Targeting the unfolded protein response in disease
Author
dc.contributor.author
Hetz Flores, Claudio
Author
dc.contributor.author
Chevet, Eric
es_CL
Author
dc.contributor.author
Harding, Heather P.
es_CL
Admission date
dc.date.accessioned
2014-01-28T13:30:13Z
Available date
dc.date.available
2014-01-28T13:30:13Z
Publication date
dc.date.issued
2013
Cita de ítem
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NATURE REVIEWS, DRUG DISCOVERY VOLUME 12 | SEPTEMBER 2013
en_US
Identifier
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doi:10.1038/nrd3976
Identifier
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https://repositorio.uchile.cl/handle/2250/129191
General note
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Artículo de publicación ISI
en_US
Abstract
dc.description.abstract
Stress induced by the accumulation of unfolded proteins in the endoplasmic reticulum (ER) is a feature of specialized secretory cells and is also observed in many diseases, including cancer, diabetes, autoimmune conditions, liver disorders, obesity and neurodegenerative disorders. Cellular adaptation to ER stress is achieved by the activation
of the unfolded protein response, which is an integrated signal transduction pathway that modulates many aspects of ER physiology. When these mechanisms of adaptation are insufficient to handle the unfolded protein load, cells undergo apoptosis. Here, we discuss recent advances in the design of novel compounds and therapeutic strategies to manipulate levels of ER stress in disease.