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Authordc.contributor.authorHetz Flores, Claudio
Cita de ítemdc.identifier.citationAntioxidants and Redox Signaling, Volumen 9, Issue 12, 2018, Pages 2345-2355
Abstractdc.description.abstractProgrammed cell death is essential for the development and maintenance of cellular homeostasis, and its deregulation results in a variety of pathologic conditions. The BCL-2 family of proteins is a group of evolutionarily conserved regulators of cell death that operate at the mitochondrial membrane to control caspase activation. This family is comprised both of antiapoptotic and proapoptotic members, in which a subset of proapoptotic members, called BH3-only proteins, acts as upstream activators of the core proapoptotic pathway. In addition to their known role at the mitochondria, different BCL-2-related proteins are located to the endoplasmic reticulum (ER) membrane, where new functions have been recently proposed. In this review, evidence is presented indicating that members of the BCL-2 protein family are contained in multiprotein complexes at the ER, regulating diverse cellular processes including autophagy, calcium homeostasis, the unfolded-protein response, ER membrane remodeling
Type of licensedc.rightsAttribution-NonCommercial-NoDerivs 3.0 Chile
Link to Licensedc.rights.uri
Sourcedc.sourceAntioxidants and Redox Signaling
Keywordsdc.subjectMolecular Biology
Keywordsdc.subjectClinical Biochemistry
Keywordsdc.subjectCell Biology
Títulodc.titleER stress signaling and the BCL-2 family of proteins: From adaptation to irreversible cellular damage
Document typedc.typeArtículo de revista
Indexationuchile.indexArtículo de publicación SCOPUS

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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