{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,2]],"date-time":"2026-04-02T06:56:05Z","timestamp":1775112965944,"version":"3.50.1"},"reference-count":68,"publisher":"Elsevier BV","issue":"7","license":[{"start":{"date-parts":[[2014,2,1]],"date-time":"2014-02-01T00:00:00Z","timestamp":1391212800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2014,2,1]],"date-time":"2014-02-01T00:00:00Z","timestamp":1391212800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2020,9,7]],"date-time":"2020-09-07T00:00:00Z","timestamp":1599436800000},"content-version":"vor","delay-in-days":2410,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["jbc.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2014,2]]},"DOI":"10.1074\/jbc.m113.518191","type":"journal-article","created":{"date-parts":[[2014,1,2]],"date-time":"2014-01-02T01:08:43Z","timestamp":1388624923000},"page":"3936-3949","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":29,"title":["mRNA Decapping Enzyme 1a (Dcp1a)-induced Translational Arrest through Protein Kinase R (PKR) Activation Requires the N-terminal Enabled Vasodilator-stimulated Protein Homology 1 (EVH1) Domain"],"prefix":"10.1016","volume":"289","author":[{"given":"Jonathan D.","family":"Dougherty","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Lucas C.","family":"Reineke","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Richard E.","family":"Lloyd","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1074\/jbc.M113.518191_bib1","doi-asserted-by":"crossref","first-page":"871","DOI":"10.1083\/jcb.200502088","article-title":"Stress granules and processing bodies are dynamically linked sites of mRNP remodeling","volume":"169","author":"Kedersha","year":"2005","journal-title":"J. Cell Biol"},{"key":"10.1074\/jbc.M113.518191_bib2","doi-asserted-by":"crossref","first-page":"430","DOI":"10.1038\/nrm2694","article-title":"RNA granules. Post-transcriptional and epigenetic modulators of gene expression","volume":"10","author":"Anderson","year":"2009","journal-title":"Nat. Rev. Mol. Cell Biol"},{"key":"10.1074\/jbc.M113.518191_bib3","doi-asserted-by":"crossref","first-page":"805","DOI":"10.1126\/science.1082320","article-title":"Decapping and decay of messenger RNA occur in cytoplasmic processing bodies","volume":"300","author":"Sheth","year":"2003","journal-title":"Science"},{"key":"10.1074\/jbc.M113.518191_bib4","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1083\/jcb.200309008","article-title":"Cytoplasmic foci are sites of mRNA decay in human cells","volume":"165","author":"Cougot","year":"2004","journal-title":"J. Cell Biol"},{"key":"10.1074\/jbc.M113.518191_bib5","doi-asserted-by":"crossref","first-page":"3970","DOI":"10.1128\/MCB.00128-07","article-title":"P-body formation is a consequence, not the cause, of RNA-mediated gene silencing","volume":"27","author":"Eulalio","year":"2007","journal-title":"Mol. Cell. Biol"},{"key":"10.1074\/jbc.M113.518191_bib6","doi-asserted-by":"crossref","first-page":"605","DOI":"10.1016\/j.molcel.2008.11.001","article-title":"The control of mRNA decapping and P-body formation","volume":"32","author":"Franks","year":"2008","journal-title":"Mol. Cell"},{"key":"10.1074\/jbc.M113.518191_bib7","doi-asserted-by":"crossref","first-page":"642","DOI":"10.1038\/382642a0","article-title":"An essential component of the decapping enzyme required for normal rates of mRNA turnover","volume":"382","author":"Beelman","year":"1996","journal-title":"Nature"},{"key":"10.1074\/jbc.M113.518191_bib8","doi-asserted-by":"crossref","first-page":"905","DOI":"10.1016\/j.molcel.2005.10.031","article-title":"Multiple processing body factors and the ARE binding protein TTP activate mRNA decapping","volume":"20","author":"Fenger-Gr\u00f8n","year":"2005","journal-title":"Mol. Cell"},{"key":"10.1074\/jbc.M113.518191_bib9","doi-asserted-by":"crossref","first-page":"8114","DOI":"10.1128\/MCB.22.23.8114-8121.2002","article-title":"Identification