Zobrazeno 1 - 10
of 21
pro vyhledávání: '"M J Welham"'
Publikováno v:
Journal of Biological Chemistry. 270:12286-12296
Interleukin-13 (IL-13) and interleukin-4 (IL-4) are related in structure and function and are thought to share a common receptor component. We have investigated the signal transduction pathways activated by these two growth factors, as well as insuli
Publikováno v:
Journal of Biological Chemistry. 269:23764-23768
Binding of interleukin (IL)-3 and granulocyte/macrophage colony-stimulating factor (GM-CSF) to their high affinity cell surface receptors induces tyrosine phosphorylation of a similar set of protein substrates. We have identified one of these common
Publikováno v:
Journal of Biological Chemistry. 269:21165-21176
Shc, grb2, and Son-of-sevenless (mSos1) proteins are potential upstream regulators of p21ras. We show that p52Shc and p46Shc comprise a significant portion of two of the major protein substrates phosphorylated on tyrosine in response to interleukin-2
Publikováno v:
Journal of Biological Chemistry. 269:5865-5873
The activation of erk/mitogen-activated protein kinases and p21ras is strongly associated with progression through the cell cycle. Cell growth induced by the cytokine interleukin-4 (IL-4) effectively dissociates the activation of p44erk-1 and p42erk-
Publikováno v:
The Journal of Immunology. 151:6862-6871
p56lck, a member of the src family of non-receptor protein tyrosine kinases, is expressed almost exclusively in cells of lymphoid origin. p56lck is known to associate with the T lymphocyte surface glycoproteins CD4 and CD8, and plays a critical role
Publikováno v:
The Journal of Immunology. 149:1683-1693
Stimulation of hemopoietic cells with IL-3, IL-4, IL-5, granulocyte-macrophage-CSF and Steel factor-(SLF) induced tyrosine phosphorylation of a number of protein substrates. Two of these proteins, designated p42 and p44, were tyrosine phosphorylated
Autor:
M J Welham, John W. Schrader
Publikováno v:
Molecular and Cellular Biology. 11:2901-2904
We examined the effects of various hemopoietins on c-kit mRNA and protein expression. Interleukin-3 (IL-3), granulocyte-macrophage colony-stimulating factor, and erythropoietin, but not IL-4, down-regulated levels of c-kit mRNA expressed by mast cell
Publikováno v:
The Journal of biological chemistry. 276(26)
We have demonstrated previously that class I(A) phosphoinositide 3-kinases play a major role in regulation of interleukin-3 (IL)-3-dependent proliferation. Investigations into the downstream targets involved have identified the MAPK cascade as a targ
Autor:
H, Bone, M J, Welham
Publikováno v:
Cellular signalling. 12(3)
p46(Shc) and p52(Shc) become heavily tyrosine phosphorylated in response to interleukin 3 (IL-3) treatment. We have investigated the potential of Shc to integrate IL-3 signalling pathways and demonstrate that Shc associates with the beta subunits of
Autor:
H J, Hinton, M J, Welham
Publikováno v:
Journal of immunology (Baltimore, Md. : 1950). 162(12)
Activation of phosphoinositide-3 kinases (PI3Ks), their downstream target protein kinase B (PKB), and phosphorylation of Bad have all been implicated in survival signaling in many systems. However, it is not known whether these events are sufficient