{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T19:03:24Z","timestamp":1791227004835,"version":"4.1.0"},"reference-count":191,"publisher":"Elsevier BV","issue":"3","license":[{"start":{"date-parts":[[2012,5,1]],"date-time":"2012-05-01T00:00:00Z","timestamp":1335830400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2012,5,1]],"date-time":"2012-05-01T00:00:00Z","timestamp":1335830400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2022,1,27]],"date-time":"2022-01-27T00:00:00Z","timestamp":1643241600000},"content-version":"vor","delay-in-days":3558,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Advances in Nutrition"],"published-print":{"date-parts":[[2012,5]]},"DOI":"10.3945\/an.112.002113","type":"journal-article","created":{"date-parts":[[2012,7,25]],"date-time":"2012-07-25T05:51:47Z","timestamp":1343195507000},"page":"307-321","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":462,"title":["Eukaryotic Initiation Factor 2 Phosphorylation and Translational Control in Metabolism"],"prefix":"10.1016","volume":"3","author":[{"given":"Thomas D.","family":"Baird","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ronald C.","family":"Wek","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.3945\/an.112.002113_bib1","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1038\/nature10098","article-title":"Global quantification of mammalian gene expression control","volume":"473","author":"Schwanh\u00e4usser","year":"2011","journal-title":"Nature"},{"key":"10.3945\/an.112.002113_bib2","doi-asserted-by":"crossref","first-page":"1099","DOI":"10.1016\/S1097-2765(00)00108-8","article-title":"Regulated translation initiation controls stress-induced gene expression in mammalian cells","volume":"6","author":"Harding","year":"2000","journal-title":"Mol Cell"},{"key":"10.3945\/an.112.002113_bib3","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1038\/sj.emboj.7600030","article-title":"Cytoprotection by pre-emptive conditional phosphorylation of translation initiation factor 2","volume":"23","author":"Lu","year":"2004","journal-title":"EMBO J"},{"key":"10.3945\/an.112.002113_bib4","doi-asserted-by":"crossref","first-page":"11269","DOI":"10.1073\/pnas.0400541101","article-title":"Reinitiation involving upstream ORFs regulates ATF4 mRNA translation in mammalian cells","volume":"101","author":"Vattem","year":"2004","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.3945\/an.112.002113_bib5","doi-asserted-by":"crossref","first-page":"619","DOI":"10.1016\/S1097-2765(03)00105-9","article-title":"An integrated stress response regulates amino acid metabolism and resistance to oxidative stress","volume":"11","author":"Harding","year":"2003","journal-title":"Mol Cell"},{"key":"10.3945\/an.112.002113_bib6","doi-asserted-by":"crossref","first-page":"407","DOI":"10.1146\/annurev.micro.59.031805.133833","article-title":"Translational regulation of GCN4 and the general amino acid control of yeast","volume":"59","author":"Hinnebusch","year":"2005","journal-title":"Annu Rev Microbiol"},{"key":"10.3945\/an.112.002113_bib7","doi-asserted-by":"crossref","first-page":"434","DOI":"10.1128\/MMBR.00008-11","article-title":"Molecular mechanism of scanning and start codon selection in eukaryotes","volume":"75","author":"Hinnebusch","year":"2011","journal-title":"Microbiol Mol Biol Rev"},{"key":"10.3945\/an.112.002113_bib8","doi-asserted-by":"crossref","first-page":"328","DOI":"10.1152\/physiolgenomics.90396.2008","article-title":"eIF2alpha kinases GCN2 and PERK modulate transcription and translation of distinct sets of mRNAs in mouse liver","volume":"38","author":"Dang Do","year":"2009","journal-title":"Physiol Genomics"},{"key":"10.3945\/an.112.002113_bib9","doi-asserted-by":"crossref","first-page":"19198","DOI":"10.1074\/jbc.M201052200","article-title":"Regulation of internal ribosomal entry site-mediated translation by phosphorylation of the translation initiation factor eIF2alpha","volume":"277","author":"Fernandez","year":"2002","journal-title":"J Biol Chem"},{"key":"10.3945\/an.112.002113_bib10","doi-asserted-by":"crossref","first-page":"10939","DOI":"10.1074\/jbc.M110.216093","article-title":"Phosphorylation of eIF2 facilitates ribosomal bypass of an inhibitory upstream ORF to enhance CHOP translation","volume":"286","author":"Palam","year":"2011","journal-title":"J Biol Chem"},{"key":"10.3945\/an.112.002113_bib11","doi-asserted-by":"crossref","first-page":"1207","DOI":"10.1101\/gad.516509","article-title":"Translational reprogramming following UVB irradiation is mediated by DNA-PKcs and allows selective recruitment to the polysomes of mRNAs encoding DNA repair enzymes","volume":"23","author":"Powley","year":"2009","journal-title":"Genes Dev"},{"key":"10.3945\/an.112.002113_bib12","doi-asserted-by":"crossref","first-page":"33165","DOI":"10.1074\/jbc.M110.167213","article-title":"Both transcriptional regulation and translational control of ATF4 are central to the integrated stress response","volume":"285","author":"Dey","year":"2010","journal-title":"J Biol Chem"},{"key":"10.3945\/an.112.002113_bib13","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1038\/nrm2838","article-title":"The mechanism of eukaryotic translation initiation and principles of its regulation","volume":"11","author":"Jackson","year":"2010","journal-title":"Nat Rev Mol Cell Biol"},{"key":"10.3945\/an.112.002113_bib14","doi-asserted-by":"crossref","first-page":"731","DOI":"10.1016\/j.cell.2009.01.042","article-title":"Regulation of translation initiation in eukaryotes: mechanisms and biological targets","volume":"136","author":"Sonenberg","year":"2009","journal-title":"Cell"},{"key":"10.3945\/an.112.002113_bib15","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1016\/j.molcel.2005.09.008","article-title":"Pi release from eIF2, not GTP hydrolysis, is the step controlled by start-site selection during eukaryotic translation initiation","volume":"20","author":"Algire","year":"2005","journal-title":"Mol Cell"},{"key":"10.3945\/an.112.002113_bib16","doi-asserted-by":"crossref","first-page":"514","DOI":"10.1101\/gad.12.4.514","article-title":"eIF2 independently binds two distinct eIF2B subcomplexes that catalyze and regulate guanine-nucleotide exchange","volume":"12","author":"Pavitt","year":"1998","journal-title":"Genes Dev"},{"key":"10.3945\/an.112.002113_bib17","doi-asserted-by":"crossref","first-page":"5292","DOI":"10.1093\/emboj\/cdf515","article-title":"Characterization of the minimal catalytic domain within eIF2B: the guanine-nucleotide exchange factor for translation initiation","volume":"21","author":"Gomez","year":"2002","journal-title":"EMBO J"},{"key":"10.3945\/an.112.002113_bib18","doi-asserted-by":"crossref","first-page":"5018","DOI":"10.1128\/MCB.21.15.5018-5030.2001","article-title":"Tight binding of the phosphorylated alpha subunit of initiation factor 2 (eIF2alpha) to the regulatory subunits of guanine nucleotide exchange factor eIF2B is required for inhibition of translation initiation","volume":"21","author":"Krishnamoorthy","year":"2001","journal-title":"Mol Cell Biol"},{"key":"10.3945\/an.112.002113_bib19","doi-asserted-by":"crossref","first-page":"12841","DOI":"10.1074\/jbc.273.21.12841","article-title":"Regulation of guanine nucleotide exchange through phosphorylation of eukaryotic initiation factor eIF2alpha. Role of the alpha- and delta-subunits of eIF2b","volume":"273","author":"Kimball","year":"1998","journal-title":"J Biol Chem"},{"key":"10.3945\/an.112.002113_bib20","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1038\/nrm3025","article-title":"mTOR: from growth signal integration to cancer, diabetes and ageing","volume":"12","author":"Zoncu","year":"2011","journal-title":"Nat Rev Mol Cell Biol"},{"key":"10.3945\/an.112.002113_bib21","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1038\/nrm2672","article-title":"Molecular mechanisms of mTOR-mediated translational control","volume":"10","author":"Ma","year":"2009","journal-title":"Nat Rev Mol Cell