Please use this identifier to cite or link to this item: https://doi.org/10.1016/B978-0-12-396456-4.00005-5
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dc.titleTargeting phosphorylation of eukaryotic initiation factor-2α to treat human disease
dc.contributor.authorFullwood, M.J.
dc.contributor.authorZhou, W.
dc.contributor.authorShenolikar, S.
dc.date.accessioned2016-10-19T08:43:12Z
dc.date.available2016-10-19T08:43:12Z
dc.date.issued2012
dc.identifier.citationFullwood, M.J., Zhou, W., Shenolikar, S. (2012). Targeting phosphorylation of eukaryotic initiation factor-2α to treat human disease. Progress in Molecular Biology and Translational Science 106 : 75-106. ScholarBank@NUS Repository. https://doi.org/10.1016/B978-0-12-396456-4.00005-5
dc.identifier.issn18771173
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/128615
dc.description.abstractThe unfolded protein response, also known as endoplasmic reticulum (ER) stress, has been implicated in numerous human diseases, including atherosclerosis, cancer, diabetes, and neurodegenerative disorders. Protein misfolding activates one or more of the three ER transmembrane sensors to initiate a complex network of signaling that transiently suppresses protein translation while also enhancing protein folding and proteasomal degradation of misfolded proteins to ensure full recovery from ER stress. Gene disruption studies in mice have provided critical insights into the role of specific signaling components and pathways in the differing responses of animal tissues to ER stress. These studies have emphasized an important contribution of translational repression to sustained insulin synthesis and β-cell viability in experimental models of type-2 diabetes. This has focused attention on the recently discovered small-molecule inhibitors of eIF2α phosphatases that prolong eIF2α phosphorylation to reduce cell death in several animal models of human disease. These compounds show significant cytoprotection in cellular and animal models of neurodegenerative disorders, highlighting a potential strategy for future development of drugs to treat human protein misfolding disorders. © 2012 Elsevier Inc.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1016/B978-0-12-396456-4.00005-5
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentDUKE-NUS GRADUATE MEDICAL SCHOOL S'PORE
dc.description.doi10.1016/B978-0-12-396456-4.00005-5
dc.description.sourcetitleProgress in Molecular Biology and Translational Science
dc.description.volume106
dc.description.page75-106
dc.identifier.isiut000306935100005
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