of a human decapping complex associated with hUpf proteins in nonsense-mediated decay","volume":"22","author":"Lykke-Andersen","year":"2002","journal-title":"Mol. Cell. Biol"},{"key":"10.1074\/jbc.M113.518191_bib10","doi-asserted-by":"crossref","first-page":"745","DOI":"10.1016\/j.molcel.2011.09.019","article-title":"Reconsidering movement of eukaryotic mRNAs between polysomes and P bodies","volume":"44","author":"Arribere","year":"2011","journal-title":"Mol. Cell"},{"key":"10.1074\/jbc.M113.518191_bib11","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1083\/jcb.200801196","article-title":"Deadenylation is prerequisite for P-body formation and mRNA decay in mammalian cells","volume":"182","author":"Zheng","year":"2008","journal-title":"J. Cell Biol"},{"key":"10.1074\/jbc.M113.518191_bib12","doi-asserted-by":"crossref","first-page":"1054","DOI":"10.1038\/nsmb1016","article-title":"Concerted action of poly(A) nucleases and decapping enzyme in mammalian mRNA turnover","volume":"12","author":"Yamashita","year":"2005","journal-title":"Nat. Struct. Mol. Biol"},{"key":"10.1074\/jbc.M113.518191_bib13","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1016\/j.virol.2012.11.017","article-title":"Diversion of stress granules and P-bodies during viral infection","volume":"436","author":"Reineke","year":"2013","journal-title":"Virology"},{"key":"10.1074\/jbc.M113.518191_bib14","doi-asserted-by":"crossref","first-page":"64","DOI":"10.1128\/JVI.01657-10","article-title":"Poliovirus-mediated disruption of cytoplasmic processing bodies","volume":"85","author":"Dougherty","year":"2011","journal-title":"J. Virol"},{"key":"10.1074\/jbc.M113.518191_bib15","doi-asserted-by":"crossref","first-page":"9041","DOI":"10.1073\/pnas.0703348104","article-title":"Interaction of TIA-1\/TIAR with West Nile and dengue virus products in infected cells interferes with stress granule formation and processing body assembly","volume":"104","author":"Emara","year":"2007","journal-title":"Proc. Natl. Acad. Sci"},{"key":"10.1074\/jbc.M113.518191_bib16","doi-asserted-by":"crossref","first-page":"6882","DOI":"10.1128\/JVI.02418-10","article-title":"Hepatitis C virus hijacks P-body and stress granule components around lipid droplets","volume":"85","author":"Ariumi","year":"2011","journal-title":"J. Virol"},{"key":"10.1074\/jbc.M113.518191_bib17","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.virol.2012.09.041","article-title":"P-body components LSM1, GW182, DDX3, DDX6 and XRN1 are recruited to WNV replication sites and positively regulate viral replication","volume":"436","author":"Chahar","year":"2013","journal-title":"Virology"},{"key":"10.1074\/jbc.M113.518191_bib18","doi-asserted-by":"crossref","first-page":"1173","DOI":"10.4161\/rna.8.6.17836","article-title":"Quantitative mass spectrometry of DENV-2 RNA-interacting proteins reveals that the DEAD-box RNA helicase DDX6 binds the DB1 and DB2 3\u2032 UTR structures","volume":"8","author":"Ward","year":"2011","journal-title":"RNA Biol"},{"key":"10.1074\/jbc.M113.518191_bib19","doi-asserted-by":"crossref","first-page":"131","DOI":"10.4161\/pri.2.4.7773","article-title":"Intracellular trafficking and dynamics of P bodies","volume":"2","author":"Aizer","year":"2008","journal-title":"Prion"},{"key":"10.1074\/jbc.M113.518191_bib20","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1242\/jcs.072140","article-title":"Cytoplasmic mRNP granules at a glance","volume":"124","author":"Erickson","year":"2011","journal-title":"J. Cell Sci"},{"key":"10.1074\/jbc.M113.518191_bib21","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1038\/nsmb0106-7","article-title":"More than 1 + 2 in mRNA decapping","volume":"13","author":"Bail","year":"2006","journal-title":"Nat. Struct. Mol. Biol"},{"key":"10.1074\/jbc.M113.518191_bib22","doi-asserted-by":"crossref","first-page":"241","DOI":"10.1016\/j.tibs.2006.03.001","article-title":"New