Biol"},{"key":"10.3945\/an.112.002113_bib22","doi-asserted-by":"crossref","first-page":"6416","DOI":"10.1038\/sj.onc.1209888","article-title":"mTOR, translation initiation and cancer","volume":"25","author":"Mamane","year":"2006","journal-title":"Oncogene"},{"key":"10.3945\/an.112.002113_bib23","doi-asserted-by":"crossref","first-page":"4106","DOI":"10.4161\/cc.9.20.13630","article-title":"eIF4B controls survival and proliferation and is regulated by proto-oncogenic signaling pathways","volume":"9","author":"Shahbazian","year":"2010","journal-title":"Cell Cycle"},{"key":"10.3945\/an.112.002113_bib24","doi-asserted-by":"crossref","first-page":"2781","DOI":"10.1038\/sj.emboj.7601166","article-title":"The mTOR\/PI3K and MAPK pathways converge on eIF4B to control its phosphorylation and activity","volume":"25","author":"Shahbazian","year":"2006","journal-title":"EMBO J"},{"key":"10.3945\/an.112.002113_bib25","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1042\/BST0340007","article-title":"Coping with stress: eIF2 kinases and translational control","volume":"34","author":"Wek","year":"2006","journal-title":"Biochem Soc Trans"},{"key":"10.3945\/an.112.002113_bib26","doi-asserted-by":"crossref","first-page":"1081","DOI":"10.1126\/science.1209038","article-title":"The unfolded protein response: from stress pathway to homeostatic regulation","volume":"334","author":"Walter","year":"2011","journal-title":"Science"},{"key":"10.3945\/an.112.002113_bib27","doi-asserted-by":"crossref","first-page":"739","DOI":"10.1146\/annurev.biochem.73.011303.074134","article-title":"The mammalian unfolded protein response","volume":"74","author":"Schr\u00f6der","year":"2005","journal-title":"Annu Rev Biochem"},{"key":"10.3945\/an.112.002113_bib28","doi-asserted-by":"crossref","first-page":"6909","DOI":"10.1093\/emboj\/20.23.6909","article-title":"Heme-regulated eIF2alpha kinase (HRI) is required for translational regulation and survival of erythroid precursors in iron deficiency","volume":"20","author":"Han","year":"2001","journal-title":"EMBO J"},{"key":"10.3945\/an.112.002113_bib29","doi-asserted-by":"crossref","first-page":"2693","DOI":"10.1182\/blood-2006-08-041830","article-title":"Regulation of protein synthesis by the heme-regulated eIF2alpha kinase: relevance to anemias","volume":"109","author":"Chen","year":"2007","journal-title":"Blood"},{"key":"10.3945\/an.112.002113_bib30","doi-asserted-by":"crossref","first-page":"901","DOI":"10.1016\/j.cell.2005.06.041","article-title":"Mechanistic link between PKR dimerization, autophosphorylation, and eIF2alpha substrate recognition","volume":"122","author":"Dey","year":"2005","journal-title":"Cell"},{"key":"10.3945\/an.112.002113_bib31","doi-asserted-by":"crossref","first-page":"799","DOI":"10.1016\/j.biochi.2007.03.001","article-title":"The dsRNA protein kinase PKR: virus and cell control","volume":"89","author":"Garc\u00eda","year":"2007","journal-title":"Biochimie"},{"key":"10.3945\/an.112.002113_bib32","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1038\/nsmb.1529","article-title":"Rapid evolution of protein kinase PKR alters sensitivity to viral inhibitors","volume":"16","author":"Rothenburg","year":"2009","journal-title":"Nat Struct Mol Biol"},{"key":"10.3945\/an.112.002113_bib33","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1089\/jir.2010.0099","article-title":"The role of protein kinase R in the interferon response","volume":"31","author":"Pindel","year":"2011","journal-title":"J Interferon Cytokine Res"},{"key":"10.3945\/an.112.002113_bib34","doi-asserted-by":"crossref","first-page":"4497","DOI":"10.1128\/MCB.15.8.4497","article-title":"The histidyl-tRNA synthetase-related sequence in the eIF-2 alpha protein kinase GCN2 interacts with tRNA and is required for activation in response to starvation for different amino acids","volume":"15","author":"Wek","year":"1995","journal-title":"Mol Cell Biol"},{"key":"10.3945\/an.112.002113_bib35","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1016\/S1097-2765(00)00028-9","article-title":"Uncharged tRNA activates GCN2 by displacing the protein kinase moiety from a bipartite tRNA-binding domain","volume":"6","author":"Dong","year":"2000","journal-title":"Mol Cell"},{"key":"10.3945\/an.112.002113_bib36","doi-asserted-by":"crossref","first-page":"4579","DOI":"10.1073\/pnas.86.12.4579","article-title":"Juxtaposition of domains homologous to protein kinases and histidyl-tRNA synthetases in GCN2 protein suggests a mechanism for coupling GCN4 expression to amino acid availability","volume":"86","author":"Wek","year":"1989","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.3945\/an.112.002113_bib37","doi-asserted-by":"crossref","first-page":"1592","DOI":"10.1128\/MCB.01446-08","article-title":"A network of hydrophobic residues impeding helix alphaC rotation maintains latency of kinase Gcn2, which phosphorylates the alpha subunit of translation initiation factor 2","volume":"29","author":"G\u00e1rriz","year":"2009","journal-title":"Mol Cell Biol"},{"key":"10.3945\/an.112.002113_bib38","doi-asserted-by":"crossref","first-page":"29289","DOI":"10.1074\/jbc.M504096200","article-title":"Structural basis for autoinhibition and mutational activation of eukaryotic initiation factor 2alpha protein kinase GCN2","volume":"280","author":"Padyana","year":"2005","journal-title":"J Biol Chem"},{"key":"10.3945\/an.112.002113_bib39","doi-asserted-by":"crossref","first-page":"1271","DOI":"10.1101\/gad.979402","article-title":"Mutations that bypass tRNA binding activate the intrinsically defective kinase domain in GCN2","volume":"16","author":"Qiu","year":"2002","journal-title":"Genes Dev"},{"key":"10.3945\/an.112.002113_bib40","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1007\/s00726-008-0199-2","article-title":"Specificity of amino acid regulated gene expression: analysis of genes subjected to either complete or single amino acid deprivation","volume":"37","author":"Palii","year":"2009","journal-title":"Amino Acids"},{"key":"10.3945\/an.112.002113_bib41","doi-asserted-by":"crossref","first-page":"31222","DOI":"10.1074\/jbc.M604511200","article-title":"Role of glutamine depletion in directing tissue-specific nutrient stress responses to L-asparaginase","volume":"281","author":"Reinert","year":"2006","journal-title":"J Biol Chem"},{"key":"10.3945\/an.112.002113_bib42","doi-asserted-by":"crossref","first-page":"36553","DOI":"10.1074\/jbc.M404559200","article-title":"Preservation of liver protein synthesis during dietary leucine deprivation occurs at the expense of skeletal muscle mass in mice deleted for eIF2 kinase GCN2","volume":"279","author":"Anthony","year":"2004","journal-title":"J Biol Chem"},{"key":"10.3945\/an.112.002113_bib43","doi-asserted-by":"crossref","first-page":"32742","DOI":"10.1074\/jbc.M109.047910","article-title":"GCN2 protein kinase is required to activate amino acid deprivation responses in mice treated with the anti-cancer agent L-asparaginase","volume":"284","author":"Bunpo","year":"2009","journal-title":"J Biol Chem"},{"key":"10.3945\/an.112.002113_bib44","doi-asserted-by":"crossref","unstructured":"Habibi D, Ogloff N, Jalili RB, Yost A, Weng AP, Ghahary A, Ong CJ, Borrelidin, a small molecule nitrile-containing macrolide inhibitor of threonyl-tRNA synthetase, is a potent inducer of apoptosis in acute lymphoblastic leukemia. Invest New Drugs. Epub 2011 Jun 17.","DOI":"10.1007\/s10637-011-9700-y"},{"key":"10.3945\/an.112.002113_bib45","doi-asserted-by":"crossref","first-page":"1153","DOI":"10.1016\/j.chembiol.2006.09.006","article-title":"Brasilicardin A, a natural immunosuppressant, targets amino acid transport system L","volume":"13","author":"Usui","year":"2006","journal-title":"Chem Biol"},{"key":"10.3945\/an.112.002113_bib46","doi-asserted-by":"crossref","first-page":"26638","DOI":"10.1074\/jbc.M111.241323","article-title":"Impaired nutrient signaling and body weight control in a Na+ neutral amino acid cotransporter (Slc6a19)-deficient