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Identification of eRF1 residues that play critical and complementary roles in stop codon recognition.

Conard SE, Buckley J, Dang M, Bedwell GJ, Carter RL, Khass M, Bedwell DM.

RNA. 2012 Jun;18(6):1210-21. doi: 10.1261/rna.031997.111.


Distinct eRF3 requirements suggest alternate eRF1 conformations mediate peptide release during eukaryotic translation termination.

Fan-Minogue H, Du M, Pisarev AV, Kallmeyer AK, Salas-Marco J, Keeling KM, Thompson SR, Pestova TV, Bedwell DM.

Mol Cell. 2008 Jun 6;30(5):599-609. doi: 10.1016/j.molcel.2008.03.020.


Stop codon recognition in ciliates: Euplotes release factor does not respond to reassigned UGA codon.

Kervestin S, Frolova L, Kisselev L, Jean-Jean O.

EMBO Rep. 2001 Aug;2(8):680-4.


Stop codon recognition in the early-diverged protozoans Giardia lamblia and Trichomonas vaginalis.

Chai B, Li C, Yu J, Hao Y, Guo P, Shen Q.

Mol Biochem Parasitol. 2015 Jul;202(1):15-21. doi: 10.1016/j.molbiopara.2015.08.004.


New insights into stop codon recognition by eRF1.

Blanchet S, Rowe M, Von der Haar T, Fabret C, Demais S, Howard MJ, Namy O.

Nucleic Acids Res. 2015 Mar 31;43(6):3298-308. doi: 10.1093/nar/gkv154.


Different modes of stop codon restriction by the Stylonychia and Paramecium eRF1 translation termination factors.

Lekomtsev S, Kolosov P, Bidou L, Frolova L, Rousset JP, Kisselev L.

Proc Natl Acad Sci U S A. 2007 Jun 26;104(26):10824-9.


[How translation termination factor eRF1 Euplotes does not recognise UGA stop codon].

Lekomtsev SA, Kolosov PM, Frolova LIu, Bidou L, Rousset JP, Kiselev LL.

Mol Biol (Mosk). 2007 Nov-Dec;41(6):1014-22. Russian.


A single amino acid substitution alters omnipotent eRF1 of Dileptus to euplotes-type dualpotent eRF1: standard codon usage may be advantageous in raptorial ciliates.

Li Y, Kim OT, Ito K, Saito K, Suzaki T, Harumoto T.

Protist. 2013 May;164(3):440-9. doi: 10.1016/j.protis.2013.02.004.


Class I release factors in ciliates with variant genetic codes.

Inagaki Y, Doolittle WF.

Nucleic Acids Res. 2001 Feb 15;29(4):921-7.


Terminating eukaryote translation: domain 1 of release factor eRF1 functions in stop codon recognition.

Bertram G, Bell HA, Ritchie DW, Fullerton G, Stansfield I.

RNA. 2000 Sep;6(9):1236-47.


A single amino acid change of translation termination factor eRF1 switches between bipotent and omnipotent stop-codon specificity.

Eliseev B, Kryuchkova P, Alkalaeva E, Frolova L.

Nucleic Acids Res. 2011 Jan;39(2):599-608. doi: 10.1093/nar/gkq759.


Convergence and constraint in eukaryotic release factor 1 (eRF1) domain 1: the evolution of stop codon specificity.

Inagaki Y, Blouin C, Doolittle WF, Roger AJ.

Nucleic Acids Res. 2002 Jan 15;30(2):532-44.


Two-step model of stop codon recognition by eukaryotic release factor eRF1.

Kryuchkova P, Grishin A, Eliseev B, Karyagina A, Frolova L, Alkalaeva E.

Nucleic Acids Res. 2013 Apr;41(8):4573-86. doi: 10.1093/nar/gkt113.


Three distinct peptides from the N domain of translation termination factor eRF1 surround stop codon in the ribosome.

Bulygin KN, Khairulina YS, Kolosov PM, Ven'yaminova AG, Graifer DM, Vorobjev YN, Frolova LY, Kisselev LL, Karpova GG.

RNA. 2010 Oct;16(10):1902-14. doi: 10.1261/rna.2066910.


Structural basis for stop codon recognition in eukaryotes.

Brown A, Shao S, Murray J, Hegde RS, Ramakrishnan V.

Nature. 2015 Aug 27;524(7566):493-6. doi: 10.1038/nature14896.


Identification of amino acids responsible for stop codon recognition for polypeptide chain release factor.

Xu L, Hao Y, Li C, Shen Q, Chai B, Wang W, Liang A.

Biochem Cell Biol. 2013 Jun;91(3):155-64. doi: 10.1139/bcb-2012-0091.


Decoding accuracy in eRF1 mutants and its correlation with pleiotropic quantitative traits in yeast.

Merritt GH, Naemi WR, Mugnier P, Webb HM, Tuite MF, von der Haar T.

Nucleic Acids Res. 2010 Sep;38(16):5479-92. doi: 10.1093/nar/gkq338.


Molecular mechanism of stop codon recognition by eRF1: a wobble hypothesis for peptide anticodons.

Muramatsu T, Heckmann K, Kitanaka C, Kuchino Y.

FEBS Lett. 2001 Jan 19;488(3):105-9.

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