoprotein Ibalpha (GpIbalpha) and thrombin is required for platelet aggregation and activation at sites of vascular injury. Abnormal GpIbalpha-thrombin binding is associated with many pathological conditions,including occlusive arterial thrombosis and bleeding disorders. The crystal structure of the GpIbalpha-thrombin complex at 2.
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