mouse","volume":"286","author":"Br\u00f6er","year":"2011","journal-title":"J Biol Chem"},{"key":"10.3945\/an.112.002113_bib47","doi-asserted-by":"crossref","first-page":"8866","DOI":"10.1074\/jbc.M110.216119","article-title":"Arginine deficiency causes runting in the suckling period by selectively activating the stress kinase GCN2","volume":"286","author":"Marion","year":"2011","journal-title":"J Biol Chem"},{"key":"10.3945\/an.112.002113_bib48","doi-asserted-by":"crossref","first-page":"647","DOI":"10.1016\/0092-8674(92)90433-D","article-title":"Autoregulation of the yeast lysyl-tRNA synthetase gene GCD5\/KRS1 by translational and transcriptional control mechanisms","volume":"70","author":"Lanker","year":"1992","journal-title":"Cell"},{"key":"10.3945\/an.112.002113_bib49","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1016\/j.cmet.2007.01.001","article-title":"The GCN2 eIF2alpha kinase regulates fatty-acid homeostasis in the liver during deprivation of an essential amino acid","volume":"5","author":"Guo","year":"2007","journal-title":"Cell Metab"},{"key":"10.3945\/an.112.002113_bib50","doi-asserted-by":"crossref","first-page":"1279","DOI":"10.1016\/S0960-9822(02)01037-0","article-title":"Activation of GCN2 in UV-irradiated cells inhibits translation","volume":"12","author":"Deng","year":"2002","journal-title":"Curr Biol"},{"key":"10.3945\/an.112.002113_bib51","doi-asserted-by":"crossref","first-page":"371","DOI":"10.1042\/BJ20041164","article-title":"GCN2 phosphorylation of eIF2alpha activates NF-kappaB in response to UV irradiation","volume":"385","author":"Jiang","year":"2005","journal-title":"Biochem J"},{"key":"10.3945\/an.112.002113_bib52","doi-asserted-by":"crossref","first-page":"14189","DOI":"10.1074\/jbc.M413660200","article-title":"Phosphorylation of the alpha-subunit of the eukaryotic initiation factor-2 (eIF2alpha) reduces protein synthesis and enhances apoptosis in response to proteasome inhibition","volume":"280","author":"Jiang","year":"2005","journal-title":"J Biol Chem"},{"key":"10.3945\/an.112.002113_bib53","doi-asserted-by":"crossref","first-page":"669","DOI":"10.18632\/aging.100216","article-title":"HDAC pharmacological inhibition promotes cell death through the eIF2alpha kinases PKR and GCN2","volume":"2","author":"Peidis","year":"2010","journal-title":"Aging"},{"key":"10.3945\/an.112.002113_bib54","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0001887","article-title":"Different effect of proteasome inhibition on vesicular stomatitis virus and poliovirus replication","volume":"3","author":"Neznanov","year":"2008","journal-title":"PLoS One"},{"key":"10.3945\/an.112.002113_bib55","doi-asserted-by":"crossref","first-page":"2706","DOI":"10.1128\/MCB.20.8.2706-2717.2000","article-title":"Glucose limitation induces GCN4 translation by activation of Gcn2 protein kinase","volume":"20","author":"Yang","year":"2000","journal-title":"Mol Cell Biol"},{"key":"10.3945\/an.112.002113_bib56","doi-asserted-by":"crossref","first-page":"2082","DOI":"10.1038\/emboj.2010.81","article-title":"The GCN2\u2013ATF4 pathway is critical for tumour cell survival and proliferation in response to nutrient deprivation","volume":"29","author":"Ye","year":"2010","journal-title":"EMBO J"},{"key":"10.3945\/an.112.002113_bib57","doi-asserted-by":"crossref","first-page":"F1202","DOI":"10.1152\/ajprenal.00272.2011","article-title":"Phosphorylation of eIF2alpha via the general control kinase, GCN2, modulates the ability of renal medullary cells to survive high urea stress","volume":"301","author":"Cai","year":"2011","journal-title":"Am J Physiol Renal Physiol"},{"key":"10.3945\/an.112.002113_bib58","doi-asserted-by":"crossref","first-page":"24989","DOI":"10.1074\/jbc.271.40.24989","article-title":"Histidyl-tRNA synthetase-related sequences in GCN2 protein kinase regulate in vitro phosphorylation of eIF-2","volume":"271","author":"Zhu","year":"1996","journal-title":"J Biol Chem"},{"key":"10.3945\/an.112.002113_bib59","doi-asserted-by":"crossref","first-page":"22820","DOI":"10.1074\/jbc.M402228200","article-title":"Dimerization is required for activation of eIF2 kinase Gcn2 in response to diverse environmental stress conditions","volume":"279","author":"Narasimhan","year":"2004","journal-title":"J Biol Chem"},{"key":"10.3945\/an.112.002113_bib60","doi-asserted-by":"crossref","first-page":"25254","DOI":"10.1074\/jbc.M109.000877","article-title":"Genome-wide analysis of tRNA charging and activation of the eIF2 kinase Gcn2p","volume":"284","author":"Zaborske","year":"2009","journal-title":"J Biol Chem"},{"key":"10.3945\/an.112.002113_bib61","doi-asserted-by":"crossref","first-page":"1887","DOI":"10.1093\/emboj\/19.8.1887","article-title":"Association of GCN1\u2013GCN20 regulatory complex with the N-terminus of eIF2alpha kinase GCN2 is required for GCN2 activation","volume":"19","author":"Garcia-Barrio","year":"2000","journal-title":"EMBO J"},{"key":"10.3945\/an.112.002113_bib62","doi-asserted-by":"crossref","first-page":"17591","DOI":"10.1074\/jbc.M011793200","article-title":"Budding yeast GCN1 binds the GI domain to activate the eIF2alpha kinase GCN2","volume":"276","author":"Kubota","year":"2001","journal-title":"J Biol Chem"},{"key":"10.3945\/an.112.002113_bib63","doi-asserted-by":"crossref","first-page":"20243","DOI":"10.1074\/jbc.C000262200","article-title":"GI domain-mediated association of the eukaryotic initiation factor 2alpha kinase GCN2 with its activator GCN1 is required for general amino acid control in budding yeast","volume":"275","author":"Kubota","year":"2000","journal-title":"J Biol Chem"},{"key":"10.3945\/an.112.002113_bib64","first-page":"3541","article-title":"GCN1, a translational activator of GCN4 in Saccharomyces cerevisiae, is required for phosphorylation of eukaryotic translation initiation factor 2 by protein kinase GCN2","volume":"13","author":"Marton","year":"1993","journal-title":"Mol Cell Biol"},{"key":"10.3945\/an.112.002113_bib65","doi-asserted-by":"crossref","first-page":"4474","DOI":"10.1128\/MCB.17.8.4474","article-title":"Evidence that GCN1 and GCN20, translational regulators of GCN4, function on elongating ribosomes in activation of eIF2alpha kinase GCN2","volume":"17","author":"Marton","year":"1997","journal-title":"Mol Cell Biol"},{"key":"10.3945\/an.112.002113_bib66","doi-asserted-by":"crossref","first-page":"6622","DOI":"10.1093\/emboj\/19.23.6622","article-title":"Separate domains in GCN1 for binding protein kinase GCN2 and ribosomes are required for GCN2 activation in amino acid-starved cells","volume":"19","author":"Sattlegger","year":"2000","journal-title":"EMBO J"},{"key":"10.3945\/an.112.002113_bib67","doi-asserted-by":"crossref","first-page":"1811","DOI":"10.1002\/cne.21652","article-title":"Distribution of the protein IMPACT, an inhibitor of GCN2, in the mouse, rat, and marmoset brain","volume":"507","author":"Bittencourt","year":"2008","journal-title":"J Comp Neurol"},{"key":"10.3945\/an.112.002113_bib68","doi-asserted-by":"crossref","first-page":"28316","DOI":"10.1074\/jbc.M408571200","article-title":"IMPACT, a protein preferentially expressed in the mouse brain, binds GCN1 and inhibits GCN2 activation","volume":"280","author":"Pereira","year":"2005","journal-title":"J Biol Chem"},{"key":"10.3945\/an.112.002113_bib69","doi-asserted-by":"crossref","first-page":"29952","DOI":"10.1074\/jbc.M404009200","article-title":"YIH1 is an actin-binding protein that inhibits protein kinase GCN2 and impairs general amino acid control when overexpressed","volume":"279","author":"Sattlegger","year":"2004","journal-title":"J Biol Chem"},{"key":"10.3945\/an.112.002113_bib70","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1038\/16729","article-title":"Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase","volume":"397","author":"Harding","year":"1999","journal-title":"Nature"},{"key":"10.3945\/an.112.002113_bib71","doi-asserted-by":"crossref","first-page":"7499","DOI":"10.1128\/MCB.18.12.7499","article-title":"Identification and characterization of pancreatic eukaryotic