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Cited In for PubMed (Select 8887689)


eIF2B is a decameric guanine nucleotide exchange factor with a γ2ε2 tetrameric core.

Gordiyenko Y, Schmidt C, Jennings MD, Matak-Vinkovic D, Pavitt GD, Robinson CV.

Nat Commun. 2014 May 23;5:3902. doi: 10.1038/ncomms4902.


Insights into the architecture of the eIF2Bα/β/δ regulatory subcomplex.

Bogorad AM, Xia B, Sandor DG, Mamonov AB, Cafarella TR, Jehle S, Vajda S, Kozakov D, Marintchev A.

Biochemistry. 2014 Jun 3;53(21):3432-45. doi: 10.1021/bi500346u. Epub 2014 May 20.


eIF2B promotes eIF5 dissociation from eIF2*GDP to facilitate guanine nucleotide exchange for translation initiation.

Jennings MD, Zhou Y, Mohammad-Qureshi SS, Bennett D, Pavitt GD.

Genes Dev. 2013 Dec 15;27(24):2696-707. doi: 10.1101/gad.231514.113.


Cytomegalovirus downregulates IRE1 to repress the unfolded protein response.

Stahl S, Burkhart JM, Hinte F, Tirosh B, Mohr H, Zahedi RP, Sickmann A, Ruzsics Z, Budt M, Brune W.

PLoS Pathog. 2013;9(8):e1003544. doi: 10.1371/journal.ppat.1003544. Epub 2013 Aug 8.


Identification of intersubunit domain interactions within eukaryotic initiation factor (eIF) 2B, the nucleotide exchange factor for translation initiation.

Reid PJ, Mohammad-Qureshi SS, Pavitt GD.

J Biol Chem. 2012 Mar 9;287(11):8275-85. doi: 10.1074/jbc.M111.331645. Epub 2012 Jan 11.


The alpha subunit of eukaryotic initiation factor 2B (eIF2B) is required for eIF2-mediated translational suppression of vesicular stomatitis virus.

Elsby R, Heiber JF, Reid P, Kimball SR, Pavitt GD, Barber GN.

J Virol. 2011 Oct;85(19):9716-25. doi: 10.1128/JVI.05146-11. Epub 2011 Jul 27.


The beta/Gcd7 subunit of eukaryotic translation initiation factor 2B (eIF2B), a guanine nucleotide exchange factor, is crucial for binding eIF2 in vivo.

Dev K, Qiu H, Dong J, Zhang F, Barthlme D, Hinnebusch AG.

Mol Cell Biol. 2010 Nov;30(21):5218-33. doi: 10.1128/MCB.00265-10. Epub 2010 Aug 30.


Fusel alcohols regulate translation initiation by inhibiting eIF2B to reduce ternary complex in a mechanism that may involve altering the integrity and dynamics of the eIF2B body.

Taylor EJ, Campbell SG, Griffiths CD, Reid PJ, Slaven JW, Harrison RJ, Sims PF, Pavitt GD, Delneri D, Ashe MP.

Mol Biol Cell. 2010 Jul 1;21(13):2202-16. doi: 10.1091/mbc.E09-11-0962. Epub 2010 May 5.


Archaeal aIF2B interacts with eukaryotic translation initiation factors eIF2alpha and eIF2Balpha: Implications for aIF2B function and eIF2B regulation.

Dev K, Santangelo TJ, Rothenburg S, Neculai D, Dey M, Sicheri F, Dever TE, Reeve JN, Hinnebusch AG.

J Mol Biol. 2009 Sep 25;392(3):701-22. doi: 10.1016/j.jmb.2009.07.030. Epub 2009 Jul 17.


Reduced eukaryotic initiation factor 2Bepsilon-subunit expression suppresses the transformed phenotype of cells overexpressing the protein.

Gallagher JW, Kubica N, Kimball SR, Jefferson LS.

Cancer Res. 2008 Nov 1;68(21):8752-60. doi: 10.1158/0008-5472.CAN-08-1042.


Minimum requirements for the function of eukaryotic translation initiation factor 2.

Erickson FL, Nika J, Rippel S, Hannig EM.

Genetics. 2001 May;158(1):123-32.


GCD14p, a repressor of GCN4 translation, cooperates with Gcd10p and Lhp1p in the maturation of initiator methionyl-tRNA in Saccharomyces cerevisiae.

Calvo O, Cuesta R, Anderson J, Gutiérrez N, García-Barrio MT, Hinnebusch AG, Tamame M.

Mol Cell Biol. 1999 Jun;19(6):4167-81.


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.

Asano K, Krishnamoorthy T, Phan L, Pavitt GD, Hinnebusch AG.

EMBO J. 1999 Mar 15;18(6):1673-88. Erratum in: EMBO J 1999 May 4;18(9):2670.

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