Zobrazeno 1 - 10
of 50
pro vyhledávání: '"Dorothea Scandella"'
Autor:
Wendy S. Bril, Thomas L. Ortel, Dorothea Scandella, Deborah A. Lewis, Ellen A. M. Turenhout, Edward N. van den Brink, Jan Voorberg, Niels Bovenschen, Marjolein Peters, Marleen G. Zuurveld, Pete Lollar, Koen Mertens, Thynn Thynn Yee
Publikováno v:
Blood, 99(8), 2828-2834. American Society of Hematology
Most plasmas from patients with inhibitors contain antibodies that are reactive with the C2 domain of factor VIII. Previously, we have shown that the variable heavy chain (V(H)) regions of antibodies to the C2 domain are encoded by the closely relate
Autor:
G. Auerswald, Ulrich Budde, H. J. Klose, H. Lenk, Dorothea Scandella, Wolfhart Kreuz, J. Klinge
Publikováno v:
Haemophilia. 7:26-32
Publikováno v:
Haemophilia. 7:13-19
Autor:
Roseline d'Oiron, Alexandre Moreau, Sébastien Lacroix-Desmazes, Dorothea Scandella, Evgueni L. Saenko, Yvette Sultan, N. Stieltjes, Michel D. Kazatchkine, Srini V. Kaveri
Publikováno v:
Europe PubMed Central
We have analyzed the properties of anti-factor VIII (FVIII) immunoglobulin (Ig) G recovered by affinity chromatography on FVIII-Sepharose from the IgG fraction of the plasma of healthy individuals and nonresponder patients with hemophilia A. Affinity
Publikováno v:
Blood. 95:564-568
Factor VIII (fVIII) circulates as a heavy chain/light chain (A1-A2-B/ap-A3-C1-C2) heterodimer. The 41-residue light chain activation peptide, ap, is cleaved from fVIII during proteolytic activation by thrombin or factor Xa. We constructed 7 active re
Autor:
Dorothea Scandella, Philip J. Fay
Publikováno v:
Journal of Biological Chemistry. 274:29826-29830
Factor VIIIa, a heterotrimer of the A1, A2, and A3-C1-C2 subunits, increases the catalytic efficiency for factor IXa-catalyzed activation of factor X. A significant fraction of naturally occurring, anti-factor VIII inhibitor antibodies reacts with th
Autor:
Midori Shima, Hiroshi Suzuki, Ichiro Tanaka, Shogo Morichika, Hiroaki Nakai, Keiji Nogami, Masaru Shibata, John C. Giddings, Dorothea Scandella, Evgueni L. Saenko, Akira Yoshioka
Publikováno v:
British Journal of Haematology. 107:196-203
Factor VIII (FVIII) inhibitor alloantibodies react with combinations of the A2, C2 and A3-C1 domains of the FVIII molecule. Some inhibitors block binding of FVIII to both von Willebrand factor (VWF) and phospholipid, and recognize a C2 domain epitope
Autor:
Marc Hoylaerts, Marc Jacquemin, Dorothea Scandella, Kathelijne Peerlinck, Jean Guy Gilles, Jef Arnout, Karen M. Johnson, Kathleen Freson, Jos Vermylen, Jean-Marie Saint-Remy, Renaud Lavend'homme
Publikováno v:
Blood. 93:2267-2273
Two unrelated patients with the same Arg2150His mutation in the factor VIII (FVIII) C1 domain, a residual FVIII activity of 0.09 IU/mL, and inhibitor titres of 300 and 6 Bethesda Units, respectively, were studied. Further analysis of patient LE, with
Autor:
Kathelijne Peerlinck, Marc G. Jacquemin, Jef Arnout, Marc F. Hoylaerts, Jean Guy G. Gilles, Renaud Lavend’homme, Karen M. Johnson, Kathleen Freson, Dorothea Scandella, Jean-Marie R. Saint-Remy, Jos Vermylen
Publikováno v:
Blood. 93:2267-2273
Two unrelated patients with the same Arg2150His mutation in the factor VIII (FVIII) C1 domain, a residual FVIII activity of 0.09 IU/mL, and inhibitor titres of 300 and 6 Bethesda Units, respectively, were studied. Further analysis of patient LE, with