GEFs and GAPs: critical elements in the control of small G proteins.
By J. Bos, H. Rehmann, A. Wittinghofer. Cell, 2007
1,952 citations recorded by the source corpus.
Subfields: Molecular Biology
View Paper: https://www.semanticscholar.org/paper/745a71d854a0ab9d3fbe078827cdb79952456fd2
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In Molecular Biology
- Rodrigo Vargas Honorato
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- Tatu Pantsar
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- Alexandre M. J. J. Bonvin
- P. Novick
- M. V. van Dijk
Citations in the corpus
- Rho GTPases in cancer cell biology (2008, background): “039 (GAPs), which stimulate the hydrolysis of GTP [3].”
- Role of Rab GTPases in Membrane Traffic and Cell Physiology (2011, background): “However, the structures of several GEF proteins indicate that they directly insert into, or indirectly alter, the Rab nucleotide or magnesium-binding site to cause displacement of the bound nucleotide (38).”
- Molecular Dynamics Simulations in Drug Discovery and Pharmaceutical Development (2020, background): “RAS bears low intrinsic hydrolytic activity, which is greatly enhanced by GTPase activating proteins (GAPs) [98,99].”
- Dragging ras back in the ring. (2014, background): “Several other GAPs are capable of downregulating Ras (Bos et al., 2007).”
- Regulation of mTORC1 by amino acids (2014, neutral): “In cells, GDP dissociation and GTP binding is mediated by guanine nucleotide exchange factors (GEFs) (54).”
- Exploring the free-energy landscape of GPCR activation (2018, background): “8), so with the larger concentration of GTP [∼10 GTP/GDP concentration ratio (58)] the exchange would be energetically favorable.”
- An expanded Ragulator is a GEF for the Rag GTPases that signal amino acid levels to mTORC1 (2012, neutral): “A characteristic of GEFs is their strong preference for binding nucleotide-free over nucleotide-loaded GTPases (Bos et al., 2007; Feig, 1999).”
- Ras superfamily GEFs and GAPs: validated and tractable targets for cancer therapy? (2010, neutral): “ABR, adenomatous polyposis coli (APC) binding region; ANK, ankyrin repeat domain; ARFGEF2, ADP-ribosylation factor guanine nucleotide-exchange factor 2 (also known as BIG2); BAR, Bin1/amphiphysin/Rvs167 domain; BCR, breakpoint cluster region; BRCT, BRCA1 C-terminus domain; CC, coiled-coil domain; CD”