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1 directly regulating the protein stability of C-RAF kinase.
2 lent Raf.MEK complexes that are required for c-Raf kinase activation and functional coupling of activ
3 e show that activation of G-kinase inhibited c-Raf kinase activation and that G-kinase phosphorylated
10 igonucleotides that target the mRNA encoding c-Raf kinase and Ha-Ras, we show here that inhibition of
11 protein (RKIP) is a physiologic inhibitor of c-RAF kinase and nuclear factor kappaB signaling that re
12 yl-beta-cyclodextrin disrupted GnRHR but not c-raf kinase association with rafts and shifted the rece
16 oxynucleotides led to specific inhibition of C-raf kinase gene expression in cell culture and in vivo
17 RH induced phosphorylation and activation of c-raf kinase, GnRH treatment led to a decrease in the ap
21 e antisense inhibitor targeted against human C-raf kinase (ISIS 5132, also known as CGP69846A), a ser
22 as/MAP kinase pathway (i) by phosphorylating c-Raf kinase on Ser43 and thereby inhibiting its activat
23 oth in vitro and in vivo; phosphorylation of c-Raf kinase on Ser43 uncouples the Ras-Raf kinase inter
24 activation and that G-kinase phosphorylated c-Raf kinase on Ser43, both in vitro and in vivo; phosph
25 ether, these results indicate that A-Raf and C-Raf kinases play an important role in regulating vascu
27 in the apparent electrophoretic mobility of c-raf kinase that partitioned into lipid rafts compared
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