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- W41879369 abstract "The Ras superfamily of small GTPases is composed of more than 150 members, which share a conserved structure and biochemical properties, acting as binary molecular switches turned on by binding GTP and off by hydrolyzing GTP to GDP. However, despite considerable structural and biochemical similarities, these proteins play multiple and divergent roles, being versatile and key regulators of virtually all fundamental cellular processes. Conversely, their dysfunction plays a crucial role in the pathogenesis of serious human diseases, including cancer and developmental syndromes. Fuelled by the original identification in 1982 of mutationally activated and transforming human Ras genes in human cancer cell lines, a variety of powerful experimental techniques have been intensively focused on discovering and studying structure, biochemistry, and biology of Ras and Ras-related small GTPases, leading to fundamental research breakthroughs into identification and structural and functional characterization of a huge number of Ras superfamily members, as well as of their multiple regulators and effectors. In this review we provide a general overview of the major milestones that eventually allowed to unlock the secret treasure chest of this large and important superfamily of proteins." @default.
- W41879369 created "2016-06-24" @default.
- W41879369 creator A5008045147 @default.
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- W41879369 creator A5085711134 @default.
- W41879369 date "2013-12-26" @default.
- W41879369 modified "2023-10-16" @default.
- W41879369 title "The Ras Superfamily of Small GTPases: The Unlocked Secrets" @default.
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- W41879369 doi "https://doi.org/10.1007/978-1-62703-791-4_1" @default.
- W41879369 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/24470015" @default.
- W41879369 hasPublicationYear "2013" @default.