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Authordc.contributor.authorCouve Correa, Andrés 
Authordc.contributor.authorHetz Flores, Claudio
Admission datedc.date.accessioned2019-03-18T11:52:08Z
Available datedc.date.available2019-03-18T11:52:08Z
Publication datedc.date.issued2014
Cita de ítemdc.identifier.citationEMBO Journal, Volumen 33, Issue 21, 2018, Pages 2444-2446
Identifierdc.identifier.issn14602075
Identifierdc.identifier.issn02614189
Identifierdc.identifier.other10.15252/embj.201489845
Identifierdc.identifier.urihttp://repositorio.uchile.cl/handle/2250/166456
Abstractdc.description.abstract© 2014 The Authors. The efficient folding of membrane and secreted proteins relies on the unfolded protein response (UPR) to buffer fluctuations in the load of misfolded proteins. Although the UPR is thought to operate on a generic manner to maintain ER proteostasis, a recent study revealed the existence of a novel mechanism to eliminate misfolded GPI-anchored proteins via the secretory pathway, termed 'rapid ER stress-induced export' (RESET) (Satpute-Krishnan et al,). RESET involves the export of misfolded GPI proteins to the plasma membrane for subsequent degradation by the lysosome.
Lenguagedc.language.isoen
Publisherdc.publisherWiley-VCH Verlag
Type of licensedc.rightsAttribution-NonCommercial-NoDerivs 3.0 Chile
Link to Licensedc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/cl/
Sourcedc.sourceEMBO Journal
Keywordsdc.subjectNeuroscience (all)
Keywordsdc.subjectMolecular Biology
Keywordsdc.subjectBiochemistry, Genetics and Molecular Biology (all)
Keywordsdc.subjectImmunology and Microbiology (all)
Títulodc.titleRESETing ER proteostasis: Selective stress pathway hidden in the secretory route
Document typedc.typeArtículo de revista
Catalogueruchile.catalogadorSCOPUS
Indexationuchile.indexArtículo de publicación SCOPUS
uchile.cosechauchile.cosechaSI


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Attribution-NonCommercial-NoDerivs 3.0 Chile
Except where otherwise noted, this item's license is described as Attribution-NonCommercial-NoDerivs 3.0 Chile