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dc.contributor.authorShackleton, S
dc.contributor.authorSmallwood, Dawn T.
dc.date.accessioned2019-11-12T15:57:06Z
dc.date.available2019-11-12T15:57:06Z
dc.date.issued2010-01-19
dc.identifier.citationSmallwood, D.T., Shackleton, S. (2010) Lamin A-linked progerias: is farnesylation the be all and end all? Biochemical Society Transactions, 38(1), pp. 281–286.en
dc.identifier.issn1470-8752
dc.identifier.urihttps://dora.dmu.ac.uk/handle/2086/18780
dc.descriptionThe Publisher's final version can be found by following the DOI link.en
dc.description.abstractHGPS (Hutchinson-Gilford progeria syndrome) is a severe childhood disorder that appears to mimic an accelerated aging process. The disease is most commonly caused by gene mutations that disrupt the normal post-translational processing of lamin A, a structural component of the nuclear envelope. Impaired processing results in aberrant retention of a farnesyl group at the C-terminus of lamin A, leading to altered membrane dynamics. It has been widely proposed that persistence of the farnesyl moiety is the major factor responsible for the disease, prompting clinical trials of farnesyltransferase inhibitors to prevent lamin A farnesylation in children afflicted with HGPS. Although there is evidence implicating farnesylation in causing some of the cellular defects of HGPS, results of several recent studies suggest that aberrant lamin A farnesylation is not the only determinant of the disease. These findings have important implications for the design of treatments for this devastating disease.en
dc.language.isoenen
dc.publisherPortland Pressen
dc.subjectProgeriaen
dc.subjectPrenylationen
dc.subjectFarnesyltranstransferaseen
dc.subjectNuclear Envelopeen
dc.subjectLamin Type Aen
dc.subjectHumanen
dc.titleLamin A-linked progerias: is farnesylation the be all and end all?en
dc.typeArticleen
dc.identifier.doihttps://doi.org/10.1042/BST0380281
dc.peerreviewedYesen
dc.funderNo external funderen
dc.cclicenceCC-BY-NCen
dc.date.acceptance2010-01
dc.researchinstituteInstitute for Allied Health Sciences Researchen
dc.exception.ref2021codes254aen


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