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dc.contributor.authorPajares, Marta
dc.contributor.authorJiménez-Moreno, Natalia
dc.contributor.authorDias, Irundika H.K.
dc.contributor.authorDebelec, Bilge
dc.contributor.authorVucetic, Milica
dc.contributor.authorFladmark, Kari Espolin
dc.contributor.authorBasaga, Huveyda
dc.contributor.authorRibaric, Samo
dc.contributor.authorMilisav, Irina
dc.contributor.authorCuadrado, Antonio
dc.date.accessioned2016-03-02T14:22:36Z
dc.date.available2016-03-02T14:22:36Z
dc.date.issued2015-12
dc.identifier.citationRedox Biology 2015, 6:409-420eng
dc.identifier.urihttp://hdl.handle.net/1956/11421
dc.description.abstractIntracellular proteolysis is critical to maintain timely degradation of altered proteins including oxidized proteins. This review attempts to summarize the most relevant findings about oxidant protein modification, as well as the impact of reactive oxygen species on the proteolytic systems that regulate cell response to an oxidant environment: the ubiquitin-proteasome system (UPS), autophagy and the unfolded protein response (UPR). In the presence of an oxidant environment, these systems are critical to ensure proteostasis and cell survival. An example of altered degradation of oxidized proteins in pathology is provided for neurodegenerative diseases. Future work will determine if protein oxidation is a valid target to combat proteinopathies.eng
dc.language.isoengeng
dc.publisherElseviereng
dc.rightsAttribution CC BYeng
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/eng
dc.titleRedox control of protein degradationeng
dc.typeJournal articleeng
dc.date.updated2015-12-29T14:01:27Z
dc.rights.holderCopyright 2015 The Authorseng
dc.type.versionpublishedVersioneng
bora.peerreviewedPeer reviewedeng
dc.type.documentJournal article
dc.identifier.cristinID1281324
dc.identifier.doi10.1016/j.redox.2015.07.003eng
dc.source.issn2213-2317eng


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Attribution CC BY
Except where otherwise noted, this item's license is described as Attribution CC BY