Regulation of translation initiation factor eIF2B at the hub of the integrated stress response
Author:
Affiliation:
1. Division Molecular and Cellular Function, School of Biological Sciences, Faculty of Biology, Medicine and Health Manchester Academic Health Science Centre, The University of Manchester Manchester UK
Funder
UK Biotechnology and Biological Sciences Research Council
Publisher
Wiley
Subject
Molecular Biology,Biochemistry
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1002/wrna.1491
Reference184 articles.
1. Pi Release from eIF2, Not GTP Hydrolysis, Is the Step Controlled by Start-Site Selection during Eukaryotic Translation Initiation
2. Direct Binding of Translation Initiation Factor eIF2γ-G Domain to Its GTPase-activating and GDP-GTP Exchange Factors eIF5 and eIF2Bϵ
3. Conserved bipartite motifs in yeast eIF5 and eIF2Bepsilon , GTPase-activating and GDP-GTP exchange factors in translation initiation, mediate binding to their common substrate eIF2
4. Characterization of a Novel PERK Kinase Inhibitor with Antitumor and Antiangiogenic Activity
5. Discovery of 7-Methyl-5-(1-{[3-(trifluoromethyl)phenyl]acetyl}-2,3-dihydro-1H-indol-5-yl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine (GSK2606414), a Potent and Selective First-in-Class Inhibitor of Protein Kinase R (PKR)-like Endoplasmic Reticulum Kinase (PERK)
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