initiation factor 2 alpha-subunit kinase, PEK, involved in translational control","volume":"18","author":"Shi","year":"1998","journal-title":"Mol Cell Biol"},{"key":"10.3945\/an.112.002113_bib72","doi-asserted-by":"crossref","first-page":"18728","DOI":"10.1074\/jbc.M200903200","article-title":"Dimerization and release of molecular chaperone inhibition facilitate activation of eukaryotic initiation factor-2 kinase in response to endoplasmic reticulum stress","volume":"277","author":"Ma","year":"2002","journal-title":"J Biol Chem"},{"key":"10.3945\/an.112.002113_bib73","doi-asserted-by":"crossref","first-page":"326","DOI":"10.1038\/35014014","article-title":"Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response","volume":"2","author":"Bertolotti","year":"2000","journal-title":"Nat Cell Biol"},{"key":"10.3945\/an.112.002113_bib74","doi-asserted-by":"crossref","first-page":"795","DOI":"10.1016\/j.jhep.2010.11.005","article-title":"Endoplasmic reticulum stress in liver disease","volume":"54","author":"Malhi","year":"2011","journal-title":"J Hepatol"},{"key":"10.3945\/an.112.002113_bib75","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1210\/er.2007-0039","article-title":"The unfolded protein response: a pathway that links insulin demand with beta-cell failure and diabetes","volume":"29","author":"Scheuner","year":"2008","journal-title":"Endocr Rev"},{"key":"10.3945\/an.112.002113_bib76","doi-asserted-by":"crossref","first-page":"900","DOI":"10.1016\/j.cell.2010.02.034","article-title":"Endoplasmic reticulum stress and the inflammatory basis of metabolic disease","volume":"140","author":"Hotamisligil","year":"2010","journal-title":"Cell"},{"key":"10.3945\/an.112.002113_bib77","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1097\/MED.0b013e3283372843","article-title":"The binary switch between life and death of endoplasmic reticulum-stressed beta cells","volume":"17","author":"Oslowski","year":"2010","journal-title":"Curr Opin Endocrinol Diabetes Obes"},{"key":"10.3945\/an.112.002113_bib78","doi-asserted-by":"crossref","first-page":"1133","DOI":"10.1152\/physrev.00015.2006","article-title":"Endoplasmic reticulum stress signaling in disease","volume":"86","author":"Marciniak","year":"2006","journal-title":"Physiol Rev"},{"key":"10.3945\/an.112.002113_bib79","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1186\/1750-1172-5-29","article-title":"Wolcott-Rallison syndrome","volume":"5","author":"Julier","year":"2010","journal-title":"Orphanet J Rare Dis"},{"key":"10.3945\/an.112.002113_bib80","doi-asserted-by":"crossref","first-page":"292","DOI":"10.1016\/S0022-3476(72)80596-1","article-title":"Infancy-onset diabetes mellitus and multiple epiphyseal dysplasia","volume":"80","author":"Wolcott","year":"1972","journal-title":"J Pediatr"},{"key":"10.3945\/an.112.002113_bib81","doi-asserted-by":"crossref","first-page":"406","DOI":"10.1038\/78085","article-title":"EIF2AK3, encoding translation initiation factor 2-alpha kinase 3, is mutated in patients with Wolcott-Rallison syndrome","volume":"25","author":"Del\u00e9pine","year":"2000","journal-title":"Nat Genet"},{"key":"10.3945\/an.112.002113_bib82","doi-asserted-by":"crossref","first-page":"1876","DOI":"10.2337\/diabetes.53.7.1876","article-title":"Wolcott-Rallison Syndrome: clinical, genetic, and functional study of EIF2AK3 mutations and suggestion of genetic heterogeneity","volume":"53","author":"Sen\u00e9e","year":"2004","journal-title":"Diabetes"},{"key":"10.3945\/an.112.002113_bib83","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1038\/nrm2199","article-title":"Signal integration in the endoplasmic reticulum unfolded protein response","volume":"8","author":"Ron","year":"2007","journal-title":"Nat Rev Mol Cell Biol"},{"key":"10.3945\/an.112.002113_bib84","doi-asserted-by":"crossref","first-page":"18773","DOI":"10.1073\/pnas.0509487102","article-title":"On the mechanism of sensing unfolded protein in the endoplasmic reticulum","volume":"102","author":"Credle","year":"2005","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.3945\/an.112.002113_bib85","doi-asserted-by":"crossref","first-page":"1891","DOI":"10.1126\/science.1209126","article-title":"Unfolded proteins are Ire1-activating ligands that directly induce the unfolded protein response","volume":"333","author":"Gardner","year":"2011","journal-title":"Science"},{"key":"10.3945\/an.112.002113_bib86","doi-asserted-by":"crossref","first-page":"16113","DOI":"10.1073\/pnas.1010580107","article-title":"Mammalian endoplasmic reticulum stress sensor IRE1 signals by dynamic clustering","volume":"107","author":"Li","year":"2010","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.3945\/an.112.002113_bib87","doi-asserted-by":"crossref","first-page":"687","DOI":"10.1038\/nature07661","article-title":"The unfolded protein response signals through high-order assembly of Ire1","volume":"457","author":"Korennykh","year":"2009","journal-title":"Nature"},{"key":"10.3945\/an.112.002113_bib88","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pgen.1002137","article-title":"Translation reinitiation relies on the interaction between eIF3a\/TIF32 and progressively folded cis-acting mRNA elements preceding short uORFs","volume":"7","author":"Munzarov\u00e1","year":"2011","journal-title":"PLoS Genet"},{"key":"10.3945\/an.112.002113_bib89","doi-asserted-by":"crossref","first-page":"2414","DOI":"10.1101\/gad.480508","article-title":"eIF3a cooperates with sequences 5\u2032 of uORF1 to promote resumption of scanning by post-termination ribosomes for reinitiation on GCN4 mRNA","volume":"22","author":"Szamecz","year":"2008","journal-title":"Genes Dev"},{"key":"10.3945\/an.112.002113_bib90","doi-asserted-by":"crossref","first-page":"436","DOI":"10.1016\/j.tem.2009.05.008","article-title":"ATF4-dependent transcription mediates signaling of amino acid limitation","volume":"20","author":"Kilberg","year":"2009","journal-title":"Trends Endocrinol Metab"},{"key":"10.3945\/an.112.002113_bib91","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1042\/bj3390135","article-title":"Complexes containing activating transcription factor (ATF)\/cAMP-responsive-element-binding protein (CREB) interact with the CCAAT\/enhancer-binding protein (C\/EBP)-ATF composite site to regulate Gadd153 expression during the stress response","volume":"339","author":"Fawcett","year":"1999","journal-title":"Biochem J"},{"key":"10.3945\/an.112.002113_bib92","doi-asserted-by":"crossref","first-page":"4390","DOI":"10.1091\/mbc.e11-06-0510","article-title":"The eIF2 kinase PERK and the integrated stress response facilitate activation of ATF6 during endoplasmic reticulum stress","volume":"22","author":"Teske","year":"2011","journal-title":"Mol Biol Cell"},{"key":"10.3945\/an.112.002113_bib93","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1172\/JCI40027","article-title":"The unfolded protein response protects human tumor cells during hypoxia through regulation of the autophagy genes MAP1LC3B and ATG5","volume":"120","author":"Rouschop","year":"2010","journal-title":"J Clin Invest"},{"key":"10.3945\/an.112.002113_bib94","doi-asserted-by":"crossref","first-page":"4424","DOI":"10.1038\/onc.2010.191","article-title":"Regulation of autophagy by ATF4 in response to severe hypoxia","volume":"29","author":"Rzymski","year":"2010","journal-title":"Oncogene"},{"key":"10.3945\/an.112.002113_bib95","doi-asserted-by":"crossref","first-page":"1365","DOI":"10.1128\/MCB.24.3.1365-1377.2004","article-title":"Activating transcription factor 3 is integral to the eukaryotic initiation factor 2 kinase stress response","volume":"24","author":"Jiang","year":"2004","journal-title":"Mol Cell Biol"},{"key":"10.3945\/an.112.002113_bib96","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1146\/annurev.nutr.24.012003.132145","article-title":"Nutritional control of gene expression: how mammalian cells respond to amino acid limitation","volume":"25","author":"Kilberg","year":"2005","journal-title":"Annu Rev