Zobrazeno 1 - 10 of 90 pro vyhledávání: '"M. W. Mosesson"'
1
Inhibition of Thrombin Generation in Plasma by Fibrin Formation (Antithrombin I)
Autor: M. W. Mosesson, M. Echenagucia, N. B. de Bosch, A. Ruiz-Sáez, A. Rodriguez-Lemoin
Publikováno v: Thrombosis and Haemostasis. 88:253-258
SummaryThe adsorption of thrombin to fibrin during clotting defines “Antithrombin I” activity. We confirmed that thrombin generation in afibrinogenemic or in Reptilase defibrinated normal plasma was higher than in normal plasma. Repletion of thes
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::a737574ec33a7ec763e14316eb4a716b
https://doi.org/10.1055/s-0037-1613195
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2
Evidence for New Endothelial Cell Binding Sites on Fibrinogen
Autor: Susan T. Lord, M. W. Mosesson, M. M. Rooney, Richard A. Smith, T. K. Gartner
Publikováno v: Thrombosis and Haemostasis. 84:819-825
SummaryIn vitro assays were used to characterize adhesion of human aortic, microvascular and umbilical vein endothelial cells to various forms of immobilized fibrinogen. All three types of endothelial cells adhered to fibrinogen in a manner that was
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::be12ff42345939cfafcc74ef9fa1e430
https://doi.org/10.1055/s-0037-1614123
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3
Progressive cross-linking of fibrin gamma chains increases resistance to fibrinolysis
Autor: M W Mosesson, K R Siebenlist
Publikováno v: Journal of Biological Chemistry. 269:28414-28419
In the presence of plasma transglutaminase (factor XIIIa) fibrin first undergoes intermolecular covalent cross-linking between its gamma chains to create gamma dimers followed by slower cross-linking among its alpha chains to form alpha polymers. Pro
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::20605b4ebbcd2b0847c50d3fc3820aeb
https://doi.org/10.1016/s0021-9258(18)46943-8
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4
Adhesion of microvascular endothelial cells to metallic implant surfaces
Autor: R A, Smith, M W, Mosesson, A U, Daniels, T K, Gartner
Publikováno v: Journal of materials science. Materials in medicine. 11(5)
The objective of this study was to explore the molecular mechanisms of adhesion of endothelial cells (ECs) to implant grades of titanium alloy (Ti) and stainless steel (SS), compared to tissue culture polystyrene (PS). The idea is that promotion of E
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::9e995473013265f3c1cb48a3a4d6ba21
https://pubmed.ncbi.nlm.nih.gov/15348024
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6
Fibrinogen gamma chain functions
Autor: M W, Mosesson
Publikováno v: Journal of thrombosis and haemostasis : JTH. 1(2)
This review covers the functional features of the fibrinogen gamma chains including their participation in fibrin polymerization and cross-linking, their role in the initiation of fibrinolysis, their binding and regulation of factor XIII activity, th
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::cba5ddbf3eed857657f79be2d50eba6b
https://pubmed.ncbi.nlm.nih.gov/12871494
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7
Inhibition of thrombin generation in plasma by fibrin formation (Antithrombin I)
Autor: N B, de Bosch, M W, Mosesson, A, Ruiz-Sáez, M, Echenagucia, A, Rodriguez-Lemoin
Publikováno v: Thrombosis and haemostasis. 88(2)
The adsorption of thrombin to fibrin during clotting defines "Antithrombin I" activity. We confirmed that thrombin generation in afibrinogenemic or in Reptilase defibrinated normal plasma was higher than in normal plasma. Repletion of these fibrinoge
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::d5f298409e77a1761a1225ebad98dc7d
https://pubmed.ncbi.nlm.nih.gov/12195697
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8
Protransglutaminase (factor XIII) mediated crosslinking of fibrinogen and fibrin
Autor: K R, Siebenlist, D A, Meh, M W, Mosesson
Publikováno v: Thrombosis and haemostasis. 86(5)
Plasma factor XIII (plasma protransglutaminase) circulates as an A2B2 tetramer bound to the gamma' variant chains of fibrinogen "2". During clotting the A subunits of fXIII are cleaved by thrombin to form fXIIIa (transglutaminase) and in the presence
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::c490dd05cb6852435b4249f236ea9ba4
https://pubmed.ncbi.nlm.nih.gov/12719793
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9
The amino acid sequence in fibrin responsible for high affinity thrombin binding
Autor: D A, Meh, K R, Siebenlist, S O, Brennan, T, Holyst, M W, Mosesson
Publikováno v: Thrombosis and haemostasis. 85(3)
Human fibrin has a low affinity thrombin binding site in its E domain and a high affinity binding site in the carboxy-terminal region of its variant gamma' chain (gamma'408-427). Comparison of the gamma' amino acid sequence (VRPEHPAETEYDSLYPEDDL) wit
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::68552829f919e8e3e5843a373474c82d
https://pubmed.ncbi.nlm.nih.gov/11307817
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10
Evidence for new endothelial cell binding sites on fibrinogen
Autor: R A, Smith, M M, Rooney, S T, Lord, M W, Mosesson, T K, Gartner
Publikováno v: Thrombosis and haemostasis. 84(5)
In vitro assays were used to characterize adhesion of human aortic, microvascular and umbilical vein endothelial cells to various forms of immobilized fibrinogen. All three types of endothelial cells adhered to fibrinogen in a manner that was indepen
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::542ee2db011dd1016fd0c339649e5a11
https://pubmed.ncbi.nlm.nih.gov/11127863
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