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1 GRF1 can also mediate high frequency stimulation-induced
2 pathways include GROWTH REGULATORY FACTOR 1 (GRF1), PHOSPHATIDYLINOSITOL 4-KINASE beta1 (PI-4Kbeta1),
5 t functions, WT and various chimeras between GRF1 and GRF2 proteins were tested for their abilities t
7 This led to a significant reduction in both GRF1-dependent ERK phosphorylation and AP1-dependent rep
9 tional inactivation of oligomer formation by GRF1 is associated with impaired biological and signalin
10 signaling activities, and that in 293T cells GRF1 mediates at least two pathways for Raf activation:
11 lated an Arabidopsis 14-3-3 gene, designated GRF1-GF14 chi (for general regulatory factor1-G-box fact
15 phosphorylation, consistent with a role for GRF1 in calcium-dependent Ras signaling in these cells.
18 the Ras-specific exchange factors Ras-GRF1 (GRF1) and Ras-GRF2 (GRF2), which are expressed in brain
19 eptors in the CA1 region of the hippocampus, GRF1 promotes LTD, whereas GRF2 promotes theta-burst sti
25 strin homology and/or coiled-coil domains of GRF1 are key to the induction of HFS-LTP by GRF proteins
26 rat brain extract, and forced expression of GRF1 and GRF2 in cultured mammalian cells formed homo- a
27 ated, at least in part, by the expression of GRF1 and possibly other transcription factors of the GRF
29 ein whose N terminus is identical to that of GRF1, a calcium-dependent guanine nucleotide exchange fa
30 smid encoding a dominant negative variant of GRF1 led to 70% reduction in ERK phosphorylation, consis
40 s-guanine nucleotide-releasing factor 1 (Ras-GRF1) and Ras-GRF2 are highly similar calcium-stimulated
41 s-guanine nucleotide-releasing factor 1 (Ras-GRF1), a neuronal activator of Ras proteins, causes a sp
42 as guanine nucleotide exchange factor 1, Ras-GRF1, by microarray analysis as a c-Jun/AP-1 regulated g
44 CaMKI, the Ca2+-stimulated Ras activator Ras-GRF1 (Ras-guanyl-nucleotide releasing factor), and ERK.
45 showed that beginning at 1 month of age, RAS-GRF1 mediates NMDA-type glutamate receptor (NMDAR)-induc
50 al amino acid exchanges between Sos1 and Ras-GRF1 revealed that the critical amino acids reside withi
54 rdinated activation of H-Ras and Rac1 by Ras-GRF1 may be a significant controller of neuronal cell si
55 onic L-DOPA treatment reveals a complex, Ras-GRF1 and pathway-independent, apparently stochastic invo
56 minate between closely related contexts, RAS-GRF1 begins to contribute to the induction of long term
58 ons of the Ras-specific exchange factors Ras-GRF1 (GRF1) and Ras-GRF2 (GRF2), which are expressed in
63 catalytically inactive dominant negative Ras-GRF1, which prevented ERK activation, reduced MMP-9 expr
69 nfirmed the regulated phosphorylation of Ras-GRF1 by Western blotting in both model systems of transf
71 thus could contribute to the function of Ras-GRF1 in neuronal signal transduction pathways that under
72 x, there was striking phosphorylation of Ras-GRF1 in the dendritic tree, supporting a role for Ras ac
79 th destabilization and ubiquitylation of Ras-GRF1, a guanine nucleotide exchange factor that activate
80 d not, however, increase the activity of Ras-GRF1, indicating that it is not sufficient for activatio
81 proteins Ha-Ras, N-Ras, and Ki-Ras, only Ras-GRF1 also activates the functionally distinct R-Ras GTPa
83 ells potentiates the ability of Tiam1 or Ras-GRF1 to activate the p38 MAP kinase cascade but not the
84 similar functional domain organization, Ras-GRF1 and Ras-GRF2 mediate opposing forms of synaptic pla
86 exchange factors revealed that both p140 Ras-GRF1 and p130 Ras-GRF2 couple NMDA glutamate receptors (
89 that c-Jun/AP-1 regulates endogenous p75-Ras-GRF1 expression and that c-Jun/AP-1-regulated anchorage-
91 75-kDa c-Jun/AP-1-inducible protein, p75-Ras-GRF1, was detected, and the inhibition of its expression
92 termed 2152) that selectively recognizes Ras-GRF1 when it is phosphorylated at Ser(916/898) confirmed
93 through the calcium/calmodulin regulated Ras-GRF1 and Ras-GRF2 exchange factors, which form AMPA-indu
99 ngly, LTP induction by CP-AMPARs through RAS-GRF1 occurs via activation of p38 MAP kinase rather than
101 nduction of NMDAR-dependent LTP, whereas Ras-GRF1 contributes predominantly to the induction of NMDAR
103 ze plants overexpressing miRNA396a-resistant GRF1 support a model proposing that distinct association
107 in Erk activity induced by ionomycin in the GRF1-expressing cells also induced a concomitant increas
108 cus-forming activity on NIH 3T3 cells of the GRF1 DH cluster mutant was reduced, while the L263Q muta
109 -263 to Gln (L263Q) in the N terminus of the GRF1 DH domain abolished the two-hybrid interaction, whi
112 f ionomycin, 293T cells expressing wild-type GRF1 contained much higher levels of Ras-GTP than contro
114 t was deficient in oligomer formation, while GRF1 containing the DH cluster mutations formed homo-oli