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dc.contributor.authorArtal-Sanz, Marta-
dc.contributor.authorTavernarakis, Nektarios-
dc.date.accessioned2009-10-26T08:15:28Z-
dc.date.available2009-10-26T08:15:28Z-
dc.date.issued2009-09-03-
dc.identifier.citationTrends in Endocrinology & Metabolism Volume 20, Issue 8, October 2009, Pages 394-401en_US
dc.identifier.urihttp://hdl.handle.net/10261/17998-
dc.description8 pages, 2 figures.--PMID: 19733482 [PubMed]en_US
dc.description.abstractProhibitins are ubiquitous, evolutionarily conserved proteins that are mainly localized in mitochondria. The mitochondrial prohibitin complex comprises two subunits, PHB1 and PHB2. These two proteins assemble into a ring-like macromolecular structure at the inner mitochondrial membrane and are implicated in diverse cellular processes: from mitochondrial biogenesis and function to cell death and replicative senescence. In humans, prohibitins have been associated with various types of cancer. While their biochemical function remains poorly understood, studies in organisms ranging from yeast to mammals have provided significant insights into the role of the prohibitin complex in mitochondrial biogenesis and metabolism. Here we review recent studies and discuss their implications for deciphering the function of prohibitins in mitochondriaen_US
dc.description.sponsorshipThis work was supported by the European Commission Coordination Action ENINET (contract number LSHM-CT-2005-19063).en_US
dc.format.extent1584512 bytes-
dc.format.mimetypeapplication/pdf-
dc.language.isoengen_US
dc.publisherElsevieren_US
dc.rightsopenAccessen_US
dc.titleProhibitin and mitochondrial biologyen_US
dc.typeartículoen_US
dc.identifier.doi10.1016/j.tem.2009.04.004-
dc.description.peerreviewedPeer revieweden_US
dc.relation.publisherversionhttp://dx.doi.org/10.1016/j.tem.2009.04.004en_US
dc.type.coarhttp://purl.org/coar/resource_type/c_6501es_ES
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item.languageiso639-1en-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.openairetypeartículo-
item.cerifentitytypePublications-
item.grantfulltextopen-
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