Dimerization of Cdc25p, the guanine-nucleotide exchange factor for Ras from Saccharomyces cerevisiae, and its interaction with Sdc25p.
about
Oligomerization of DH domain is essential for Dbl-induced transformationRas-specific exchange factor GRF: oligomerization through its Dbl homology domain and calcium-dependent activation of RafA role for the noncatalytic N terminus in the function of Cdc25, a Saccharomyces cerevisiae Ras-guanine nucleotide exchange factor.Protein–protein interactions and selection: yeast-based approaches that exploit guanine nucleotide-binding protein signaling.p55-hGRF, a short natural form of the Ras-GDP exchange factor high yield production and characterization.
P2860
Dimerization of Cdc25p, the guanine-nucleotide exchange factor for Ras from Saccharomyces cerevisiae, and its interaction with Sdc25p.
description
1997 nî lūn-bûn
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1997年の論文
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1997年学术文章
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1997年学术文章
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1997年学术文章
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1997年学术文章
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1997年学术文章
@zh-sg
1997年學術文章
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1997年學術文章
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1997年學術文章
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name
Dimerization of Cdc25p, the gu ...... d its interaction with Sdc25p.
@en
Dimerization of Cdc25p, the gu ...... d its interaction with Sdc25p.
@nl
type
label
Dimerization of Cdc25p, the gu ...... d its interaction with Sdc25p.
@en
Dimerization of Cdc25p, the gu ...... d its interaction with Sdc25p.
@nl
prefLabel
Dimerization of Cdc25p, the gu ...... d its interaction with Sdc25p.
@en
Dimerization of Cdc25p, the gu ...... d its interaction with Sdc25p.
@nl
P2093
P2860
P1433
P1476
Dimerization of Cdc25p, the gu ...... d its interaction with Sdc25p.
@en
P2093
M Geymonat
S Baudet-Nessler
P2860
P304
P356
10.1111/J.1432-1033.1997.00703.X
P407
P577
1997-07-01T00:00:00Z