Zobrazeno 1 - 10
of 25
pro vyhledávání: '"S. G. Macdonald"'
Publikováno v:
Science. 265:1713-1716
To identify proteins that may participate in the activation of the protein kinase Raf, proteins that interact with Raf were selected in a two-hybrid screen. Two members of the 14-3-3 protein family were isolated that interacted with both the amino te
Publikováno v:
Molecular and Cellular Biology. 14:4722-4730
Plasma membrane targeting of Ras requires CAAX motif modifications together with a second signal from an adjacent polybasic domain or nearby cysteine palmitoylation sites. N-terminal myristoylation is known to restore membrane binding to H-ras C186S
Publikováno v:
Science. 264:1463-1467
The small guanine nucleotide binding protein Ras participates in a growth promoting signal transduction pathway. The mechanism by which interaction of Ras with the protein kinase Raf leads to activation of Raf was studied. Raf was targeted to the pla
Publikováno v:
Molecular Biology of the Cell. 5:173-181
Raf-1 is a serine/threonine kinase that acts downstream of Ras in mitogenic signal transduction pathways, but the mechanism by which Ras transmits signals to Raf-1 is not known. We have examined the interaction between Raf-1 and human H-ras in three
Autor:
S. G. Macdonald, J. Driller, Frank McCormick, R Clark, Craig M. Crews, Lelia Wu, R. L. Erikson
Publikováno v:
Molecular and Cellular Biology. 13:6615-6620
Raf-1 is a serine/threonine kinase which is essential in cell growth and differentiation. Tyrosine kinase oncogenes and receptors and p21ras can activate Raf-1, and recent studies have suggested that Raf-1 functions upstream of MEK (MAP/ERK kinase),
Autor:
S G, Macdonald
Publikováno v:
Proceedings of the Royal Society of Medicine. 26(4)
Autor:
S G, Macdonald
Publikováno v:
Proceedings of the Royal Society of Medicine. 20(11)
Autor:
S G, Macdonald
Publikováno v:
Proceedings of the Royal Society of Medicine. 15
Autor:
S G, Macdonald
Publikováno v:
Proceedings of the Royal Society of Medicine. 24(1)
Publikováno v:
Biochemistry. 35(9)
We have previously shown that the high-affinity binding of substance P (SP) to its receptor is dependent on an interaction with a PTX-insensitive G protein. This G protein couples SP receptor activation to stimulation of its effector, phospholipase C