Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Patricia A. Morateck"'
Autor:
Qizhen Shi, Scot A. Fahs, Jeremy G. Mattson, Hongyin Yu, Crystal L. Perry, Patricia A. Morateck, Jocelyn A. Schroeder, Jessica Rapten, Hartmut Weiler, Robert R. Montgomery
Publikováno v:
Blood advances. 6(9)
Type 2N von Willebrand disease is caused by mutations in the factor VIII (FVIII) binding site of von Willebrand factor (VWF), resulting in dysfunctional VWF with defective binding capacity for FVIII. We developed a novel type 2N mouse model using CRI
Autor:
Stefana Gavazova, Michael Balistreri, Patricia A. Morateck, Joan Cox Gill, Marilyn J. Manco-Johnson, Sandra L. Haberichter, Daniel B. Bellissimo, Robert R. Montgomery, Pamela A. Christopherson
Publikováno v:
Blood. 108:3344-3351
Type 1 von Willebrand disease (VWD) is characterized by a partial quantitative deficiency of von Willebrand factor (VWF). Few VWF gene mutations have been identified that cause dominant type 1 VWD. The decreased survival of VWF in plasma has recently
Autor:
Qizhen Shi, Clive Wells, Hartmut Weiler, Drashti Desai, Jack Gorski, David A. Wilcox, Brian C. Cooley, Patricia A. Morateck, Robert R. Montgomery, Scot A. Fahs
Publikováno v:
Journal of Clinical Investigation. 116:1974-1982
Inhibitory immune response to exogenously infused factor VIII (FVIII) is a major complication in the treatment of hemophilia A. Generation of such inhibitors has the potential to disrupt gene therapy for hemophilia A. We explore what we believe to be
Autor:
Patricia A. Morateck, Qizhen Shi, D. Kenny, Robert R. Montgomery, David A. Wilcox, Scot A. Fahs
Publikováno v:
Journal of Thrombosis and Haemostasis. 2:1989-1997
Bernard-Soulier Syndrome (BSS) is a severe congenital platelet disorder that results from a deficiency of the platelet membrane glycoprotein (GP) Ib/IX complex that is composed of four subunits (GPIbalpha, GPIbbeta, GPIX, and GPV). Mutations in eithe
Publikováno v:
Blood. 99:4428-4433
The glycoprotein Ib (GPIb) complex is composed of GPIbα covalently attached to GPIbβ and noncovalently complexed with GPIX and GPV. Patients with Bernard-Soulier syndrome demonstrate that mutations in either GPIbβ or GPIX result in an absence of p
Autor:
Desmond J. Fitzgerald, Michelle Ryan, Dermot Kenny, Adele Deering, Robert R. Montgomery, Niamh Moran, Patricia A. Morateck
Publikováno v:
Blood. 96:532-539
Bernard-Soulier syndrome is a rare bleeding disorder caused by a quantitative or qualitative defect in the platelet glycoprotein (GP) Ib-IX-V complex. The complex, which serves as a platelet receptor for von Willebrand factor, is composed of 4 subuni
Publikováno v:
Blood. 93:2968-2975
Bernard-Soulier syndrome is an uncommon bleeding disorder caused by a quantitative or qualitative defect in the platelet glycoprotein (GP)Ib/IX complex. The complex is composed of four subunits, GPIb, GPIbβ, GPIX, and GPV. Here we describe the mo
Publikováno v:
Thrombosis and Haemostasis. 82:1327-1333
SummaryThe interaction of the glycoprotein (GP) Ib-IX-V complex with von Willebrand factor (vWF) is critical in initiation of haemostasis and thrombosis through platelet adhesion to damaged endothelium. The binding site for vWF resides within the GPI
Publikováno v:
Blood. 92:175-183
The platelet GPIb-V-IX complex is the receptor for the initial binding of von Willebrand factor (vWF) mediating platelet adhesion. The complex is composed of four membrane-spanning glycoproteins (GP): GPIbalpha, GPIbbeta, GPIX, and GPV. Bernard-Souli
Publikováno v:
Blood. 90:2626-2633
The platelet membrane glycoprotein (GP)Ib-V-IX complex is the receptor for von Willebrand factor and is composed of four membrane-spanning polypeptides: GPIbα, GPIbβ, GPIX, and GPV. A qualitative or quantitative deficiency in the GPIb-V-IX complex