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Ras inhibitors and related small GTPase modulators act on KRAS and on the Rac, Rho and Cdc42 proteins. Small GTPases of the Ras superfamily work as molecular switches. They cycle between an active form bound to guanosine triphosphate (GTP) and an inactive form bound to guanosine diphosphate (GDP). Oncogenic KRAS mutations such as G12C keep the protein in its signaling state. ARS-853 and KRas G12C inhibitor 4 target the mutant cysteine of KRAS G12C, while Kobe2602 interferes with binding of Ras to Raf. Salirasib, a farnesylcysteine mimetic, disrupts the membrane association of Ras. Rho-family tools include NSC 23766 and EHT 1864, which inhibit Rac, and CASIN, which targets Cdc42.
