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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.PublishedRedox Biology 2015, 6:409-420eng
dc.identifier.issn2213-2317en_US
dc.identifier.urihttps://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.en_US
dc.language.isoengeng
dc.publisherElsevieren_US
dc.rightsAttribution CC BYeng
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/eng
dc.titleRedox control of protein degradationen_US
dc.typePeer reviewed
dc.typeJournal article
dc.date.updated2015-12-29T14:01:27Z
dc.description.versionpublishedVersionen_US
dc.rights.holderCopyright 2015 The Authorsen_US
dc.identifier.doihttps://doi.org/10.1016/j.redox.2015.07.003
dc.identifier.cristin1281324


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