Zobrazeno 1 - 10
of 98
pro vyhledávání: '"L M, Regan"'
Publikováno v:
Journal of Biological Chemistry. 266:16219-16225
In CD4+ T cells, the src-like tyrosine kinase pp56lck is associated with the CD4 receptor and cross-linking of CD4 results in the activation of this enzyme. The mechanism responsible for this activation is not known, although there is evidence that t
Publikováno v:
Haematologica. 84(3)
The molecular links between inflammation and coagulation are unquestioned. Inflammation promotes coagulation by leading to intravascular tissue factor expression, eliciting the expression of leukocyte adhesion molecules on the intravascular cell surf
Autor:
C T, Esmon, W, Ding, K, Yasuhiro, J M, Gu, G, Ferrell, L M, Regan, D J, Stearns-Kurosawa, S, Kurosawa, T, Mather, Z, Laszik, N L, Esmon
Publikováno v:
Thrombosis and haemostasis. 78(1)
Publikováno v:
The Journal of biological chemistry. 271(29)
A soluble form of the endothelial cell protein C receptor (EPCR) was analyzed for the ability to modulate the functional properties of protein C and activated protein C (APC). In a plasma clotting system initiated with factor Xa, EPCR blocked the ant
Publikováno v:
The Journal of biological chemistry. 271(11)
The intrinsic factor Xase complex (FXase) is comprised of a serine protease, FIXa, and a protein cofactor, FVIIIa, assembled on a phospholipid surface. Activity of FXase decays with time and reflects the lability of FVIIIa. Two mechanisms potentially
Publikováno v:
The Journal of biological chemistry. 269(32)
Factor VIIIa is a non-covalent heterotrimer of A1, A2, and A3-C1-C2 subunits. Previously, we speculated that the central portion of the A2 subunit, in and around the activated protein C-sensitive bond at Arg562-Gly (Fay, P. J., Smudzin, T.M., and Wal
Publikováno v:
The Journal of biological chemistry. 269(13)
Factor VIIIa is inactivated by both factor IXa and activated protein C. The latter protease rapidly attacked a site at Arg562 (A2 subunit), whereas both proteases slowly cleaved factor VIIIa at Arg336 (A1 subunit). Cofactor inactivation catalyzed by
Publikováno v:
The Journal of biological chemistry. 266(24)
In CD4+ T cells, the src-like tyrosine kinase pp56lck is associated with the CD4 receptor and cross-linking of CD4 results in the activation of this enzyme. The mechanism responsible for this activation is not known, although there is evidence that t
Autor:
Gudka, Mishal, Obura, David, Treml, Eric, Samoilys, Melita, Aboud, Swaleh A., Osuka, Kennedy Edeye, Mbugua, James, Mwaura, Jelvas, Karisa, Juliet, Knoester, Ewout Geerten, Musila, Peter, Omar, Mohamed, Nicholson, Emily
Publikováno v:
Conservation Science & Practice; Dec2024, Vol. 6 Issue 12, p1-16, 16p
Publikováno v:
Methods in Ecology & Evolution; Apr2024, Vol. 15 Issue 4, p612-627, 16p