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dc.contributor.author Buday, László
dc.contributor.author Vas, Virág
dc.date.accessioned 2021-05-17T07:27:37Z
dc.date.available 2021-05-17T07:27:37Z
dc.date.issued 2020
dc.identifier.citation journalVolume=39;journalIssueNumber=4;journalTitle=CANCER AND METASTASIS REVIEWS;pagerange=1067-1073;journalAbbreviatedTitle=CANCER METAS REV;
dc.identifier.uri http://repo.lib.semmelweis.hu//handle/123456789/8506
dc.identifier.uri doi:10.1007/s10555-020-09918-2
dc.description.abstract Somatic mutations in the RAS genes are frequent in human tumors, especially in pancreatic, colorectal, and non-small-cell lung cancers. Such mutations generally decrease the ability of Ras to hydrolyze GTP, maintaining the protein in a constitutively active GTP-bound form that drives uncontrolled cell proliferation. Efforts to develop drugs that target Ras oncoproteins have been unsuccessful. Recent emerging data suggest that Ras regulation is more complex than the scientific community has believed for decades. In this review, we summarize advances in the "textbook" view of Ras activation. We also discuss a novel type of Ras regulation that involves direct phosphorylation and dephosphorylation of Ras tyrosine residues. The discovery that pharmacological inhibition of the tyrosine phosphoprotein phosphatase SHP2 maintains mutant Ras in an inactive state suggests that SHP2 could be a novel drug target for the treatment of Ras-driven human cancers.
dc.relation.ispartof urn:issn:0167-7659
dc.title Novel regulation of Ras proteins by direct tyrosine phosphorylation and dephosphorylation
dc.type Journal Article
dc.date.updated 2020-09-24T07:50:02Z
dc.language.rfc3066 en
dc.rights.holder NULL
dc.identifier.mtmt 31607092
dc.identifier.pubmed 32936431
dc.contributor.department SE/AOK/I/Orvosi Vegytani, Molekuláris Biológiai és Patobiokémiai Intézet
dc.contributor.institution Semmelweis Egyetem


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