insights into the control of mRNA decapping","volume":"31","author":"Simon","year":"2006","journal-title":"Trends Biochem. Sci"},{"key":"10.1074\/jbc.M113.518191_bib23","doi-asserted-by":"crossref","first-page":"1126","DOI":"10.1016\/S1097-2765(03)00198-9","article-title":"mRNA decay. X (XRN1) marks the spot","volume":"11","author":"Long","year":"2003","journal-title":"Mol. Cell"},{"key":"10.1074\/jbc.M113.518191_bib24","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.molcel.2004.06.031","article-title":"Regulation of mRNA decay. Decapping goes solo","volume":"15","author":"Jacobson","year":"2004","journal-title":"Mol. Cell"},{"key":"10.1074\/jbc.M113.518191_bib25","doi-asserted-by":"crossref","first-page":"861","DOI":"10.1146\/annurev.biochem.73.011303.074032","article-title":"Eukaryotic mRNA decapping","volume":"73","author":"Coller","year":"2004","journal-title":"Annu. Rev. Biochem"},{"key":"10.1074\/jbc.M113.518191_bib26","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1016\/0003-9861(87)90040-3","article-title":"A 5\u2032-3\u2032 exoribonuclease of Saccharomyces cerevisiae. Size and novel substrate specificity","volume":"252","author":"Stevens","year":"1987","journal-title":"Arch. Biochem. Biophys"},{"key":"10.1074\/jbc.M113.518191_bib27","doi-asserted-by":"crossref","first-page":"932","DOI":"10.1016\/j.molcel.2009.11.020","article-title":"Eukaryotic stress granules. The ins and outs of translation","volume":"36","author":"Buchan","year":"2009","journal-title":"Mol. Cell"},{"key":"10.1074\/jbc.M113.518191_bib28","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1016\/S0076-6879(01)42549-3","article-title":"5\u2032-exoribonuclease 1. Xrn1","volume":"342","author":"Stevens","year":"2001","journal-title":"Methods Enzymol"},{"key":"10.1074\/jbc.M113.518191_bib29","doi-asserted-by":"crossref","first-page":"6915","DOI":"10.1093\/emboj\/cdf678","article-title":"Human Dcp2. A catalytically active mRNA decapping enzyme located in specific cytoplasmic structures","volume":"21","author":"van Dijk","year":"2002","journal-title":"EMBO J"},{"key":"10.1074\/jbc.M113.518191_bib30","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1038\/nsmb730","article-title":"Crystal structure of Dcp1p and its functional implications in mRNA decapping","volume":"11","author":"She","year":"2004","journal-title":"Nat. Struct. Mol. Biol"},{"key":"10.1074\/jbc.M113.518191_bib31","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1016\/j.molcel.2008.01.002","article-title":"Structural basis of dcp2 recognition and activation by dcp1","volume":"29","author":"She","year":"2008","journal-title":"Mol. Cell"},{"key":"10.1074\/jbc.M113.518191_bib32","doi-asserted-by":"crossref","first-page":"581","DOI":"10.1083\/jcb.201006089","article-title":"c-Jun N-terminal kinase phosphorylates DCP1a to control formation of P bodies","volume":"194","author":"Rzeczkowski","year":"2011","journal-title":"J. Cell Biol"},{"key":"10.1074\/jbc.M113.518191_bib33","doi-asserted-by":"crossref","first-page":"e49783","DOI":"10.1371\/journal.pone.0049783","article-title":"The P body protein Dcp1a is hyper-phosphorylated during mitosis","volume":"8","author":"Aizer","year":"2013","journal-title":"PLoS ONE"},{"key":"10.1074\/jbc.M113.518191_bib34","doi-asserted-by":"crossref","first-page":"4154","DOI":"10.1091\/mbc.e08-05-0513","article-title":"The dynamics of mammalian P body transport, assembly, and disassembly in vivo","volume":"19","author":"Aizer","year":"2008","journal-title":"Mol. Biol. Cell"},{"key":"10.1074\/jbc.M113.518191_bib35","doi-asserted-by":"crossref","first-page":"21591","DOI":"10.1073\/pnas.0909871106","article-title":"DCP1 forms asymmetric trimers to assemble into active mRNA decapping complexes in