Results 261 to 270 of about 288,586 (288)
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Chest, 2003
After generation from prothrombin, thrombin plays multiple roles in the blood coagulation cascade that are mediated by interaction with a number of physiologic substrates, effectors, and inhibitors. Structural and mutagenesis studies have helped unravel the molecular basis of thrombin interactions in the context of both well-established and emerging ...
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After generation from prothrombin, thrombin plays multiple roles in the blood coagulation cascade that are mediated by interaction with a number of physiologic substrates, effectors, and inhibitors. Structural and mutagenesis studies have helped unravel the molecular basis of thrombin interactions in the context of both well-established and emerging ...
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Oligonucleotide inhibitors of human thrombin that bind distinct epitopes.
Journal of Molecular Biology, 1997Thrombin, a multifunctional serine protease, recognizes multiple macromolecular substrates and plays a key role in both procoagulant and anticoagulant functions.
D. Tasset, M. F. Kubik, W. Steiner
semanticscholar +1 more source
Analytical Chemistry, 2011
Interactions between surface plasmons (SP) of metallic surfaces and photoluminescence (PL) of semiconductor nanocrystal (S-NC) surfaces have been extensively investigated, and SP-induced PL enhancement has been used as a sensitive analytical technique ...
Jing Wang +4 more
semanticscholar +1 more source
Interactions between surface plasmons (SP) of metallic surfaces and photoluminescence (PL) of semiconductor nanocrystal (S-NC) surfaces have been extensively investigated, and SP-induced PL enhancement has been used as a sensitive analytical technique ...
Jing Wang +4 more
semanticscholar +1 more source
Chest, 2003
The generation of the enzyme thrombin from its precursor prothrombin is the central event of the blood coagulation process, which is essential to hemostasis and the culprit in thrombosis. Thrombin is produced by a complex series of proteolytic events that are initiated when cryptic tissue factor interacts with plasma factor VIIa to initiate the complex
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The generation of the enzyme thrombin from its precursor prothrombin is the central event of the blood coagulation process, which is essential to hemostasis and the culprit in thrombosis. Thrombin is produced by a complex series of proteolytic events that are initiated when cryptic tissue factor interacts with plasma factor VIIa to initiate the complex
openaire +2 more sources
Cell-derived Microparticles Circulate in Healthy Humans and Support Low Grade Thrombin Generation
Thrombosis and Haemostasis, 2001Summary We determined the numbers, cellular origin and thrombin-generating properties of microparticles in healthy individuals (n = 15). Micro-particles, isolated from fresh blood samples and identified by flow cytometry, originated from platelets ...
R. Nieuwland +5 more
semanticscholar +1 more source
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2012
Thrombin is the final protease generated in the blood coagulation cascade. It has multiple substrates and cofactors, and serves both pro- and anti-coagulant functions. How thrombin activity is directed throughout the evolution of a clot and the role of conformational change in determining thrombin specificity are issues that lie at the heart of the ...
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Thrombin is the final protease generated in the blood coagulation cascade. It has multiple substrates and cofactors, and serves both pro- and anti-coagulant functions. How thrombin activity is directed throughout the evolution of a clot and the role of conformational change in determining thrombin specificity are issues that lie at the heart of the ...
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Thrombosis and Haemostasis, 1974
SummaryThe possibility that thrombin acts on platelets by a mechanism other than proteolysis was investigated. The proteolytic site of thrombin was modified with phenylmethylsulfonyl fluoride (PMSF). This modified enzyme did not induce platelet aggregation or the platelet release reaction.
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SummaryThe possibility that thrombin acts on platelets by a mechanism other than proteolysis was investigated. The proteolytic site of thrombin was modified with phenylmethylsulfonyl fluoride (PMSF). This modified enzyme did not induce platelet aggregation or the platelet release reaction.
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Thrombin signalling and protease-activated receptors
Nature, 2000S. Coughlin
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Selection of single-stranded DNA molecules that bind and inhibit human thrombin
Nature, 1992L. C. Bock +4 more
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