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RGNEF protein, human

Known as: p190RhoGEF protein, human, 190 kDa Guanine Nucleotide Exchange Factor, p190-RhoGEF 
Rho-guanine nucleotide exchange factor (1705 aa, ~192 kDa) is encoded by the human RGNEF gene. This protein is involved in the mediation of guanine… 
National Institutes of Health

Related topics

Related topics

11 relations
ARHGEF28 geneCell Differentiation processDAG/PE-Binding DomainDH Domain

Broader (2)

Guanine Nucleotide Exchange FactorsRho Guanine Nucleotide Exchange Factors

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
2018
2018
Crystal structures of the PH domains from Lbc family of RhoGEFs bound to activated RhoA GTPase
2014
2014
Follicle stimulating hormone (FSH) induction of aromatase and luteinizing hormone receptor (LHR) is dependent, in part, on the protein kinase a regulatory-rho-guanine nucleotide exchange factor…
2013
2013
Characterization of the Rho-GEF Kalirin-7 in the Mouse Brain: Evidence for a Role in Learning and Addictive-Like Behaviors, as Well as Neuronal Morphology and NMDA Receptor Signaling.
Kalirin-7 (Kal7) is a Rho-guanine nucleotide exchange factor localized to the post-synaptic density (PSD) of neurons in the… 
2012
2012
Rgnef (p190RhoGEF) Knockout Inhibits RhoA Activity, Focal Adhesion Establishment, and Cell Motility Downstream of Integrins
Background Cell migration is a highly regulated process that involves the formation and turnover of cell-matrix contact sites… 
Highly Cited
2009
Highly Cited
2009
The rho-guanine nucleotide exchange factor domain of obscurin activates rhoA signaling in skeletal muscle.
Obscurin is a large ( approximately 800-kDa), modular protein of striated muscle that concentrates around the M-bands and Z-disks… 
Highly Cited
2008
Highly Cited
2008
The rho-guanine nucleotide exchange factor domain of obscurin regulates assembly of titin at the Z-disk through interactions with Ran binding protein 9.
Obscurin is an approximately 800-kDa protein composed of structural and signaling domains that organizes contractile structures… 
2005
2005
Fluorescence approaches for monitoring interactions of Rho GTPases with nucleotides, regulators, and effectors.
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