Zobrazeno 1 - 10
of 26
pro vyhledávání: '"J S, Brugge"'
Publikováno v:
The Journal of Immunology. 158:1650-1659
Engagement of immunoreceptors in hemopoietic cells leads to activation of Src family tyrosine kinases as well as Syk or ZAP-70. Current models propose that Src family kinases are critical in immune response signal transduction through their role in p
Autor:
E A, Clark, J S, Brugge
Publikováno v:
Trends in cardiovascular medicine. 3(6)
Tyrosine phosphorylation has been shown to play a critical role in the induction of cellular responses to extracellular stimuli in a wide variety of cell types. In platelets, many diverse agonists induce multiple waves of tyrosine phosphorylation, su
Autor:
M. Cunningham, J. S. Brugge
Publikováno v:
MD Conference Express. 14:15-16
Publikováno v:
Molecular and Cellular Biology. 12:1835-1845
The amino-termina, noncatalytic half of Src contains two domains, designated the Src homology 2 (SH2) and Src homology 3 (SH3) domains, that are highly conserved among members of the Src family of tyrosine kinases. The SH2 domain (which can be furthe
Autor:
S M, Thomas, M, Hayes, G, D'Arcangelo, R C, Armstrong, B E, Meyer, A, Zilberstein, J S, Brugge, S, Halegoua
Publikováno v:
Molecular and Cellular Biology. 11:4739-4750
PC12 cells treated with nerve growth factor (NGF) or infected with Rous sarcoma virus differentiate into sympathetic, neuronlike cells. To compare the differentiation programs induced by NGF and v-src, we have established a PC12 cell line expressing
Autor:
R J, Lee, C, Albanese, R J, Stenger, G, Watanabe, G, Inghirami, G K, Haines, M, Webster, W J, Muller, J S, Brugge, R J, Davis, R G, Pestell
Publikováno v:
The Journal of biological chemistry. 274(11)
The cyclin D1 gene is overexpressed in breast tumors and encodes a regulatory subunit of cyclin-dependent kinases that phosphorylate the retinoblastoma protein. pp60(c-src) activity is frequently increased in breast tumors; however, the mechanisms go
Publikováno v:
Journal of immunology (Baltimore, Md. : 1950). 158(4)
Engagement of immunoreceptors in hemopoietic cells leads to activation of Src family tyrosine kinases as well as Syk or ZAP-70. Current models propose that Src family kinases are critical in immune response signal transduction through their role in p
Publikováno v:
The Journal of biological chemistry. 269(46)
Agonist stimulation of platelets induces multiple waves of tyrosine phosphorylation, several of which are dependent on the integrin alpha IIb beta 3. At least two classes of protein tyrosine kinases are activated during various stages of platelet act
Publikováno v:
The Journal of biological chemistry. 269(35)
Tyrosine phosphorylation of multiple platelet proteins is regulated by the integrin alpha IIb beta 3. In order to further examine integrin-regulated tyrosine phosphorylation, we have used small Arg-Gly-Asp-containing snake venom proteins (termed disi
Autor:
S J, Shattil, B, Haimovich, M, Cunningham, L, Lipfert, J T, Parsons, M H, Ginsberg, J S, Brugge
Publikováno v:
The Journal of biological chemistry. 269(20)
FAK is a focal adhesion kinase that is phosphorylated on tyrosine in activated platelets. Induction of FAK phosphorylation requires both fibrinogen binding to integrin alpha IIb beta 3 and post-occupancy events during agonist-induced platelet aggrega