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pro vyhledávání: '"Shiraazkhan Abdul"'
Autor:
Shiraazkhan Abdul, Miet Peeters, Els Brouwers, Joyce J M C Malfliet, Frank W G Leebeek, Paul J Declerck, Dingeman C Rijken, Shirley Uitte de Willige
Publikováno v:
PLoS ONE, Vol 13, Iss 5, p e0196911 (2018)
Around 70% of circulating alpha-2-antiplasmin (α2AP), the main natural plasmin inhibitor, is N-terminally cleaved between residues Pro12 and Asn13 by antiplasmin-cleaving enzyme. This converts native Met-α2AP into the more potent fibrinolysis inhib
Externí odkaz:
https://doaj.org/article/e2a6b9d1253348ceb014e9f164bf1048
Autor:
Robert A. S. Ariëns, Shiraazkhan Abdul, Shirley Uitte de Willige, Frank W.G. Leebeek, Dingeman C. Rijken, Dick H. W. Dekkers
Publikováno v:
Journal of Thrombosis and Haemostasis
Journal of Thrombosis and Haemostasis, 18(5), 1162-1170. Wiley-Blackwell Publishing Ltd
Journal of Thrombosis and Haemostasis, 18(5), 1162-1170. Wiley-Blackwell Publishing Ltd
Background: Alpha‐2‐antiplasmin (α2AP) is the main natural inhibitor of plasmin. The C‐terminus of α2AP is crucial for the initial interaction with plasmin(ogen) and the rapid inhibitory mechanism. Approximately 35% of circulating α2AP has l
Autor:
Frank W.G. Leebeek, Joyce J. M. C. Malfliet, S. Uitte de Willige, Shiraazkhan Abdul, Dingeman C. Rijken
Publikováno v:
Journal of Thrombosis and Haemostasis, 14(7), 1453-1461. Wiley-Blackwell Publishing Ltd
textabstractEssentials Factor XIIIa inhibits fibrinolysis by forming fibrin-fibrin and fibrin-inhibitor cross-links. Conflicting studies about magnitude and mechanisms of inhibition have been reported. Factor XIIIa most strongly inhibits lysis of mec
Publikováno v:
Blood, 127(5), 538-545. American Society of Hematology
Human alpha 2-antiplasmin (alpha 2AP, also called alpha 2-plasmin inhibitor) is the main physiological inhibitor of the fibrinolytic enzyme plasmin. alpha 2AP inhibits plasmin on the fibrin clot or in the circulation by forming plasmin-antiplasmin co
Autor:
Joyce J.C.M. Malfliet, Shirley Uitte de Willige, Dingeman C. Rijken, Shiraazkhan Abdul, Frank W.G. Leebeek
Publikováno v:
Thrombosis Research, 166, 19-21. Elsevier Ltd.
Introduction Circulating fibroblast activation protein (cFAP) cleaves alpha-2-antiplasmin (α2AP) N-terminally, converting native Met-α2AP into Asn-α2AP. Previous studies in purified model systems showed that Asn-α2AP is faster incorporated into a
Autor:
Joyce J. M. C. Malfliet, Els Brouwers, Shiraazkhan Abdul, Miet Peeters, Frank W.G. Leebeek, Paul Declerck, Shirley Uitte de Willige, Dingeman C. Rijken
Publikováno v:
PLoS ONE, Vol 13, Iss 5, p e0196911 (2018)
PLoS One (online), 13(5):e0196911. Public Library of Science
PLoS ONE
PLoS One (online), 13(5):e0196911. Public Library of Science
PLoS ONE
Around 70% of circulating alpha-2-antiplasmin (α2AP), the main natural plasmin inhibitor, is N-terminally cleaved between residues Pro12 and Asn13 by antiplasmin-cleaving enzyme. This converts native Met-α2AP into the more potent fibrinolysis inhib