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John D. Olson

Researcher at University of Texas Health Science Center at Houston

Publications -  6
Citations -  320

John D. Olson is an academic researcher from University of Texas Health Science Center at Houston. The author has contributed to research in topics: Platelet & Ristocetin. The author has an hindex of 5, co-authored 6 publications receiving 319 citations.

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Delayed and Recurrent Intracranial Hematomas Related to Disseminated Intravascular Clotting and Fibrinolysis in Head Injury

TL;DR: Seven of 8 delayed traumatic intracerebral hematomas were associated with clotting abnormalities suggesting disseminated intravascular clotting and fibrinolysis (DICF), which suggests an increased risk of bleeding in association with the insertion of ventricular catheters in patients with DICF.
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Binding of radioiodinated human von Willebrand factor to Bernard-Soulier, thrombasthenic and von Willebrand's disease platelets

TL;DR: It is defective attachment of exogenous vWF which prevents vWF-mediated agglutination of BSS platelets, rather than defective platelet-to-platelet contact subsequent tovWF-BSS platelet binding.
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Prothrombin Houston: a dysprothrombin identifiable by crossed immunoelectrofocusing and abnormal Echis carinatus venom activation.

TL;DR: SDS-slab gel electrophoresis revealed that the prothrombin present in the patient's eluate was cleaved by Echis carinatus venom, suggesting that the coagulopathy of prothrome results from the generation of a dysfunctional thrombin.
Journal Article

Interaction of platelets, von Willebrand factor, and ristocetin during platelet agglutination.

TL;DR: The results indicate that (1) the initial binding of human vWF polymers to platelets is a specific interaction which requires the presence of ristocetin; (2) ristOCetin andhuman vWF do not form persistent complexes in solution; and (3) the association of ristsocet in and platelets are of low affinity.
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Platelets, von Willebrand factor, and prostaglandin I2

TL;DR: It is concluded that FVIIIvWF-mediated agglutination requires both functional platelet FV IIIvWF binding sites and platelet-platelet cohesion sites, and that platelet surface cohesion sites are altered by AET and PGI2.