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The structural basis of the activation of Ras by Sos
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title
The structural basis of the activation of Ras by Sos
(English)
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author name string
P A Boriack-Sjodin
series ordinal
1
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S M Margarit
series ordinal
2
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D Bar-Sagi
series ordinal
3
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J Kuriyan
series ordinal
4
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language of work or name
English
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publication date
23 July 1998
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published in
Nature
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volume
394
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page(s)
337-43
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issue
6691
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cites work
The GTPase superfamily: conserved structure and molecular mechanism
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Proteins regulating Ras and its relatives
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Ras activation by insulin and epidermal growth factor through enhanced exchange of guanine nucleotides on p21ras
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Epidermal growth factor regulates p21ras through the formation of a complex of receptor, Grb2 adapter protein, and Sos nucleotide exchange factor
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Grb2 mediates the EGF-dependent activation of guanine nucleotide exchange on Ras
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The Sos (Son of sevenless) protein
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How receptor tyrosine kinases activate Ras.
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Structure of guanine-nucleotide-exchange factor human Mss4 and identification of its Rab-interacting surface
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Structure of the guanine nucleotide exchange factor Sec7 domain of human arno and analysis of the interaction with ARF GTPase
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Structure of the Sec7 domain of the Arf exchange factor ARNO
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The 1.7 A crystal structure of the regulator of chromosome condensation (RCC1) reveals a seven-bladed propeller
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The structure of the Escherichia coli EF-Tu.EF-Ts complex at 2.5 A resolution
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Protein structure comparison by alignment of distance matrices
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Human Sos1: a guanine nucleotide exchange factor for Ras that binds to GRB2
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Kinetic analysis by fluorescence of the interaction between Ras and the catalytic domain of the guanine nucleotide exchange factor Cdc25Mm
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Influence of guanine nucleotides on complex formation between Ras and CDC25 proteins
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Molecular switch for signal transduction: structural differences between active and inactive forms of protooncogenic ras proteins
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Structure of the GDP domain of EF-Tu and location of the amino acids homologous to ras oncogene proteins
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Dominant yeast and mammalian RAS mutants that interfere with the CDC25-dependent activation of wild-type RAS in Saccharomyces cerevisiae
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The Kinetic Mechanism of Ran-Nucleotide Exchange Catalyzed by RCC1
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RAS residues that are distant from the GDP binding site play a critical role in dissociation factor-stimulated release of GDP
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Residues crucial for Ras interaction with GDP-GTP exchangers
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Identification of residues of the H-ras protein critical for functional interaction with guanine nucleotide exchange factors
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Two distinct regions of Ras participate in functional interaction with GDP-GTP exchangers
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Distal switch II region of Ras2p is required for interaction with guanine nucleotide exchange factor.
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Involvement of the switch 2 domain of Ras in its interaction with guanine nucleotide exchange factors
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Inhibition of NIH 3T3 cell proliferation by a mutant ras protein with preferential affinity for GDP.
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Functional cloning of BUD5, a CDC25-related gene from S. cerevisiae that can suppress a dominant-negative RAS2 mutant.
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Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 A resolution: implications for the mechanism of GTP hydrolysis
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Structure of the guanine-nucleotide-binding domain of the Ha-ras oncogene product p21 in the triphosphate conformation
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Identifiers
DOI
10.1038/28548
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stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4556684
Dimensions Publication ID
1021391978
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Fatcat ID
release_ogxh7fdzsbb57jm53ifbjpphrq
1 reference
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Fatcat
reference URL
https://api.fatcat.wiki/v0/release/ogxh7fdzsbb57jm53ifbjpphrq
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24 November 2022
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mapped directly with Wikidata item
OpenCitations bibliographic resource ID
4556684
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4556684
PubMed ID
9690470
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4556684
Springer Nature article ID
10.1038/28548
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