RAS residues that are distant from the GDP binding site play a critical role in dissociation factor-stimulated release of GDP.
about
Characterization of a guanine nucleotide dissociation stimulator for a ras-related GTPaseIdentification of Rap1 as a target for the Crk SH3 domain-binding guanine nucleotide-releasing factor C3GResidues crucial for Ras interaction with GDP-GTP exchangers.Identification of residues critical for Ras(17N) growth-inhibitory phenotype and for Ras interaction with guanine nucleotide exchange factors.Aberrant function of the Ras-related protein TC21/R-Ras2 triggers malignant transformation.Distinct subclasses of small GTPases interact with guanine nucleotide exchange factors in a similar manner.Distinct structural elements of rab5 define its functional specificity.Identification of residues of the H-ras protein critical for functional interaction with guanine nucleotide exchange factorsA glutamic finger in the guanine nucleotide exchange factor ARNO displaces Mg2+ and the beta-phosphate to destabilize GDP on ARF1.A novel HRAS substitution (c.266C>G; p.S89C) resulting in decreased downstream signaling suggests a new dimension of RAS pathway dysregulation in human development.
P2860
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P2860
RAS residues that are distant from the GDP binding site play a critical role in dissociation factor-stimulated release of GDP.
description
1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
1992年论文
@zh
1992年论文
@zh-cn
name
RAS residues that are distant ...... tor-stimulated release of GDP.
@en
type
label
RAS residues that are distant ...... tor-stimulated release of GDP.
@en
prefLabel
RAS residues that are distant ...... tor-stimulated release of GDP.
@en
P2093
P2860
P1433
P1476
RAS residues that are distant ...... ctor-stimulated release of GDP
@en
P2093
Créchet JB
De Vendittis E
Di Blasi F
Kavounis C
Mirisola MG
Nastopoulos V
Parmeggiani A
Verrotti AC
P2860
P304
P356
10.1002/J.1460-2075.1992.TB05353.X
P407
P577
1992-08-01T00:00:00Z