Nutr"},{"key":"10.3945\/an.112.002113_bib97","doi-asserted-by":"crossref","first-page":"50829","DOI":"10.1074\/jbc.M409173200","volume":"279","author":"Chen","year":"2004","journal-title":"J Biol Chem"},{"key":"10.3945\/an.112.002113_bib98","doi-asserted-by":"crossref","first-page":"3066","DOI":"10.1101\/gad.1250704","article-title":"CHOP induces death by promoting protein synthesis and oxidation in the stressed endoplasmic reticulum","volume":"18","author":"Marciniak","year":"2004","journal-title":"Genes Dev"},{"key":"10.3945\/an.112.002113_bib99","doi-asserted-by":"crossref","first-page":"1573","DOI":"10.1096\/fj.02-1184fje","article-title":"The function of GADD34 is a recovery from a shutoff of protein synthesis induced by ER stress: elucidation by GADD34-deficient mice","volume":"17","author":"Kojima","year":"2003","journal-title":"FASEB J"},{"key":"10.3945\/an.112.002113_bib100","doi-asserted-by":"crossref","first-page":"1011","DOI":"10.1083\/jcb.153.5.1011","article-title":"Feedback inhibition of the unfolded protein response by GADD34-mediated dephosphorylation of eIF2alpha","volume":"153","author":"Novoa","year":"2001","journal-title":"J Cell Biol"},{"key":"10.3945\/an.112.002113_bib101","doi-asserted-by":"crossref","first-page":"1180","DOI":"10.1093\/emboj\/cdg112","article-title":"Stress-induced gene expression requires programmed recovery from translational repression","volume":"22","author":"Novoa","year":"2003","journal-title":"EMBO J"},{"key":"10.3945\/an.112.002113_bib102","doi-asserted-by":"crossref","first-page":"1292","DOI":"10.1128\/MCB.23.4.1292-1303.2003","article-title":"Growth arrest and DNA damage-inducible protein GADD34 targets protein phosphatase 1 alpha to the endoplasmic reticulum and promotes dephosphorylation of the alpha subunit of eukaryotic translation initiation factor 2","volume":"23","author":"Brush","year":"2003","journal-title":"Mol Cell Biol"},{"key":"10.3945\/an.112.002113_bib103","doi-asserted-by":"crossref","first-page":"34864","DOI":"10.1074\/jbc.M301107200","article-title":"Delineation of a negative feedback regulatory loop that controls protein translation during endoplasmic reticulum stress","volume":"278","author":"Ma","year":"2003","journal-title":"J Biol Chem"},{"key":"10.3945\/an.112.002113_bib104","doi-asserted-by":"crossref","first-page":"736","DOI":"10.1182\/blood.V99.3.736","article-title":"Targeted disruption of the activating transcription factor 4 gene results in severe fetal anemia in mice","volume":"99","author":"Masuoka","year":"2002","journal-title":"Blood"},{"key":"10.3945\/an.112.002113_bib105","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1006\/dbio.2000.9699","article-title":"Microphthalmia due to p53-mediated apoptosis of anterior lens epithelial cells in mice lacking the CREB-2 transcription factor","volume":"222","author":"Hettmann","year":"2000","journal-title":"Dev Biol"},{"key":"10.3945\/an.112.002113_bib106","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1016\/j.gep.2010.10.005","article-title":"Unfolded Protein Response (UPR) is activated during normal lens development","volume":"11","author":"Firtina","year":"2011","journal-title":"Gene Expr Patterns"},{"key":"10.3945\/an.112.002113_bib107","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1016\/S0092-8674(04)00344-7","article-title":"ATF4 is a substrate of RSK2 and an essential regulator of osteoblast biology; implication for Coffin-Lowry Syndrome","volume":"117","author":"Yang","year":"2004","journal-title":"Cell"},{"key":"10.3945\/an.112.002113_bib108","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1016\/j.cmet.2006.10.010","article-title":"ATF4 mediation of NF1 functions in osteoblast reveals a nutritional basis for congenital skeletal dysplasiae","volume":"4","author":"Elefteriou","year":"2006","journal-title":"Cell Metab"},{"key":"10.3945\/an.112.002113_bib109","doi-asserted-by":"crossref","first-page":"2565","DOI":"10.2337\/db09-0335","article-title":"Atf4 regulates obesity, glucose homeostasis, and energy expenditure","volume":"58","author":"Seo","year":"2009","journal-title":"Diabetes"},{"key":"10.3945\/an.112.002113_bib110","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1016\/j.cmet.2009.06.002","article-title":"Translation attenuation through eIF2alpha phosphorylation prevents oxidative stress and maintains the differentiated state in beta cells","volume":"10","author":"Back","year":"2009","journal-title":"Cell Metab"},{"key":"10.3945\/an.112.002113_bib111","doi-asserted-by":"crossref","first-page":"520","DOI":"10.1016\/j.cmet.2008.04.011","article-title":"Dephosphorylation of translation initiation factor 2alpha enhances glucose tolerance and attenuates hepatosteatosis in mice","volume":"7","author":"Oyadomari","year":"2008","journal-title":"Cell Metab"},{"key":"10.3945\/an.112.002113_bib112","doi-asserted-by":"crossref","first-page":"829","DOI":"10.1016\/j.devcel.2008.10.015","article-title":"UPR pathways combine to prevent hepatic steatosis caused by ER stress-mediated suppression of transcriptional master regulators","volume":"15","author":"Rutkowski","year":"2008","journal-title":"Dev Cell"},{"key":"10.3945\/an.112.002113_bib113","doi-asserted-by":"crossref","first-page":"3378","DOI":"10.1172\/JCI34587","article-title":"Chop deletion reduces oxidative stress, improves beta cell function, and promotes cell survival in multiple mouse models of diabetes","volume":"118","author":"Song","year":"2008","journal-title":"J Clin Invest"},{"key":"10.3945\/an.112.002113_bib114","doi-asserted-by":"crossref","first-page":"344","DOI":"10.1006\/geno.2002.6838","article-title":"Mouse Atf5: molecular cloning of two novel mRNAs, genomic organization, and odorant sensory neuron localization","volume":"80","author":"Hansen","year":"2002","journal-title":"Genomics"},{"key":"10.3945\/an.112.002113_bib115","doi-asserted-by":"crossref","first-page":"7064","DOI":"10.1074\/jbc.M708530200","article-title":"Phosphorylation of eIF2 directs ATF5 translational control in response to diverse stress conditions","volume":"283","author":"Zhou","year":"2008","journal-title":"J Biol Chem"},{"key":"10.3945\/an.112.002113_bib116","doi-asserted-by":"crossref","first-page":"2543","DOI":"10.1074\/jbc.M707781200","article-title":"Stress-induced translation of ATF5 mRNA is regulated by the 5\u2032-untranslated region","volume":"283","author":"Watatani","year":"2008","journal-title":"J Biol Chem"},{"key":"10.3945\/an.112.002113_bib117","doi-asserted-by":"crossref","first-page":"739","DOI":"10.1038\/onc.2011.276","article-title":"Regulated ATF5 loss-of-function in adult mice blocks formation and causes regression\/eradication of gliomas","volume":"31","author":"Arias","year":"2013","journal-title":"Oncogene"},{"key":"10.3945\/an.112.002113_bib118","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1111\/j.1471-4159.2008.05749.x","article-title":"The transcription factor ATF5: role in neurodevelopment and neural tumors","volume":"108","author":"Greene","year":"2009","journal-title":"J Neurochem"},{"key":"10.3945\/an.112.002113_bib119","doi-asserted-by":"crossref","first-page":"1351","DOI":"10.1016\/S0022-2836(02)00234-6","article-title":"Two distinct stress signaling pathways converge upon the CHOP promoter during the mammalian unfolded protein response","volume":"318","author":"Ma","year":"2002","journal-title":"J Mol Biol"},{"key":"10.3945\/an.112.002113_bib120","doi-asserted-by":"crossref","first-page":"5288","DOI":"10.1074\/jbc.M311862200","article-title":"Induction of CHOP expression by amino acid limitation requires both ATF4 expression and ATF2 phosphorylation","volume":"279","author":"Averous","year":"2004","journal-title":"J Biol Chem"},{"key":"10.3945\/an.112.002113_bib121","doi-asserted-by":"crossref","first-page":"4341","DOI":"10.1093\/nar\/29.21.4341","article-title":"Inhibition of CHOP translation by a peptide encoded by an open reading frame localized in the chop 5\u2032UTR","volume":"29","author":"Jousse","year":"2001","journal-title":"Nucleic