Results 221 to 230 of about 41,746 (257)

Dbl family guanine nucleotide exchange factors

Trends in Biochemical Sciences, 2001
The Dbl family of guanine nucleotide exchange factors are multifunctional molecules that transduce diverse intracellular signals leading to the activation of Rho GTPases. The tandem Dbl-homology and pleckstrin-homology domains shared by all members of this family represent the structural module responsible for catalyzing the GDP-GTP exchange reaction ...
Yi Zheng
exaly   +3 more sources

The guanine nucleotide-exchange factor, eIF-2B

Biochimie, 1994
Eukaryotic initiation factor eIF-2B catalyses the exchange of guanine nucleotides on another translation initiation factor, eIF-2, which itself mediates the binding of the initiator Met-tRNA to the 40S ribosomal subunit during translation initiation. eIF-2B promotes the release of GDP from inactive [eIF-2.GDP] complexes, thus allowing formation of the ...
Christopher G Proud
exaly   +3 more sources

Asef is a Cdc42-specific guanine nucleotide exchange factor

Biological Chemistry, 2007
Asef is a member of the Dbl-family of guanine nucleotide exchange factors (GEFs) with a proposed specificity for the small GTPase Rac1. Here we investigated the specificity and regulation of Asef by measuring its GEF activity in vitro and observed hardly any activity towards Rac1, Rac2 and Rac3, or RhoA and TC10.
Gotthardt, K., Ahmadian, M.
openaire   +5 more sources

Characterization of GFR, a novel guanine nucleotide exchange factor for Rap1

FEBS Letters, 1999
Three groups of Rap1-specific guanine nucleotide exchange factors including C3G, CalDAG-GEFI, and Epac/cAMP-GEFI/II have been identified to date. In the present study, we report a new Rap1 guanine nucleotide exchange factor which we have named GFR ...
Yasutaka Hoshi, Y Eto, Yuji Hoshi
exaly   +2 more sources

Structural outline of the detailed mechanism for elongation factor Ts-mediated guanine nucleotide exchange on elongation factor Tu

Journal of Structural Biology, 2015
Translation elongation factor EF-Tu belongs to the superfamily of guanine-nucleotide binding proteins, which play key cellular roles as regulatory switches. All G-proteins require activation via exchange of GDP for GTP to carry out their respective tasks.
Charlotte R Knudsen
exaly   +2 more sources

A Small Molecule-Regulated Guanine Nucleotide Exchange Factor

Journal of the American Chemical Society, 2009
Selective, pharmacological agents are attractive tools for studying signal transduction because they allow rapid, reversible, and dose-dependent control over intracellular protein function. However, for many targets the identification of potent and selective small molecule agonists and antagonists is a formidable challenge.
Inna, Goreshnik, Dustin J, Maly
openaire   +2 more sources

Mechanism of activation of guanine nucleotide exchange factor by insulin

Endocrine, 1995
Insulin increases activity of the guanine nucleotide exchange factor (GEF) in Rat-1 fibroblasts transfected with human insulin receptors (HIRc cells), thereby promoting formation of the active form of p21Ras (p21Ras•GTP). In order to identify the upstream molecules mediating this aspect of insulin action, we selectively removed some of these molecules ...
J, Langlois, W, Leitner, J, Medh, T, Sasaoka, J M, Olefsky, B, Draznin   +5 more
openaire   +2 more sources

Structural snapshots of the mechanism and inhibition of a guanine nucleotide exchange factor

Nature, 2003
Small GTP-binding (G) proteins are activated by GDP/GTP nucleotide exchange stimulated by guanine nucleotide exchange factors (GEFs). Nucleotide dissociation from small G protein-GEF complexes involves transient GDP-bound intermediates whose structures have never been described.
Renault, Louis, Guibert, Bernard, Cherfils, Jacqueline   +2 more
openaire   +3 more sources