metazoa","volume":"106","author":"Tritschler","year":"2009","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M113.518191_bib36","doi-asserted-by":"crossref","first-page":"e61697","DOI":"10.1371\/journal.pone.0061697","article-title":"Phosphorylation of mRNA decapping protein Dcp1a by the ERK signaling pathway during early differentiation of 3T3-L1 preadipocytes","volume":"8","author":"Chiang","year":"2013","journal-title":"PLoS ONE"},{"key":"10.1074\/jbc.M113.518191_bib37","doi-asserted-by":"crossref","first-page":"178","DOI":"10.1016\/S0014-5793(02)02751-5","article-title":"An EVH1\/WH1 domain as a key actor in TGF\u03b2 signalling","volume":"519","author":"Callebaut","year":"2002","journal-title":"FEBS Lett"},{"key":"10.1074\/jbc.M113.518191_bib38","doi-asserted-by":"crossref","first-page":"324","DOI":"10.1016\/j.molcel.2007.11.027","article-title":"mRNA decapping is promoted by an RNA-binding channel in Dcp2","volume":"29","author":"Deshmukh","year":"2008","journal-title":"Mol. Cell"},{"key":"10.1074\/jbc.M113.518191_bib39","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1016\/S0092-8674(00)80757-6","article-title":"Structure of the enabled\/VASP homology 1 domain-peptide complex. A key component in the spatial control of actin assembly","volume":"97","author":"Prehoda","year":"1999","journal-title":"Cell"},{"key":"10.1074\/jbc.M113.518191_bib40","doi-asserted-by":"crossref","first-page":"1071","DOI":"10.1016\/j.molcel.2007.10.033","article-title":"Tes, a specific Mena interacting partner, breaks the rules for EVH1 binding","volume":"28","author":"Bo\u00ebda","year":"2007","journal-title":"Mol. Cell"},{"key":"10.1074\/jbc.M113.518191_bib41","doi-asserted-by":"crossref","first-page":"278","DOI":"10.1261\/rna.2382011","article-title":"Dcp1 links coactivators of mRNA decapping to Dcp2 by proline recognition","volume":"17","author":"Borja","year":"2011","journal-title":"RNA"},{"key":"10.1074\/jbc.M113.518191_bib42","doi-asserted-by":"crossref","first-page":"1324","DOI":"10.1038\/nsmb.2413","article-title":"A direct interaction between DCP1 and XRN1 couples mRNA decapping to 5\u2032 exonucleolytic degradation","volume":"19","author":"Braun","year":"2012","journal-title":"Nat. Struct. Mol. Biol"},{"key":"10.1074\/jbc.M113.518191_bib43","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1016\/S0014-5793(01)03291-4","article-title":"EVH1 domains. Structure, function and interactions","volume":"513","author":"Ball","year":"2002","journal-title":"FEBS Lett"},{"key":"10.1074\/jbc.M113.518191_bib44","doi-asserted-by":"crossref","first-page":"415","DOI":"10.1016\/0042-6822(83)90180-0","article-title":"The effect of poliovirus infection on the translation in vitro of VSV messenger ribonucleoprotein particles","volume":"129","author":"Jones","year":"1983","journal-title":"Virology"},{"key":"10.1074\/jbc.M113.518191_bib45","doi-asserted-by":"crossref","first-page":"2010","DOI":"10.1101\/gad.1219104","article-title":"UNR, a new partner of poly(A)-binding protein, plays a key role in translationally coupled mRNA turnover mediated by the c-fos major coding-region determinant","volume":"18","author":"Chang","year":"2004","journal-title":"Genes Dev"},{"key":"10.1074\/jbc.M113.518191_bib46","doi-asserted-by":"crossref","first-page":"10837","DOI":"10.1073\/pnas.89.22.10837","article-title":"Mechanism of interferon action: autoregulation of RNA-dependent P1\/eIF-2 \u03b1 protein kinase (PKR) expression in transfected mammalian cells","volume":"89","author":"Thomis","year":"1992","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1074\/jbc.M113.518191_bib47","doi-asserted-by":"crossref","first-page":"20688","DOI":"10.1074\/jbc.M110.209452","article-title":"RNA binding targets aminoacyl-tRNA synthetases to translating ribosomes","volume":"286","author":"David","year":"2011","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M113.518191_bib48","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1038\/nmeth.1314","article-title":"SUnSET, a