Zobrazeno 1 - 10
of 15
pro vyhledávání: '"S C Bailey"'
Autor:
Li Zhai, Randolph B. Lyde, Rodney M. Camire, Denise E. Sabatino, Mortimer Poncz, Michele P. Lambert, Valder R. Arruda, S. C. Bailey, Teshell K. Greene
Publikováno v:
Journal of Thrombosis and Haemostasis. 12:2102-2112
Summary Background Ectopically expressed B-domainless factor VIII in megakaryocytes is stored in α-granules, is effective in a number of murine hemostatic models, and is protected from circulating inhibitors. However, this platelet (p) FVIII has dif
Publikováno v:
Journal of Biological Chemistry. 266:24121-24125
Erythropoietin, the prime regulator of red blood cell growth and differentiation, causes rapid changes in the phosphorylation of several integral plasma membrane proteins (Choi, H-S., Wojchowski, D. M., and Sytkowski, A. J. (1987) J. Biol. Chem. 262,
Publikováno v:
Journal of Biological Chemistry. 266:681-684
The peptide hormone erythropoietin is a major regulator of red blood cell production. While red blood cell development has been studied intensively, little is known about the intracellular signaling events that follow the binding of erythropoietin to
Publikováno v:
Inflammation research : official journal of the European Histamine Research Society ... [et al.]. 44
The preferred method for rank-ordering the potency of topical corticosteroids is the clinical Vasoconstrictor Assay. Measurement of skin blanching in this assay is quantitatible and correlates well with clinical efficacy [1]. But, this test is an ind
Publikováno v:
Inflammation research : official journal of the European Histamine Research Society ... [et al.]. 44
Autor:
S C, Bailey
Publikováno v:
Health estate journal : journal of the Institute of Hospital Engineering. 48(9)
Publikováno v:
Experimental hematology. 21(12)
The binding of erythropoietin (Epo) to its plasma membrane receptor activates signal pathways that result in erythroid cell proliferation and differentiation. To elucidate the structural features of the receptor that are important for hormone binding
Publikováno v:
The Journal of biological chemistry. 266(35)
Erythropoietin, the prime regulator of red blood cell growth and differentiation, causes rapid changes in the phosphorylation of several integral plasma membrane proteins (Choi, H-S., Wojchowski, D. M., and Sytkowski, A. J. (1987) J. Biol. Chem. 262,
Publikováno v:
The Journal of biological chemistry. 266(2)
The peptide hormone erythropoietin is a major regulator of red blood cell production. While red blood cell development has been studied intensively, little is known about the intracellular signaling events that follow the binding of erythropoietin to
Publikováno v:
The Journal of biological chemistry. 265(7)
We have shown previously that purified human erythropoietin rapidly alters the phosphorylation of an integral erythroid membrane protein, pp43 (Choi, H.-S., Wojchowski, D. M., and Sytkowski, A. J. (1987) J. Biol. Chem. 262, 2933-2936). We have now pu