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Autordc.contributor.authorCurtis, Jessica M. 
Autordc.contributor.authorHahn, Wendy S. 
Autordc.contributor.authorStone, Matthew D. 
Autordc.contributor.authorInda, Jacob J. 
Autordc.contributor.authorDroullard, David J. 
Autordc.contributor.authorKuzmicic, Jovan P. 
Autordc.contributor.authorDonoghue, Margaret A. 
Autordc.contributor.authorLong, Eric K. 
Autordc.contributor.authorArmien, Anibal G. 
Autordc.contributor.authorLavandero González, Sergio 
Autordc.contributor.authorArriaga, Edgar 
Autordc.contributor.authorGriffin, Timothy J. 
Autordc.contributor.authorBernlohr, David A. 
Fecha ingresodc.date.accessioned2019-03-15T16:03:27Z
Fecha disponibledc.date.available2019-03-15T16:03:27Z
Fecha de publicacióndc.date.issued2012
Cita de ítemdc.identifier.citationJournal of Biological Chemistry, Volumen 287, Issue 39, 2018, Pages 32967-32980
Identificadordc.identifier.issn00219258
Identificadordc.identifier.issn1083351X
Identificadordc.identifier.other10.1074/jbc.M112.400663
Identificadordc.identifier.urihttps://repositorio.uchile.cl/handle/2250/165837
Resumendc.description.abstractCarbonylation is the covalent, non-reversible modification of the side chains of cysteine, histidine, and lysine residues by lipid peroxidation end products such as 4-hydroxy- and 4-oxononenal. In adipose tissue the effects of such modifications are associated with increased oxidative stress and metabolic dysregulation centered on mitochondrial energy metabolism. To address the role of protein carbonylation in the pathogenesis of mitochondrial dysfunction, quantitative proteomics was employed to identify specific targets of carbonylation in GSTA4-silenced or overexpressing 3T3-L1 adipocytes. GSTA4-silenced adipocytes displayed elevated carbonylation of several key mitochondrial proteins including the phosphate carrier protein, NADH dehydrogenase 1α subcomplexes 2 and 3, translocase of inner mitochondrial membrane 50, and valyl-tRNA synthetase. Elevated protein carbonylation is accompanied by diminished complex I activity, impaired respiration, increased superoxide production, and a red
Idiomadc.language.isoen
Tipo de licenciadc.rightsAttribution-NonCommercial-NoDerivs 3.0 Chile
Link a Licenciadc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/cl/
Fuentedc.sourceJournal of Biological Chemistry
Palabras clavesdc.subjectBiochemistry
Palabras clavesdc.subjectMolecular Biology
Palabras clavesdc.subjectCell Biology
Títulodc.titleProtein carbonylation and adipocyte mitochondrial function
Tipo de documentodc.typeArtículo de revista
dcterms.accessRightsdcterms.accessRightsAcceso Abierto
Catalogadoruchile.catalogadorSCOPUS
Indizaciónuchile.indexArtículo de publicación SCOPUS
uchile.cosechauchile.cosechaSI


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Excepto si se señala otra cosa, la licencia del ítem se describe como Attribution-NonCommercial-NoDerivs 3.0 Chile