Structure and function of factor X: properties, activation, and activity in prothrombinase. A retrospective in a historical context
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DOI: 10.1007/s11239-021-02421-7
Abstract: The evolution of our understanding of the formation of thrombin from the postulated thrombokinase of Morawitz to activated Factor X and prothrombinase occurred during a period of nearly 100 years. During this time structure–function relationships… read more here.
Keywords: factor; prothrombinase; structure function; function factor ... See more keywords
Prothrombinase: the paradigm for membrane bound enzyme complexes; a memoir
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DOI: 10.1007/s11239-021-02451-1
Abstract: This review is a brief summary of the history of the development of the Prothrombinase complex paradigm and its incorporation into the “extrinsic pathway”. It summarizes my laboratory’s research from 1968 to 2012 and identifies… read more here.
Keywords: paradigm; paradigm membrane; membrane bound; bound enzyme ... See more keywords
BFPI: A Minimal Prothrombinase Inhibitor from the Saliva of Simulium Vittatum
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DOI: 10.1182/blood-2018-99-118666
Abstract: Background: The black fly, Simulium Vittatum, has an anticoagulant protein in its saliva that allows it to feed on mammalian blood (black fly protease inhibitor; BFPI). Remarkably, BFPI is similar to the human anticoagulant tissue… read more here.
Keywords: bfpi; fxa; inhibitor; inhibition ... See more keywords
Assembly of alternative prothrombinase by extracellular histones initiate and disseminate intravascular coagulation.
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DOI: 10.1182/blood.2019002973
Abstract: Thrombin generation is pivotal to both physiological blood clot formation and pathological development of disseminated intravascular coagulation (DIC). In critical illness, extensive cell damage can release histones into the circulation, which can increase thrombin generation… read more here.
Keywords: coagulation; alternative prothrombinase; prothrombinase; extracellular histones ... See more keywords