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dc.contributor.authorGorman, Adrienne M.
dc.contributor.authorHealy, Sandra J.M.
dc.contributor.authorJäger, Richard
dc.contributor.authorSamali, Afshin
dc.date.accessioned2018-05-23T08:57:31Z
dc.date.available2018-05-23T08:57:31Z
dc.date.issued2012-02-17
dc.identifier.citationGorman, A. M., Healy, S. J. M., Jäger, R., & Samali, A. (2012). Stress management at the ER: Regulators of ER stress-induced apoptosis. Pharmacology & Therapeutics, 134(3), 306-316. doi: https://doi.org/10.1016/j.pharmthera.2012.02.003en_IE
dc.identifier.issn1879-016X
dc.identifier.urihttp://hdl.handle.net/10379/7371
dc.description.abstractThe endoplasmic reticulum (ER) is an elaborate cellular organelle essential for cell function and survival. Conditions that interfere with ER function lead to the accumulation and aggregation of unfolded proteins which are detected by ER transmembrane receptors that initiate the unfolded protein response (UPR) to restore normal ER function. If the ER stress is prolonged, or the adaptive response fails, apoptotic cell death ensues. Many studies have focused on how this failure initiates apoptosis, particularly because ER stress-induced apoptosis is implicated in the pathophysiology of several neurodegenerative and cardiovascular diseases. In this review we aim to shed light on the proteins that are not core components of the UPR signaling pathway but which can influence the course of the ER stress response by regulating the switch from the adaptive phase to apoptosis.en_IE
dc.description.sponsorshipOur research is supported by Science Foundation Ireland (09/RFP/BIC2371; 09/RFP/BMT2153), the Health Research Board (HRA/2009/59) and Breast Cancer Campaign (2008NovPhD21; 2010NovPR13).en_IE
dc.language.isoenen_IE
dc.publisherElsevieren_IE
dc.relation.ispartofPharmacology & therapeuticsen
dc.subjectEndoplasmic reticulum (ER) stressen_IE
dc.subjectUnfolded protein response (UPR)en_IE
dc.subjectApoptosisen_IE
dc.subjectBcl-2 familyen_IE
dc.titleStress management at the ER: regulators of ER stress-induced apoptosis.en_IE
dc.typeArticleen_IE
dc.date.updated2018-05-23T08:43:12Z
dc.identifier.doi10.1016/j.pharmthera.2012.02.003
dc.local.publishedsourcehttps://doi.org/10.1016/j.pharmthera.2012.02.003en_IE
dc.description.peer-reviewedpeer-reviewed
dc.contributor.funderScience Foundation Irelanden_IE
dc.contributor.funderHealth Research Boarden_IE
dc.contributor.funderBreast Cancer Campaignen_IE
dc.internal.rssid5737174
dc.local.contactAdrienne Gorman, Biochemistry, School Of Natural Science, Bioresearch Building, Nui. 2417 Email: adrienne.gorman@nuigalway.ie
dc.local.copyrightcheckedYes
dc.local.versionACCEPTED
dcterms.projectinfo:eu-repo/grantAgreement/SFI/SFI Research Frontiers Programme (RFP)/09/RFP/BIC2371/IE/Regulation of IRE1 signalling by BCL-2 during the unfolded protein response/
dcterms.projectinfo:eu-repo/grantAgreement/SFI/SFI Research Frontiers Programme (RFP)/09/RFP/BMT2153/IE/Novel neurotrophin variants with altered receptor binding/
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