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The 5'-7-methylguanosine cap on eukaryotic mRNAs serves both to stimulate canonical translation initiation and to block an alternative pathway.

Mitchell SF, Walker SE, Algire MA, Park EH, Hinnebusch AG, Lorsch JR.

Mol Cell. 2010 Sep 24;39(6):950-62. doi: 10.1016/j.molcel.2010.08.021.


Specific domains in yeast translation initiation factor eIF4G strongly bias RNA unwinding activity of the eIF4F complex toward duplexes with 5'-overhangs.

Rajagopal V, Park EH, Hinnebusch AG, Lorsch JR.

J Biol Chem. 2012 Jun 8;287(24):20301-12. doi: 10.1074/jbc.M112.347278. Epub 2012 Mar 30.


Human eukaryotic initiation factor 4G (eIF4G) protein binds to eIF3c, -d, and -e to promote mRNA recruitment to the ribosome.

Villa N, Do A, Hershey JW, Fraser CS.

J Biol Chem. 2013 Nov 15;288(46):32932-40. doi: 10.1074/jbc.M113.517011. Epub 2013 Oct 3.


Yeast eIF4B binds to the head of the 40S ribosomal subunit and promotes mRNA recruitment through its N-terminal and internal repeat domains.

Walker SE, Zhou F, Mitchell SF, Larson VS, Valasek L, Hinnebusch AG, Lorsch JR.

RNA. 2013 Feb;19(2):191-207. doi: 10.1261/rna.035881.112. Epub 2012 Dec 12.


The nematode eukaryotic translation initiation factor 4E/G complex works with a trans-spliced leader stem-loop to enable efficient translation of trimethylguanosine-capped RNAs.

Wallace A, Filbin ME, Veo B, McFarland C, Stepinski J, Jankowska-Anyszka M, Darzynkiewicz E, Davis RE.

Mol Cell Biol. 2010 Apr;30(8):1958-70. doi: 10.1128/MCB.01437-09. Epub 2010 Feb 12.


The eukaryotic initiation factor (eIF) 4G HEAT domain promotes translation re-initiation in yeast both dependent on and independent of eIF4A mRNA helicase.

Watanabe R, Murai MJ, Singh CR, Fox S, Ii M, Asano K.

J Biol Chem. 2010 Jul 16;285(29):21922-33. doi: 10.1074/jbc.M110.132027. Epub 2010 May 12.


Cap-dependent eukaryotic initiation factor-mRNA interactions probed by cross-linking.

Lindqvist L, Imataka H, Pelletier J.

RNA. 2008 May;14(5):960-9. doi: 10.1261/rna.971208. Epub 2008 Mar 26.


RNA aptamers to mammalian initiation factor 4G inhibit cap-dependent translation by blocking the formation of initiation factor complexes.

Miyakawa S, Oguro A, Ohtsu T, Imataka H, Sonenberg N, Nakamura Y.

RNA. 2006 Oct;12(10):1825-34. Epub 2006 Aug 29.


Novel insights into the architecture and protein interaction network of yeast eIF3.

Khoshnevis S, Hauer F, Milón P, Stark H, Ficner R.

RNA. 2012 Dec;18(12):2306-19. doi: 10.1261/rna.032532.112. Epub 2012 Oct 26.


Small ribosomal protein RPS0 stimulates translation initiation by mediating 40S-binding of eIF3 via its direct contact with the eIF3a/TIF32 subunit.

Kouba T, Dányi I, Gunišová S, Munzarová V, Vlčková V, Cuchalová L, Neueder A, Milkereit P, Valášek LS.

PLoS One. 2012;7(7):e40464. doi: 10.1371/journal.pone.0040464. Epub 2012 Jul 5.


Dynamic recognition of the mRNA cap by Saccharomyces cerevisiae eIF4E.

O'Leary SE, Petrov A, Chen J, Puglisi JD.

Structure. 2013 Dec 3;21(12):2197-207. doi: 10.1016/j.str.2013.09.016. Epub 2013 Oct 31.


Identification and characterization of functionally critical, conserved motifs in the internal repeats and N-terminal domain of yeast translation initiation factor 4B (yeIF4B).

Zhou F, Walker SE, Mitchell SF, Lorsch JR, Hinnebusch AG.

J Biol Chem. 2014 Jan 17;289(3):1704-22. doi: 10.1074/jbc.M113.529370. Epub 2013 Nov 27. Erratum in: J Biol Chem. 2014 Apr 25;289(17):11860.


Repressor binding to a dorsal regulatory site traps human eIF4E in a high cap-affinity state.

Ptushkina M, von der Haar T, Karim MM, Hughes JM, McCarthy JE.

EMBO J. 1999 Jul 15;18(14):4068-75.


β-Hairpin loop of eukaryotic initiation factor 1 (eIF1) mediates 40 S ribosome binding to regulate initiator tRNA(Met) recruitment and accuracy of AUG selection in vivo.

Martin-Marcos P, Nanda J, Luna RE, Wagner G, Lorsch JR, Hinnebusch AG.

J Biol Chem. 2013 Sep 20;288(38):27546-62. doi: 10.1074/jbc.M113.498642. Epub 2013 Jul 26.


Cap-independent translation is required for starvation-induced differentiation in yeast.

Gilbert WV, Zhou K, Butler TK, Doudna JA.

Science. 2007 Aug 31;317(5842):1224-7.

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