Acids Res"},{"key":"10.3945\/an.112.002113_bib122","doi-asserted-by":"crossref","first-page":"e139","DOI":"10.1093\/nar\/gkr645","article-title":"Transgenic zebrafish model to study translational control mediated by upstream open reading frame of human chop gene","volume":"39","author":"Lee","year":"2011","journal-title":"Nucleic Acids Res"},{"key":"10.3945\/an.112.002113_bib123","doi-asserted-by":"crossref","first-page":"764","DOI":"10.1093\/nar\/gkp1034","article-title":"Differential regulation of CHOP translation by phosphorylated eIF4E under stress conditions","volume":"38","author":"Chen","year":"2010","journal-title":"Nucleic Acids Res"},{"key":"10.3945\/an.112.002113_bib124","doi-asserted-by":"crossref","first-page":"8125","DOI":"10.1093\/nar\/15.20.8125","article-title":"An analysis of 5\u2032-noncoding sequences from 699 vertebrate messenger RNAs","volume":"15","author":"Kozak","year":"1987","journal-title":"Nucleic Acids Res"},{"key":"10.3945\/an.112.002113_bib125","doi-asserted-by":"crossref","first-page":"6661","DOI":"10.1074\/jbc.M806735200","article-title":"An upstream open reading frame regulates translation of GADD34 during cellular stresses that induce eIF2alpha phosphorylation","volume":"284","author":"Lee","year":"2009","journal-title":"J Biol Chem"},{"key":"10.3945\/an.112.002113_bib126","doi-asserted-by":"crossref","first-page":"29066","DOI":"10.1074\/jbc.M402727200","article-title":"BCL-2 translation is mediated via internal ribosome entry during cell stress","volume":"279","author":"Sherrill","year":"2004","journal-title":"J Biol Chem"},{"key":"10.3945\/an.112.002113_bib127","doi-asserted-by":"crossref","first-page":"4665","DOI":"10.1093\/nar\/gkq241","article-title":"Distinct 5\u2032 UTRs regulate XIAP expression under normal growth conditions and during cellular stress","volume":"38","author":"Riley","year":"2010","journal-title":"Nucleic Acids Res"},{"key":"10.3945\/an.112.002113_bib128","doi-asserted-by":"crossref","first-page":"1792","DOI":"10.1091\/mbc.02-02-0017","article-title":"Hypoxia-inducible factor-1alpha mRNA contains an internal ribosome entry site that allows efficient translation during normoxia and hypoxia","volume":"13","author":"Lang","year":"2002","journal-title":"Mol Biol Cell"},{"key":"10.3945\/an.112.002113_bib129","doi-asserted-by":"crossref","first-page":"405","DOI":"10.1016\/j.molcel.2004.12.024","article-title":"Ribosome stalling regulates IRES-mediated translation in eukaryotes, a parallel to prokaryotic attenuation","volume":"17","author":"Fernandez","year":"2005","journal-title":"Mol Cell"},{"key":"10.3945\/an.112.002113_bib130","doi-asserted-by":"crossref","first-page":"511","DOI":"10.1016\/S0092-8674(00)00055-6","article-title":"Initiation of protein synthesis from the A site of the ribosome","volume":"102","author":"Wilson","year":"2000","journal-title":"Cell"},{"key":"10.3945\/an.112.002113_bib131","doi-asserted-by":"crossref","first-page":"e374","DOI":"10.1371\/journal.pbio.0040374","article-title":"Adaptation to ER stress is mediated by differential stabilities of pro-survival and pro-apoptotic mRNAs and proteins","volume":"4","author":"Rutkowski","year":"2006","journal-title":"PLoS Biol"},{"key":"10.3945\/an.112.002113_bib132","doi-asserted-by":"crossref","first-page":"462","DOI":"10.1097\/01.WCB.0000056064.25434.CA","article-title":"Dysfunction of the unfolded protein response during global brain ischemia and reperfusion","volume":"23","author":"Kumar","year":"2003","journal-title":"J Cereb Blood Flow Metab"},{"key":"10.3945\/an.112.002113_bib133","doi-asserted-by":"crossref","first-page":"568","DOI":"10.1053\/j.gastro.2007.10.039","article-title":"Activation and dysregulation of the unfolded protein response in nonalcoholic fatty liver disease","volume":"134","author":"Puri","year":"2008","journal-title":"Gastroenterology"},{"key":"10.3945\/an.112.002113_bib134","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1247\/csf.07044","article-title":"ATF6 is a transcription factor specializing in the regulation of quality control proteins in the endoplasmic reticulum","volume":"33","author":"Adachi","year":"2008","journal-title":"Cell Struct Funct"},{"key":"10.3945\/an.112.002113_bib135","doi-asserted-by":"crossref","first-page":"6091","DOI":"10.1074\/jbc.M109.014092","article-title":"Regulation of endoplasmic reticulum stress-induced cell death by ATF4 in neuroectodermal tumor cells","volume":"285","author":"Armstrong","year":"2010","journal-title":"J Biol Chem"},{"key":"10.3945\/an.112.002113_bib136","doi-asserted-by":"crossref","first-page":"24120","DOI":"10.1074\/jbc.M201959200","article-title":"ATF4 is a mediator of the nutrient-sensing response pathway that activates the human asparagine synthetase gene","volume":"277","author":"Siu","year":"2002","journal-title":"J Biol Chem"},{"key":"10.3945\/an.112.002113_bib137","doi-asserted-by":"crossref","first-page":"1007","DOI":"10.1161\/ATVBAHA.110.204354","article-title":"Oxidized phospholipids regulate expression of ATF4 and VEGF in endothelial cells via NRF2-dependent mechanism: novel point of convergence between electrophilic and unfolded protein stress pathways","volume":"30","author":"Afonyushkin","year":"2010","journal-title":"Arterioscler Thromb Vasc Biol"},{"key":"10.3945\/an.112.002113_bib138","doi-asserted-by":"crossref","first-page":"1226","DOI":"10.1167\/iovs.10-5775","article-title":"Transcriptional regulation of activating transcription factor 4 under oxidative stress in retinal pigment epithelial ARPE-19\/HPV-16 cells","volume":"52","author":"Miyamoto","year":"2011","journal-title":"Invest Ophthalmol Vis Sci"},{"key":"10.3945\/an.112.002113_bib139","first-page":"5027","article-title":"Pleiotropic resistance to DNA-interactive drugs is associated with increased expression of genes involved in DNA replication, repair, and stress response","volume":"60","author":"Levenson","year":"2000","journal-title":"Cancer Res"},{"key":"10.3945\/an.112.002113_bib140","first-page":"8592","article-title":"Activating transcription factor 4 increases the cisplatin resistance of human cancer cell lines","volume":"63","author":"Tanabe","year":"2003","journal-title":"Cancer Res"},{"key":"10.3945\/an.112.002113_bib141","doi-asserted-by":"crossref","first-page":"4749","DOI":"10.1038\/sj.onc.1210289","article-title":"Clock and ATF4 transcription system regulates drug resistance in human cancer cell lines","volume":"26","author":"Igarashi","year":"2007","journal-title":"Oncogene"},{"key":"10.3945\/an.112.002113_bib142","doi-asserted-by":"crossref","first-page":"19090","DOI":"10.1073\/pnas.0904849106","article-title":"Pdx1 (MODY4) regulates pancreatic beta cell susceptibility to ER stress","volume":"106","author":"Sachdeva","year":"2009","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.3945\/an.112.002113_bib143","doi-asserted-by":"crossref","first-page":"703","DOI":"10.1016\/S0092-8674(00)81668-2","article-title":"Transport-dependent proteolysis of SREBP: relocation of site-1 protease from Golgi to ER obviates the need for SREBP transport to Golgi","volume":"99","author":"DeBose-Boyd","year":"1999","journal-title":"Cell"},{"key":"10.3945\/an.112.002113_bib144","doi-asserted-by":"crossref","first-page":"43046","DOI":"10.1074\/jbc.M408466200","article-title":"Dependence of site-2 protease cleavage of ATF6 on prior site-1 protease digestion is determined by the size of the luminal domain of ATF6","volume":"279","author":"Shen","year":"2004","journal-title":"J Biol Chem"},{"key":"10.3945\/an.112.002113_bib145","doi-asserted-by":"crossref","first-page":"92","DOI":"10.1038\/415092a","article-title":"IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA","volume":"415","author":"Calfon","year":"2002","journal-title":"Nature"},{"key":"10.3945\/an.112.002113_bib146","doi-asserted-by":"crossref","first-page":"881","DOI":"10.1016\/S0092-8674(01)00611-0","article-title":"XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor","volume":"107","author":"Yoshida","year":"2001","journal-title":"Cell"},{"key":"10.3945\/an.112.002113_bib147","doi-asserted-by":"crossref","first-page":"541","DOI":"10.1016\/j.molcel.2007.12.023","article-title":"Loss