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Article: SIRT1 and AMPK in regulating mammalian senescence: A critical review and a working model

TitleSIRT1 and AMPK in regulating mammalian senescence: A critical review and a working model
Authors
KeywordsAging
Energy metabolism
LKB1
Sirtuin
Stress
Issue Date2011
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/febslet
Citation
Febs Letters, 2011, v. 585 n. 7, p. 986-994 How to Cite?
AbstractAgeing in mammals remains an unsolved mystery. Anti-ageing is a recurring topic in the history of scientific research. Lifespan extension evoked by Sir2 protein in lower organisms has attracted a large amount of interests in the last decade. This review summarizes recent evidence supporting the role of a Sir2 mammalian homologue, SIRT1 (Silent information regulator T1), in regulating ageing and cellular senescence. The various signaling networks responsible for the anti-ageing and anti-senescence activity of SIRT1 have been discussed. In particular, a counter-balancing model involving the cross-talks between SIRT1 and AMP-activated protein kinase (AMPK), another stress and energy sensor, is suggested for controlling the senescence program in mammalian © 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reservedcells.
Persistent Identifierhttp://hdl.handle.net/10722/142456
ISSN
2015 Impact Factor: 3.519
2015 SCImago Journal Rankings: 2.026
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorWang, Yen_HK
dc.contributor.authorLiang, Yen_HK
dc.contributor.authorVanhoutte, PMen_HK
dc.date.accessioned2011-10-28T02:46:30Z-
dc.date.available2011-10-28T02:46:30Z-
dc.date.issued2011en_HK
dc.identifier.citationFebs Letters, 2011, v. 585 n. 7, p. 986-994en_HK
dc.identifier.issn0014-5793en_HK
dc.identifier.urihttp://hdl.handle.net/10722/142456-
dc.description.abstractAgeing in mammals remains an unsolved mystery. Anti-ageing is a recurring topic in the history of scientific research. Lifespan extension evoked by Sir2 protein in lower organisms has attracted a large amount of interests in the last decade. This review summarizes recent evidence supporting the role of a Sir2 mammalian homologue, SIRT1 (Silent information regulator T1), in regulating ageing and cellular senescence. The various signaling networks responsible for the anti-ageing and anti-senescence activity of SIRT1 have been discussed. In particular, a counter-balancing model involving the cross-talks between SIRT1 and AMP-activated protein kinase (AMPK), another stress and energy sensor, is suggested for controlling the senescence program in mammalian © 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reservedcells.en_HK
dc.languageengen_US
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/febsleten_HK
dc.relation.ispartofFEBS Lettersen_HK
dc.rightsNOTICE: this is the author’s version of a work that was accepted for publication in FEBS Letters. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in FEBS Letters, 2011, v. 585 n. 7, p. 986-994. DOI: 10.1016/j.febslet.2010.11.047-
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.subjectAgingen_HK
dc.subjectEnergy metabolismen_HK
dc.subjectLKB1en_HK
dc.subjectSirtuinen_HK
dc.subjectStressen_HK
dc.subject.meshAMP-Activated Protein Kinases - metabolism-
dc.subject.meshCell Aging-
dc.subject.meshModels, Biological-
dc.subject.meshSignal Transduction-
dc.subject.meshSirtuin 1 - metabolism-
dc.titleSIRT1 and AMPK in regulating mammalian senescence: A critical review and a working modelen_HK
dc.typeArticleen_HK
dc.identifier.emailWang, Y: yuwanghk@hku.hken_HK
dc.identifier.emailVanhoutte, PM: vanhoutt@hku.hken_HK
dc.identifier.authorityWang, Y=rp00239en_HK
dc.identifier.authorityVanhoutte, PM=rp00238en_HK
dc.description.naturepostprint-
dc.identifier.doi10.1016/j.febslet.2010.11.047en_HK
dc.identifier.pmid21130086-
dc.identifier.scopuseid_2-s2.0-79953239122en_HK
dc.identifier.hkuros184378en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-79953239122&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume585en_HK
dc.identifier.issue7en_HK
dc.identifier.spage986en_HK
dc.identifier.epage994en_HK
dc.identifier.isiWOS:000289057800008-
dc.publisher.placeNetherlandsen_HK
dc.identifier.scopusauthoridWang, Y=34973733700en_HK
dc.identifier.scopusauthoridLiang, Y=35305492300en_HK
dc.identifier.scopusauthoridVanhoutte, PM=7202304247en_HK
dc.identifier.citeulike8367187-

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