nonradioactive method to monitor protein synthesis","volume":"6","author":"Schmidt","year":"2009","journal-title":"Nat. Methods"},{"key":"10.1074\/jbc.M113.518191_bib49","doi-asserted-by":"crossref","first-page":"16925","DOI":"10.1074\/jbc.M412882200","article-title":"Heme-regulated inhibitor kinase-mediated phosphorylation of eukaryotic translation initiation factor 2 inhibits translation, induces stress granule formation, and mediates survival upon arsenite exposure","volume":"280","author":"McEwen","year":"2005","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M113.518191_bib50","doi-asserted-by":"crossref","first-page":"5018","DOI":"10.1128\/MCB.21.15.5018-5030.2001","article-title":"Tight binding of the phosphorylated \u03b1 subunit of initiation factor 2 (eIF2\u03b1) 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":"10.1074\/jbc.M113.518191_bib51","doi-asserted-by":"crossref","first-page":"12929","DOI":"10.1021\/bi0008682","article-title":"Phosphorylation of serine 51 in initiation factor 2 \u03b1 (eIF2 \u03b1) promotes complex formation between eIF2 \u03b1(P) and eIF2B and causes inhibition in the guanine nucleotide exchange activity of eIF2B","volume":"39","author":"Sudhakar","year":"2000","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.M113.518191_bib52","doi-asserted-by":"crossref","first-page":"3499","DOI":"10.1091\/mbc.e12-05-0385","article-title":"Large G3BP-induced granules trigger eIF2\u03b1 phosphorylation","volume":"23","author":"Reineke","year":"2012","journal-title":"Mol. Biol. Cell"},{"key":"10.1074\/jbc.M113.518191_bib53","doi-asserted-by":"crossref","first-page":"5657","DOI":"10.1128\/jvi.65.11.5657-5662.1991","article-title":"Adenovirus virus-associated RNA and translation control","volume":"65","author":"Mathews","year":"1991","journal-title":"J. Virol"},{"key":"10.1074\/jbc.M113.518191_bib54","doi-asserted-by":"crossref","first-page":"543","DOI":"10.1016\/0092-8674(82)90310-5","article-title":"Adenovirus VAI RNA is required for efficient translation of viral mRNAs at late times after infection","volume":"31","author":"Thimmappaya","year":"1982","journal-title":"Cell"},{"key":"10.1074\/jbc.M113.518191_bib55","doi-asserted-by":"crossref","first-page":"37993","DOI":"10.1074\/jbc.M004762200","article-title":"PACT, a stress-modulated cellular activator of interferon-induced double-stranded RNA-activated protein kinase, PKR","volume":"275","author":"Patel","year":"2000","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M113.518191_bib56","doi-asserted-by":"crossref","first-page":"4379","DOI":"10.1093\/emboj\/17.15.4379","article-title":"Pact, a protein activator of the interferon-induced protein kinase, PKR","volume":"17","author":"Patel","year":"1998","journal-title":"EMBO J"},{"key":"10.1074\/jbc.M113.518191_bib57","doi-asserted-by":"crossref","first-page":"320","DOI":"10.1038\/334320a0","article-title":"Internal initiation of translation of eukaryotic mRNA directed by a sequence derived from poliovirus RNA","volume":"334","author":"Pelletier","year":"1988","journal-title":"Nature"},{"key":"10.1074\/jbc.M113.518191_bib58","doi-asserted-by":"crossref","first-page":"8884","DOI":"10.1128\/JVI.00792-11","article-title":"Poliovirus switches to an eIF2-independent mode of translation during infection","volume":"85","author":"White","year":"2011","journal-title":"J. Virol"},{"key":"10.1074\/jbc.M113.518191_bib59","doi-asserted-by":"crossref","first-page":"611","DOI":"10.1093\/emboj\/16.3.611","article-title":"Oncogenic potential of TAR RNA binding protein TRBP and its regulatory interaction with RNA-dependent protein kinase PKR","volume":"16","author":"Benkirane","year":"1997","journal-title":"EMBO J"},{"key":"10.1074\/jbc.M113.518191_bib60","doi-asserted-by":"crossref","first-page":"254","DOI":"10.1128\/MCB.01030-08","article-title":"TRBP control of PACT-induced phosphorylation