Zobrazeno 1 - 10
of 22
pro vyhledávání: '"W C, Kouns"'
Publikováno v:
Thrombosis Research. 88:109-125
Inhibition of aggregation by Ro 44-9883, a potent and selective non-peptide GPIIb/IIIa antagonist, resulted in inhibition of serotonin secretion induced by weak agonists such as ADP or low doses of either thrombin receptor agonist peptide (TRAP) or c
Autor:
Tatjana V. Byzova, S. G. Khaspekova, Oleg Yu. Tikhomirov, Michael C. Berndt, W. C. Kouns, Beat Steiner, Mazurov Av
Publikováno v:
FEBS Letters. 391:84-88
Platelet glycoprotein (GP) IIb-IIIa complex (alpha IIb beta 3-integrin) changes its conformation upon platelet activation that results in binding of RGD-containing ligands and expression of ligand-induced binding site (LIBS) neoepitopes. Anti-GIIb-II
Autor:
Josef Hübscher, W. C. Kouns, Beat Steiner, Jurg Hurst, Daniel Schlatter, Richard Barner, Walter Huber
Publikováno v:
European Journal of Biochemistry. 227:647-656
The binding reaction between purified human platelet glycoprotein IIb-IIIa and fibrinogen was investigated by real-time measurements using the surface-plasmon-resonance sensor technology. In these experiments, either glycoprotein IIb-IIIa or fibrinog
Autor:
François Lanza, Lisa K. Jennings, Beat Steiner, Sylvie Moog, W. C. Kouns, Joseph Jutzi, Thomas J. Kunicki, Jean-Pierre Cazenave
Publikováno v:
Blood. 84:1108-1115
One proposed ligand binding site on platelet integrin alpha IIb beta 3 is the region of the beta 3 subunit encompassing amino acids 211–221. However, we recently showed that synthetic peptides corresponding to amino acids 211–221 inhibit fibrinog
Publikováno v:
Journal of Biological Chemistry. 269:8754-8761
Integrin alpha IIb-beta 3 binds fibrinogen via the recognition sequence Arg-Gly-Asp-Ser (RGDS). We have used the baculovirus/insect cell expression system to study the structural requirements for the formation of a functionally active fragment of alp
Publikováno v:
Journal of Biological Chemistry. 268:6870-6873
Peptides derived from a sequence within the loop structure of human platelet glycoprotein (GP) IIIa (integrin beta 3) were previously shown to inhibit fibrinogen binding to purified GPIIb-IIIa. In this study a series of peptides based on the GPIIIa s
Autor:
Paul Hadvary, Beat Steiner, Hans R. Baumgartner, D Kirchhofer, G Pfenninger, LK Jennings, A Edenhofer, Thomas Weller, W. C. Kouns
Publikováno v:
Blood. 80:2539-2547
Platelet glycoprotein (GP) IIb-IIIa inhibitors may become useful antithrombotic agents. Ro 4–5054 is a low molecular weight, noncyclic, peptidomimetic inhibitor that is three orders of magnitude more potent than RGDS in inhibiting fibrinogen bindin
Publikováno v:
Journal of Biological Chemistry. 267:18844-18851
This study characterized conformational states of platelet glycoprotein IIb-IIIa (GPIIb-IIIa) and regions of the molecule required for fibrinogen binding. Platelet lysates were passed sequentially over concanavalin A and aminoethylglycine (Aeg)RGDS a
Autor:
Lisa K. Jennings, W C Kouns, PJ Newman, CD Wall, C F Fox, Jerome M. Seyer, AA Miller, KJ Puckett
Publikováno v:
Blood. 78:3215-3223
Glycoprotein (GP) IIb-IIIa serves as the platelet fibrinogen receptor. Studies of the tertiary structure of GPIIIa have shown that the protein has a large loop structure of at least 325 amino acids in length. To further characterize this loop structu
Autor:
W C, Kouns, P J, Newman, K J, Puckett, A A, Miller, C D, Wall, C F, Fox, J M, Seyer, L K, Jennings
Publikováno v:
Blood. 78:3215-3223
Glycoprotein (GP) IIb-IIIa serves as the platelet fibrinogen receptor. Studies of the tertiary structure of GPIIIa have shown that the protein has a large loop structure of at least 325 amino acids in length. To further characterize this loop structu