Zobrazeno 1 - 10
of 101
pro vyhledávání: '"G. Claeson"'
Autor:
Rainer Metternich, S R Stone, C Tapparelli, Michael F. Scully, C Ehrhardt, M Zurini, G. Claeson
Publikováno v:
Journal of Biological Chemistry. 268:4734-4741
Peptide boronic acid derivatives have proven to be very potent inhibitors of serine proteases with boroarginine derivatives being particularly potent thrombin inhibitors. The importance of the charged side chain of arginine has been investigated by s
Autor:
G, Claeson
Publikováno v:
Blood coagulationfibrinolysis : an international journal in haemostasis and thrombosis. 5(3)
The synthesis of peptides as imitations of the thrombin cleavage site of fibrinogen has led to sequences with affinity for the enzyme. These peptides were first developed as chromogenic and fluorogenic substrates for thrombin. The same idea was also
Publikováno v:
The Journal of biological chemistry. 268(7)
Peptide boronic acid derivatives have proven to be very potent inhibitors of serine proteases with boroarginine derivatives being particularly potent thrombin inhibitors. The importance of the charged side chain of arginine has been investigated by s
Autor:
E. Agner, Ling-Hao Niu, T. Desoyza, Vijay V. Kakkar, Michael F. Scully, Rainer Metternich, Manfred Philipp, G. Claeson
Publikováno v:
The Biochemical journal. 290
Thrombin, the blood-clotting enzyme, is a serine proteinase with trypsin-like specificity and is able to cleave Arg-Xaa peptide bonds but only in a very limited number of substrates (and sites therein). For the prevention and treatment of thrombosis
Publikováno v:
Advances in experimental medicine and biology. 340
Publikováno v:
Advances in experimental medicine and biology. 340
Publikováno v:
Advances in experimental medicine and biology. 340
Publikováno v:
Advances in Experimental Medicine and Biology ISBN: 9781489924209
In 1956, Bettelheim1 showed that fibrinopeptide A (FPA) competitively inhibits the reaction between thrombin and fibrinogen, that is the amino acid sequence, FPA, preceding the bond split by thrombin has affinity for the enzyme.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f91de4df958ca923e0781565765957e8
https://doi.org/10.1007/978-1-4899-2418-6_8
https://doi.org/10.1007/978-1-4899-2418-6_8
Publikováno v:
Advances in Experimental Medicine and Biology ISBN: 9781489924209
Phosphorus-containing inhibitors, such as diisopropyl phosphorofluoride (DFP), are classical inhibitors of serine proteases. These compounds react irreversibly with the active site serine hydroxy group, forming a covalent adduct. Nonpeptidyl phosphor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2a97c23be3d3032e805e9472dd1bd6c1
https://doi.org/10.1007/978-1-4899-2418-6_15
https://doi.org/10.1007/978-1-4899-2418-6_15
Publikováno v:
Advances in experimental medicine and biology. 340