of protein kinase R is reversed by stress","volume":"29","author":"Daher","year":"2009","journal-title":"Mol. Cell. Biol"},{"key":"10.1074\/jbc.M113.518191_bib61","doi-asserted-by":"crossref","first-page":"15427","DOI":"10.1074\/jbc.274.22.15427","article-title":"RAX, a cellular activator for double-stranded RNA-dependent protein kinase during stress signaling","volume":"274","author":"Ito","year":"1999","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M113.518191_bib62","doi-asserted-by":"crossref","first-page":"821","DOI":"10.1182\/blood-2005-11-006817","article-title":"RAX, the PKR activator, sensitizes cells to inflammatory cytokines, serum withdrawal, chemotherapy, and viral infection","volume":"108","author":"Bennett","year":"2006","journal-title":"Blood"},{"key":"10.1074\/jbc.M113.518191_bib63","doi-asserted-by":"crossref","first-page":"457","DOI":"10.1016\/j.jmb.2008.10.068","article-title":"Essential role of PACT-mediated PKR activation in tunicamycin-induced apoptosis","volume":"385","author":"Singh","year":"2009","journal-title":"J. Mol. Biol"},{"key":"10.1074\/jbc.M113.518191_bib64","doi-asserted-by":"crossref","first-page":"4550","DOI":"10.1021\/bi200104h","article-title":"Stress-induced phosphorylation of PACT reduces its interaction with TRBP and leads to PKR activation","volume":"50","author":"Singh","year":"2011","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.M113.518191_bib65","doi-asserted-by":"crossref","first-page":"2839","DOI":"10.1074\/jbc.M112.401851","article-title":"Activation of double-stranded RNA-activated protein kinase (PKR) by interferon-stimulated gene 15 (ISG15) modification down-regulates protein translation","volume":"288","author":"Okumura","year":"2013","journal-title":"J. Biol. Chem"},{"key":"10.1074\/jbc.M113.518191_bib66","doi-asserted-by":"crossref","first-page":"180","DOI":"10.1006\/viro.1996.0364","article-title":"Characterization of the heparin-mediated activation of PKR, the interferon-inducible RNA-dependent protein kinase","volume":"221","author":"George","year":"1996","journal-title":"Virology"},{"key":"10.1074\/jbc.M113.518191_bib67","doi-asserted-by":"crossref","first-page":"973","DOI":"10.1016\/j.jmb.2011.09.025","article-title":"Heparin activates PKR by inducing dimerization","volume":"413","author":"Anderson","year":"2011","journal-title":"J. Mol. Biol"},{"key":"10.1074\/jbc.M113.518191_bib68","doi-asserted-by":"crossref","first-page":"76","DOI":"10.1016\/j.virusres.2005.10.016","article-title":"Translational control by viral proteinases","volume":"119","author":"Lloyd","year":"2006","journal-title":"Virus Res"}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S002192582044181X?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S002192582044181X?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1074\/jbc.M113.518191","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,3,20]],"date-time":"2025-03-20T19:27:27Z","timestamp":1742498847000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S002192582044181X"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2014,2]]},"references-count":68,"journal-issue":{"issue":"7","published-print":{"date-parts":[[2014,2]]}},"alternative-id":["S002192582044181X"],"URL":"https:\/\/doi.org\/10.1074\/jbc.m113.518191","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2014,2]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"mRNA Decapping Enzyme 1a (Dcp1a)-induced Translational Arrest through Protein Kinase R (PKR) Activation Requires the N-terminal Enabled Vasodilator-stimulated Protein Homology 1 (EVH1) Domain","name":"articletitle","label":"Article Title"},{"value":"Journal of Biological Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1074\/jbc.M113.518191","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2014 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.","name":"copyright","label":"Copyright"}]}}