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- W2775307197 endingPage "130" @default.
- W2775307197 startingPage "121" @default.
- W2775307197 abstract "For decades oncogenic RAS proteins were considered undruggable due to a lack of accessible binding pockets on the protein surfaces. Seminal early research in RAS biology uncovered the basic paradigm of post-translational isoprenylation of RAS polypeptides, typically with covalent attachment of a farnesyl group, leading to isoprenyl-mediated RAS anchorage at the plasma membrane and signal initiation at those sites. However, the failure of farnesyltransferase inhibitors to translate to the clinic stymied anti-RAS therapy development. Over the past ten years, a more complete picture has emerged of RAS protein maturation, intracellular trafficking, and location, positioning and retention in subdomains at the plasma membrane, with a corresponding expansion in our understanding of how these properties of RAS contribute to signal outputs. Each of these aspects of RAS regulation presents a potential vulnerability in RAS function that may be exploited for therapeutic targeting, and inhibitors have been identified or developed that interfere with RAS for nearly all of them. This review will summarize current understanding of RAS membrane targeting with a focus on highlighting development and outcomes of inhibitors at each step." @default.
- W2775307197 created "2017-12-22" @default.
- W2775307197 creator A5003137587 @default.
- W2775307197 creator A5012588951 @default.
- W2775307197 date "2019-02-01" @default.
- W2775307197 modified "2023-09-29" @default.
- W2775307197 title "Concepts and advances in cancer therapeutic vulnerabilities in RAS membrane targeting" @default.
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