of the tuberous sclerosis complex tumor suppressors triggers the unfolded protein response to regulate insulin signaling and apoptosis","volume":"29","author":"Ozcan","year":"2008","journal-title":"Mol Cell"},{"key":"10.3945\/an.112.002113_bib148","doi-asserted-by":"crossref","first-page":"457","DOI":"10.1126\/science.1103160","article-title":"Endoplasmic reticulum stress links obesity, insulin action, and type 2 diabetes","volume":"306","author":"Ozcan","year":"2004","journal-title":"Science"},{"key":"10.3945\/an.112.002113_bib149","doi-asserted-by":"crossref","first-page":"664","DOI":"10.1126\/science.287.5453.664","article-title":"Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1","volume":"287","author":"Urano","year":"2000","journal-title":"Science"},{"key":"10.3945\/an.112.002113_bib150","doi-asserted-by":"crossref","first-page":"508","DOI":"10.1634\/theoncologist.8-6-508","article-title":"Velcade: U.S. FDA approval for the treatment of multiple myeloma progressing on prior therapy","volume":"8","author":"Kane","year":"2003","journal-title":"Oncologist"},{"key":"10.3945\/an.112.002113_bib151","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1038\/cdd.2010.82","article-title":"The TSC1 and TSC2 tumor suppressors are required for proper ER stress response and protect cells from ER stress-induced apoptosis","volume":"18","author":"Kang","year":"2011","journal-title":"Cell Death Differ"},{"key":"10.3945\/an.112.002113_bib152","doi-asserted-by":"crossref","first-page":"783","DOI":"10.1083\/jcb.201003138","article-title":"Regulation of basal cellular physiology by the homeostatic unfolded protein response","volume":"189","author":"Rutkowski","year":"2010","journal-title":"J Cell Biol"},{"key":"10.3945\/an.112.002113_bib153","doi-asserted-by":"crossref","first-page":"184","DOI":"10.1038\/ncb0311-184","article-title":"Integrating the mechanisms of apoptosis induced by endoplasmic reticulum stress","volume":"13","author":"Tabas","year":"2011","journal-title":"Nat Cell Biol"},{"key":"10.3945\/an.112.002113_bib154","doi-asserted-by":"crossref","first-page":"1158","DOI":"10.1016\/j.freeradbiomed.2009.01.015","article-title":"Activating transcription factor 4 and CCAAT\/enhancer-binding protein-beta negatively regulate the mammalian target of rapamycin via Redd1 expression in response to oxidative and endoplasmic reticulum stress","volume":"46","author":"Jin","year":"2009","journal-title":"Free Radic Biol Med"},{"key":"10.3945\/an.112.002113_bib155","doi-asserted-by":"crossref","first-page":"5834","DOI":"10.1128\/MCB.25.14.5834-5845.2005","article-title":"Regulation of mTOR and cell growth in response to energy stress by REDD1","volume":"25","author":"Sofer","year":"2005","journal-title":"Mol Cell Biol"},{"key":"10.3945\/an.112.002113_bib156","doi-asserted-by":"crossref","first-page":"451","DOI":"10.1016\/j.bbrc.2008.12.079","article-title":"ATF4 is necessary and sufficient for ER stress-induced upregulation of REDD1 expression","volume":"379","author":"Whitney","year":"2009","journal-title":"Biochem Biophys Res Commun"},{"key":"10.3945\/an.112.002113_bib157","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1016\/j.cmet.2008.01.008","article-title":"ATF4-mediated induction of 4E\u2013BP1 contributes to pancreatic beta cell survival under endoplasmic reticulum stress","volume":"7","author":"Yamaguchi","year":"2008","journal-title":"Cell Metab"},{"key":"10.3945\/an.112.002113_bib158","doi-asserted-by":"crossref","first-page":"1153","DOI":"10.1016\/S1097-2765(01)00264-7","article-title":"Diabetes mellitus and exocrine pancreatic dysfunction in PERK\u2212\/\u2212 mice reveals a role for translational control in secretory cell survival","volume":"7","author":"Harding","year":"2001","journal-title":"Mol Cell"},{"key":"10.3945\/an.112.002113_bib159","doi-asserted-by":"crossref","first-page":"3864","DOI":"10.1128\/MCB.22.11.3864-3874.2002","article-title":"The PERK eukaryotic initiation factor 2 alpha kinase is required for the development of the skeletal system, postnatal growth, and the function and viability of the pancreas","volume":"22","author":"Zhang","year":"2002","journal-title":"Mol Cell Biol"},{"key":"10.3945\/an.112.002113_bib160","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1016\/j.cmet.2006.11.002","article-title":"PERK EIF2AK3 control of pancreatic beta cell differentiation and proliferation is required for postnatal glucose homeostasis","volume":"4","author":"Zhang","year":"2006","journal-title":"Cell Metab"},{"key":"10.3945\/an.112.002113_bib161","doi-asserted-by":"crossref","first-page":"38","DOI":"10.1186\/1471-2121-8-38","article-title":"PERK eIF2 alpha kinase is required to regulate the viability of the exocrine pancreas in mice","volume":"8","author":"Iida","year":"2007","journal-title":"BMC Cell Biol"},{"key":"10.3945\/an.112.002113_bib162","doi-asserted-by":"crossref","first-page":"409","DOI":"10.2337\/diabetes.52.2.409","article-title":"Dominant negative pathogenesis by mutant proinsulin in the Akita diabetic mouse","volume":"52","author":"Izumi","year":"2003","journal-title":"Diabetes"},{"key":"10.3945\/an.112.002113_bib163","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1172\/JCI4431","article-title":"A mutation in the insulin 2 gene induces diabetes with severe pancreatic beta-cell dysfunction in the Mody mouse","volume":"103","author":"Wang","year":"1999","journal-title":"J Clin Invest"},{"key":"10.3945\/an.112.002113_bib164","doi-asserted-by":"crossref","first-page":"15040","DOI":"10.1073\/pnas.0707291104","article-title":"Insulin gene mutations as a cause of permanent neonatal diabetes","volume":"104","author":"St\u00f8y","year":"2007","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.3945\/an.112.002113_bib165","doi-asserted-by":"crossref","first-page":"452","DOI":"10.2337\/diabetes.54.2.452","article-title":"Cytokines downregulate the sarcoendoplasmic reticulum pump Ca2+ ATPase 2b and deplete endoplasmic reticulum Ca2+, leading to induction of endoplasmic reticulum stress in pancreatic beta-cells","volume":"54","author":"Cardozo","year":"2005","journal-title":"Diabetes"},{"key":"10.3945\/an.112.002113_bib166","doi-asserted-by":"crossref","first-page":"3398","DOI":"10.1210\/en.2005-1494","article-title":"Chronic palmitate but not oleate exposure induces endoplasmic reticulum stress, which may contribute to INS-1 pancreatic beta-cell apoptosis","volume":"147","author":"Karaskov","year":"2006","journal-title":"Endocrinology"},{"key":"10.3945\/an.112.002113_bib167","doi-asserted-by":"crossref","first-page":"5087","DOI":"10.1210\/en.2004-0478","article-title":"Free fatty acids and cytokines induce pancreatic beta-cell apoptosis by different mechanisms: role of nuclear factor-kappaB and endoplasmic reticulum stress","volume":"145","author":"Kharroubi","year":"2004","journal-title":"Endocrinology"},{"key":"10.3945\/an.112.002113_bib168","doi-asserted-by":"crossref","first-page":"10845","DOI":"10.1073\/pnas.191207498","article-title":"Nitric oxide-induced apoptosis in pancreatic beta cells is mediated by the endoplasmic reticulum stress pathway","volume":"98","author":"Oyadomari","year":"2001","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.3945\/an.112.002113_bib169","doi-asserted-by":"crossref","first-page":"525","DOI":"10.1172\/JCI0214550","article-title":"Targeted disruption of the Chop gene delays endoplasmic reticulum stress-mediated diabetes","volume":"109","author":"Oyadomari","year":"2002","journal-title":"J Clin Invest"},{"key":"10.3945\/an.112.002113_bib170","doi-asserted-by":"crossref","first-page":"3616","DOI":"10.1128\/MCB.05164-11","article-title":"PERK integrates autophagy and oxidative stress responses to promote survival during extracellular matrix detachment","volume":"31","author":"Avivar-Valderas","year":"2011","journal-title":"Mol Cell