Results 261 to 270 of about 84,425 (312)

Expanding functions of GIT Arf GTPase-activating proteins, PIX Rho guanine nucleotide exchange factors and GIT-PIX complexes.

J Cell Sci, 2016
Zhou W, Li X, Premont RT.
europepmc   +1 more source

Regulated localization is sufficient for hormonal control of regulator of G protein signaling homology Rho guanine nucleotide exchange factors (RH-RhoGEFs). [PDF]

J Biol Chem, 2014
Carter AM, Gutowski S, Sternweis PC.
europepmc   +1 more source

Overexpression of GEFT, a Rho family guanine nucleotide exchange factor, predicts poor prognosis in patients with rhabdomyosarcoma.

, 2014
Chao Sun, Chunxia Liu, Shugang Li, Hong-an Li, Yuanyuan Wang, Yuwen Xie, Bingcheng Li, Xiaobin Cui, Yunzhao Chen, Wenjie Zhang, Feng Li   +10 more
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The Guanine Exchange Factor <i>SsEFA6</i> Participates in Appressorium Formation and Virulence in <i>Sclerotinia sclerotiorum</i>. [PDF]

J Fungi (Basel)
Wang K, Wang T, Xia Q, Xie N, Cao J, Xia S.   +5 more
europepmc   +1 more source

Optimized conditions for GTP loading of Ras. [PDF]

J Biol Chem
Vish KJ, Paul ME, Rollins AP, Boggon TJ.
europepmc   +1 more source

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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 ...
N, Price, C, Proud
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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 ...
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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
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Guanine nucleotide exchange factors: Activators of Ras superfamily proteins

Molecular Reproduction and Development, 1995
AbstractMembers of the Ras superfamily of proteins function as regulated GDP/GTP switches that cycle between active GTP‐complexed and inactive GDP‐complexed states. Guanine nucleotide exchange factors (GEFs) stimulate formation of the GTP‐bound state, whereas GTPase activating proteins (GAPs) catalyze the formation of the GDP‐bound state.
A F, Overbeck, T R, Brtva, A D, Cox, S M, Graham, S Y, Huff, R, Khosravi-Far, L A, Quilliam, P A, Solski, C J, Der   +8 more
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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.
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