Ras proteins: different signals from different locations

By John Hancock. Nature reviews. Molecular cell biology, 2003

884 citations recorded by the source corpus.

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

Thematic review series: Lipid Posttranslational Modifications. Protein palmitoylation by a family of DHHC protein S-acyltransferases Published, JLR Papers in Press, April 1, 2006. (2006, background): “Yeast Ras proteins, like their mammalian counterparts, require membrane localization to function as signal transducers (22).”
Shaping cups into phagosomes and macropinosomes (2008, background): “These GTPases associate with membranes by regulated exposure of covalently associated acyl chains and by non-covalent interactions with phospholipids or membrane protein”
The RAF proteins take centre stage (2004, background): “As RAS is predominantly attached to the INNER LEAFLET of the plasma membran”
Neuronal polarity: from extracellular signals to intracellular mechanisms (2007, background): “Ras proteins (H-Ras, K-Ras, N-Ras and R-Ras), which are small GTPases that regulate cell growth and differentiatio”
Molecular Dynamics Simulations in Drug Discovery and Pharmaceutical Development (2020, background): “Recently, we conducted a comprehensive analysis of KRAS G domain (excluding the HVR) dynamics by classical all-atom MD simulations, including wild-type KRAS and all G12 missense mutants (G12A, G12C, G12D, G12R, G12S, G12V) bound to both nucleotides GDP and GTP [124].”