Translational and posttranslational regulation of XIAP by eIF2α and ATF4 promotes ER stress–induced cell death during the unfolded protein response
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Title
Translational and posttranslational regulation of XIAP by eIF2α and ATF4 promotes ER stress–induced cell death during the unfolded protein response
Authors
Keywords
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Journal
MOLECULAR BIOLOGY OF THE CELL
Volume 25, Issue 9, Pages 1411-1420
Publisher
American Society for Cell Biology (ASCB)
Online
2014-03-13
DOI
10.1091/mbc.e13-11-0664
References
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Note: Only part of the references are listed.- ER-stress-induced transcriptional regulation increases protein synthesis leading to cell death
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- Phosphorylation of eIF2α at Serine 51 Is an Important Determinant of Cell Survival and Adaptation to Glucose Deficiency
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- Transnitrosylation of XIAP Regulates Caspase-Dependent Neuronal Cell Death
- (2010) Tomohiro Nakamura et al. MOLECULAR CELL
- Distinct 5′ UTRs regulate XIAP expression under normal growth conditions and during cellular stress
- (2010) Alura Riley et al. NUCLEIC ACIDS RESEARCH
- XIAP as a ubiquitin ligase in cellular signaling
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- Divergent Effects of PERK and IRE1 Signaling on Cell Viability
- (2009) Jonathan H. Lin et al. PLoS One
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- Regulation of apoptosis by XIAP ubiquitin-ligase activity
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- ATF4 is an oxidative stress–inducible, prodeath transcription factor in neurons in vitro and in vivo
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- Ablation of the UPR-Mediator CHOP Restores Motor Function and Reduces Demyelination in Charcot-Marie-Tooth 1B Mice
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- PERK-dependent regulation of IAP translation during ER stress
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