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Structure of RGS4 bound to AlF4--activated G(i alpha1): stabilization of the transition state for GTP hydrolysis
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Europe PubMed Central
PubMed ID
9108480
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9108480%20AND%20SRC:MED&resulttype=core&format=json
retrieved
2 November 2019
title
Structure of RGS4 bound to AlF4--activated G(i alpha1): stabilization of the transition state for GTP hydrolysis
(English)
1 reference
stated in
Europe PubMed Central
PubMed ID
9108480
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9108480%20AND%20SRC:MED&resulttype=core&format=json
retrieved
2 November 2019
author
John Tesmer
series ordinal
1
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Europe PubMed Central
PubMed ID
9108480
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9108480%20AND%20SRC:MED&resulttype=core&format=json
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2 November 2019
author name string
D M Berman
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2
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Europe PubMed Central
PubMed ID
9108480
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9108480%20AND%20SRC:MED&resulttype=core&format=json
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2 November 2019
A G Gilman
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3
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Europe PubMed Central
PubMed ID
9108480
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9108480%20AND%20SRC:MED&resulttype=core&format=json
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2 November 2019
S R Sprang
series ordinal
4
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Europe PubMed Central
PubMed ID
9108480
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9108480%20AND%20SRC:MED&resulttype=core&format=json
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2 November 2019
language of work or name
English
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publication date
1 April 1997
1 reference
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Europe PubMed Central
PubMed ID
9108480
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9108480%20AND%20SRC:MED&resulttype=core&format=json
retrieved
2 November 2019
published in
Cell
1 reference
stated in
Europe PubMed Central
PubMed ID
9108480
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9108480%20AND%20SRC:MED&resulttype=core&format=json
retrieved
2 November 2019
volume
89
1 reference
stated in
Europe PubMed Central
PubMed ID
9108480
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9108480%20AND%20SRC:MED&resulttype=core&format=json
retrieved
2 November 2019
page(s)
251-261
1 reference
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Europe PubMed Central
PubMed ID
9108480
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9108480%20AND%20SRC:MED&resulttype=core&format=json
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2 November 2019
issue
2
1 reference
stated in
Europe PubMed Central
PubMed ID
9108480
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9108480%20AND%20SRC:MED&resulttype=core&format=json
retrieved
2 November 2019
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The GTPase-activating protein RGS4 stabilizes the transition state for nucleotide hydrolysis
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GAIP and RGS4 are GTPase-activating proteins for the Gi subfamily of G protein alpha subunits
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RGS-r, a retinal specific RGS protein, binds an intermediate conformation of transducin and enhances recycling
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GAIP, a protein that specifically interacts with the trimeric G protein G alpha i3, is a member of a protein family with a highly conserved core domain
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Sst2, a negative regulator of pheromone signaling in the yeast Saccharomyces cerevisiae: expression, localization, and genetic interaction and physical association with Gpa1 (the G-protein alpha subunit).
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RGS proteins and signaling by heterotrimeric G proteins
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Inhibition of G-protein-mediated MAP kinase activation by a new mammalian gene family
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Accurate bond and angle parameters for X-ray protein structure refinement
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Mutational and kinetic analyses of the GTPase-activating protein (GAP)-p21 interaction: the C-terminal domain of GAP is not sufficient for full activity
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G proteins: transducers of receptor-generated signals
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RGS4 and GAIP are GTPase-activating proteins for Gq alpha and block activation of phospholipase C beta by gamma-thio-GTP-Gq alpha
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RGS10 is a selective activator of G alpha i GTPase activity
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Mechanism of GTP hydrolysis by G-protein alpha subunits
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EGL-10 regulates G protein signaling in the C. elegans nervous system and shares a conserved domain with many mammalian 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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Formation of a Transition-State Analog of the Ras GTPase Reaction by Ras GDP, Tetrafluoroaluminate, and GTPase-Activating Proteins
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Heterotrimeric G proteins: organizers of transmembrane signals
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X-ray crystal structures of transforming p21 ras mutants suggest a transition-state stabilization mechanism for GTP hydrolysis
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Conformation of Polypeptides and Proteins
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Crystal structure of the GTPase-activating domain of human p120GAP and implications for the interaction with Ras
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GTPase mechanism of Gproteins from the 1.7-A crystal structure of transducin alpha-GDP-AIF-4
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Yeast and mammalian ras proteins have conserved biochemical properties
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CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
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A cytoplasmic protein stimulates normal N-ras p21 GTPase, but does not affect oncogenic mutants
1 reference
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7 January 2021
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The structure of the G protein heterotrimer Gi alpha 1 beta 1 gamma 2
1 reference
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7 January 2021
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RGS family members: GTPase-activating proteins for heterotrimeric G-protein alpha-subunits
1 reference
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7 January 2021
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Structural and functional diversity in 4-α-helical proteins
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7 January 2021
based on heuristic
inferred from DOI database lookup
Identifiers
DOI
10.1016/S0092-8674(00)80204-4
1 reference
stated in
Europe PubMed Central
PubMed ID
9108480
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9108480%20AND%20SRC:MED&resulttype=core&format=json
retrieved
2 November 2019
PubMed ID
9108480
1 reference
stated in
Europe PubMed Central
PubMed ID
9108480
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9108480%20AND%20SRC:MED&resulttype=core&format=json
retrieved
2 November 2019
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