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dc.contributor.author Silberman, Dafne Magali
dc.contributor.author Mostoslavsky, Raul
dc.date.available 2017-06-02T20:54:14Z
dc.date.issued 2011-08
dc.identifier.citation Silberman, Dafne Magali; Mostoslavsky, Raul; SIRT3 deacetylase: the Jekyll and Hyde sirtuin; Embo Press; Embo Reports; 12; 8; 8-2011; 746-747
dc.identifier.issn 1469-221X
dc.identifier.uri http://hdl.handle.net/11336/17438
dc.description.abstract Post‐translational modifications have crucial roles in regulating the functions of many eukaryotic proteins. Among them, lysine acetylation has been traditionally studied in the context of nuclear histone modifications, and was one of the first to be described as part of the ‘histone code’ hypothesis (Kim et al, 2006). More recently, work from several groups has demonstrated that lysine acetylation also modulates the activity of several non‐histone proteins. In this context, this modification seems particularly abundant on mitochondrial proteins (Schwer et al, 2009). However, the way in which acetylation influences enzyme function and metabolic reprogramming in pathological states remains unknown. In an article published online this month in EMBO reports, Sack and colleagues shed new light on the role of mitochondrial SIRT3 deacetylase during paracetamol‐induced toxicity, describing the mitochondrial protein aldehyde dehydrogenase 2 (ALDH2) as a new target of SIRT3, and a protective role for protein acetylation in this context.
dc.format application/pdf
dc.language.iso eng
dc.publisher Embo Press
dc.rights info:eu-repo/semantics/restrictedAccess
dc.rights.uri https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject Sirtuin family
dc.subject.classification Bioquímica y Biología Molecular
dc.subject.classification Ciencias Biológicas
dc.subject.classification CIENCIAS NATURALES Y EXACTAS
dc.title SIRT3 deacetylase: the Jekyll and Hyde sirtuin
dc.type info:eu-repo/semantics/article
dc.type info:ar-repo/semantics/artículo
dc.type info:eu-repo/semantics/publishedVersion
dc.date.updated 2017-05-31T20:04:24Z
dc.journal.volume 12
dc.journal.number 8
dc.journal.pagination 746-747
dc.journal.pais Alemania
dc.journal.ciudad Heidelberg
dc.description.fil Fil: Silberman, Dafne Magali. Harvard Medical School; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Centro de Estudios Farmacológicos y Botánicos. Universidad de Buenos Aires. Facultad de Medicina. Centro de Estudios Farmacológicos y Botánicos; Argentina
dc.description.fil Fil: Mostoslavsky, Raul. Harvard Medical School; Estados Unidos
dc.journal.title Embo Reports
dc.relation.alternativeid info:eu-repo/semantics/altIdentifier/url/http://embor.embopress.org/content/12/8/746.long
dc.relation.alternativeid info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1038/embor.2011.147
dc.relation.alternativeid info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3147273/


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info:eu-repo/semantics/restrictedAccess Excepto donde se diga explícitamente, este item se publica bajo la siguiente descripción: Creative Commons Attribution-NonCommercial-ShareAlike 2.5 Unported (CC BY-NC-SA 2.5)