Small molecule stabilization of the KSR inactive state antagonizes oncogenic Ras signalling - Dhawan, Neil S.; Scopton, Alex P.; Dar, Arvin C. (Nature (London), 2016)
Keywords: 13; 631/45/275; 631/67/1059/602; 631/80/86/2368; 631/92; 82; 82/83; 96; 96/98; Alleles; Allosteric Regulation - drug effects; BASIC BIOLOGICAL SCIENCES; Cancer; Cancer treatment; Care and treatment; Cell Line; Chemical biology; Crystal structure; Deregulation; Enzyme Stability - drug effects; Genes; Growth factor signalling; Humanities and Social Sciences; Humans; Kinases; letter; Ligands; MAP Kinase Signaling System - drug effects; Methods; Mitogen-Activated Protein Kinase Kinases - antagonists & inhibitors; Mitogen-Activated Protein Kinase Kinases - chemistry; Mitogen-Activated Protein Kinase Kinases - metabolism; Models, Molecular; multidisciplinary; Mutation; Neoplasms - drug therapy; Neoplasms - enzymology; Neoplasms - genetics; Neoplasms - metabolism; Oncogenes - drug effects; Oncogenes - genetics; Phosphorylation; Phosphorylation - drug effects; Phosphotransferases; Physiological aspects; Protein Binding; Protein Conformation - drug effects; Protein Multimerization - drug effects; Protein-Serine-Threonine Kinases - chemistry; Protein-Serine-Threonine Kinases - genetics; Protein-Serine-Threonine Kinases - metabolism; Pyridones - pharmacology; Pyrimidinones - pharmacology; Quinazolines - pharmacology; raf Kinases - chemistry; raf Kinases - metabolism; Ras genes; ras Proteins - antagonists & inhibitors; ras Proteins - genetics; ras Proteins - metabolism; Science; Signal transduction; Targeted therapies