Biol"},{"key":"10.3945\/an.112.002113_bib171","doi-asserted-by":"crossref","first-page":"1243","DOI":"10.1038\/sj.emboj.7600596","article-title":"TRB3, a novel ER stress-inducible gene, is induced via ATF4-CHOP pathway and is involved in cell death","volume":"24","author":"Ohoka","year":"2005","journal-title":"EMBO J"},{"key":"10.3945\/an.112.002113_bib172","doi-asserted-by":"crossref","first-page":"1337","DOI":"10.1016\/j.cell.2007.04.027","article-title":"ER stress triggers apoptosis by activating BH3-only protein Bim","volume":"129","author":"Puthalakath","year":"2007","journal-title":"Cell"},{"key":"10.3945\/an.112.002113_bib173","doi-asserted-by":"crossref","first-page":"45495","DOI":"10.1074\/jbc.M406933200","article-title":"CHOP is involved in endoplasmic reticulum stress-induced apoptosis by enhancing DR5 expression in human carcinoma cells","volume":"279","author":"Yamaguchi","year":"2004","journal-title":"J Biol Chem"},{"key":"10.3945\/an.112.002113_bib174","doi-asserted-by":"crossref","first-page":"5662","DOI":"10.1158\/0008-5472.CAN-05-0693","article-title":"Proteasome inhibitor MG132 induces death receptor 5 through CCAAT\/enhancer-binding protein homologous protein","volume":"65","author":"Yoshida","year":"2005","journal-title":"Cancer Res"},{"key":"10.3945\/an.112.002113_bib175","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1038\/2441","article-title":"A gene encoding a transmembrane protein is mutated in patients with diabetes mellitus and optic atrophy (Wolfram syndrome)","volume":"20","author":"Inoue","year":"1998","journal-title":"Nat Genet"},{"key":"10.3945\/an.112.002113_bib176","doi-asserted-by":"crossref","first-page":"2021","DOI":"10.1093\/hmg\/7.13.2021","article-title":"Diabetes insipidus, diabetes mellitus, optic atrophy and deafness (DIDMOAD) caused by mutations in a novel gene (wolframin) coding for a predicted transmembrane protein","volume":"7","author":"Strom","year":"1998","journal-title":"Hum Mol Genet"},{"key":"10.3945\/an.112.002113_bib177","doi-asserted-by":"crossref","first-page":"52755","DOI":"10.1074\/jbc.M310331200","article-title":"Wolframin expression induces novel ion channel activity in endoplasmic reticulum membranes and increases intracellular calcium","volume":"278","author":"Osman","year":"2003","journal-title":"J Biol Chem"},{"key":"10.3945\/an.112.002113_bib178","doi-asserted-by":"crossref","first-page":"2003","DOI":"10.1093\/hmg\/ddg214","article-title":"Wolfram syndrome: structural and functional analyses of mutant and wild-type wolframin, the WFS1 gene product","volume":"12","author":"Hofmann","year":"2003","journal-title":"Hum Mol Genet"},{"key":"10.3945\/an.112.002113_bib179","first-page":"266","article-title":"Endoplasmic reticulum stress and pancreatic beta-cell death","volume":"22","author":"Fonseca","year":"2011","journal-title":"Trends Endocrinol Metab"},{"key":"10.3945\/an.112.002113_bib180","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1146\/annurev.nutr.27.061406.093726","article-title":"Mechanisms of food intake repression in indispensable amino acid deficiency","volume":"27","author":"Gietzen","year":"2007","journal-title":"Annu Rev Nutr"},{"key":"10.3945\/an.112.002113_bib181","doi-asserted-by":"crossref","first-page":"1776","DOI":"10.1126\/science.1104882","article-title":"Uncharged tRNA and sensing of amino acid deficiency in mammalian piriform cortex","volume":"307","author":"Hao","year":"2005","journal-title":"Science"},{"key":"10.3945\/an.112.002113_bib182","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1016\/j.cmet.2005.03.004","article-title":"The GCN2 kinase biases feeding behavior to maintain amino acid homeostasis in omnivores","volume":"1","author":"Maurin","year":"2005","journal-title":"Cell Metab"},{"key":"10.3945\/an.112.002113_bib183","doi-asserted-by":"crossref","first-page":"1166","DOI":"10.1038\/nature03897","article-title":"Translational control of hippocampal synaptic plasticity and memory by the eIF2alpha kinase GCN2","volume":"436","author":"Costa-Mattioli","year":"2005","journal-title":"Nature"},{"key":"10.3945\/an.112.002113_bib184","doi-asserted-by":"crossref","first-page":"244","DOI":"10.1055\/s-2008-1071551","article-title":"Diffuse white matter disease in three children: an encephalopathy with unique features on magnetic resonance imaging and proton magnetic resonance spectroscopy","volume":"24","author":"Hanefeld","year":"1993","journal-title":"Neuropediatrics"},{"key":"10.3945\/an.112.002113_bib185","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1002\/ana.410350314","article-title":"Childhood ataxia with diffuse central nervous system hypomyelination","volume":"35","author":"Schiffmann","year":"1994","journal-title":"Ann Neurol"},{"key":"10.3945\/an.112.002113_bib186","doi-asserted-by":"crossref","first-page":"987","DOI":"10.1097\/NEN.0b013e3181f2eafa","article-title":"Leukoencephalopathy with vanishing white matter: a review","volume":"69","author":"Bugiani","year":"2010","journal-title":"J Neuropathol Exp Neurol"},{"key":"10.3945\/an.112.002113_bib187","doi-asserted-by":"crossref","first-page":"3295","DOI":"10.1128\/MCB.24.8.3295-3306.2004","article-title":"Mutations linked to leukoencephalopathy with vanishing white matter impair the function of the eukaryotic initiation factor 2B complex in diverse ways","volume":"24","author":"Li","year":"2004","journal-title":"Mol Cell Biol"},{"key":"10.3945\/an.112.002113_bib188","doi-asserted-by":"crossref","first-page":"383","DOI":"10.1038\/ng764","article-title":"Subunits of the translation initiation factor eIF2B are mutant in leukoencephalopathy with vanishing white matter","volume":"29","author":"Leegwater","year":"2001","journal-title":"Nat Genet"},{"key":"10.3945\/an.112.002113_bib189","doi-asserted-by":"crossref","first-page":"2352","DOI":"10.1128\/MCB.24.6.2352-2363.2004","article-title":"Mutations causing childhood ataxia with central nervous system hypomyelination reduce eukaryotic initiation factor 2B complex formation and activity","volume":"24","author":"Richardson","year":"2004","journal-title":"Mol Cell Biol"},{"key":"10.3945\/an.112.002113_bib190","doi-asserted-by":"crossref","first-page":"629","DOI":"10.1146\/annurev.biochem.75.103004.142520","article-title":"Asparagine synthetase chemotherapy","volume":"75","author":"Richards","year":"2006","journal-title":"Annu Rev Biochem"},{"key":"10.3945\/an.112.002113_bib191","doi-asserted-by":"crossref","first-page":"9517","DOI":"10.1128\/MCB.01145-06","article-title":"Perk-dependent translational regulation promotes tumor cell adaptation and angiogenesis in response to hypoxic stress","volume":"26","author":"Blais","year":"2006","journal-title":"Mol Cell Biol"}],"container-title":["Advances in Nutrition"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2161831322009991?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S2161831322009991?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/academic.oup.com\/advances\/article-pdf\/3\/3\/307\/23735435\/307.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,9,15]],"date-time":"2024-09-15T03:24:43Z","timestamp":1726370683000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S2161831322009991"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2012,5]]},"references-count":191,"journal-issue":{"issue":"3","published-print":{"date-parts":[[2012,5]]}},"alternative-id":["S2161831322009991"],"URL":"https:\/\/doi.org\/10.3945\/an.112.002113","relation":{},"ISSN":["2161-8313"],"issn-type":[{"value":"2161-8313","type":"print"}],"subject":[],"published":{"date-parts":[[2012,5]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Eukaryotic Initiation Factor 2 Phosphorylation and Translational Control in Metabolism","name":"articletitle","label":"Article Title"},{"value":"Advances in Nutrition","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.3945\/an.112.002113","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2012 American Society for Nutrition","name":"copyright","label":"Copyright"}]}}