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Items: 1 to 20 of 109

1.

Misacylation of tRNA with methionine in Saccharomyces cerevisiae.

Wiltrout E, Goodenbour JM, Fréchin M, Pan T.

Nucleic Acids Res. 2012 Nov 1;40(20):10494-506. doi: 10.1093/nar/gks805. Epub 2012 Aug 31.

2.
3.

The yeast protein Arc1p binds to tRNA and functions as a cofactor for the methionyl- and glutamyl-tRNA synthetases.

Simos G, Segref A, Fasiolo F, Hellmuth K, Shevchenko A, Mann M, Hurt EC.

EMBO J. 1996 Oct 1;15(19):5437-48.

4.

Arc1p: anchoring, routing, coordinating.

Frechin M, Kern D, Martin RP, Becker HD, Senger B.

FEBS Lett. 2010 Jan 21;584(2):427-33. doi: 10.1016/j.febslet.2009.11.037. Review.

5.

Misacylation of specific nonmethionyl tRNAs by a bacterial methionyl-tRNA synthetase.

Jones TE, Alexander RW, Pan T.

Proc Natl Acad Sci U S A. 2011 Apr 26;108(17):6933-8. doi: 10.1073/pnas.1019033108. Epub 2011 Apr 11.

6.

The tRNA aminoacylation co-factor Arc1p is excluded from the nucleus by an Xpo1p-dependent mechanism.

Galani K, Hurt E, Simos G.

FEBS Lett. 2005 Feb 14;579(5):969-75. Epub 2005 Jan 18.

7.

Role of Arc1p in the modulation of yeast glutamyl-tRNA synthetase activity.

Graindorge JS, Senger B, Tritch D, Simos G, Fasiolo F.

Biochemistry. 2005 Feb 1;44(4):1344-52.

PMID:
15667228
8.

The intracellular location of two aminoacyl-tRNA synthetases depends on complex formation with Arc1p.

Galani K, Grosshans H, Deinert K, Hurt EC, Simos G.

EMBO J. 2001 Dec 3;20(23):6889-98.

9.

Quaternary structure of the yeast Arc1p-aminoacyl-tRNA synthetase complex in solution and its compaction upon binding of tRNAs.

Koehler C, Round A, Simader H, Suck D, Svergun D.

Nucleic Acids Res. 2013 Jan 7;41(1):667-76. doi: 10.1093/nar/gks1072. Epub 2012 Nov 17.

10.

Arc1p organizes the yeast aminoacyl-tRNA synthetase complex and stabilizes its interaction with the cognate tRNAs.

Deinert K, Fasiolo F, Hurt EC, Simos G.

J Biol Chem. 2001 Feb 23;276(8):6000-8. Epub 2000 Nov 7.

11.

Global tRNA misacylation induced by anaerobiosis and antibiotic exposure broadly increases stress resistance in Escherichia coli.

Schwartz MH, Waldbauer JR, Zhang L, Pan T.

Nucleic Acids Res. 2016 Dec 1;44(21):10292-10303. Epub 2016 Sep 26.

12.

Incorporation of the Arc1p tRNA-binding domain to the catalytic core of MetRS can functionally replace the yeast Arc1p-MetRS complex.

Karanasios E, Boleti H, Simos G.

J Mol Biol. 2008 Sep 5;381(3):763-71. doi: 10.1016/j.jmb.2008.06.044. Epub 2008 Jun 21.

PMID:
18598703
13.

Molecular determinants of the yeast Arc1p-aminoacyl-tRNA synthetase complex assembly.

Karanasios E, Simader H, Panayotou G, Suck D, Simos G.

J Mol Biol. 2007 Dec 7;374(4):1077-90. Epub 2007 Oct 11.

PMID:
17976650
14.

Structural basis of yeast aminoacyl-tRNA synthetase complex formation revealed by crystal structures of two binary sub-complexes.

Simader H, Hothorn M, Köhler C, Basquin J, Simos G, Suck D.

Nucleic Acids Res. 2006;34(14):3968-79. Epub 2006 Aug 12.

15.

Identification of the tRNA-binding protein Arc1p as a novel target of in vivo biotinylation in Saccharomyces cerevisiae.

Kim HS, Hoja U, Stolz J, Sauer G, Schweizer E.

J Biol Chem. 2004 Oct 8;279(41):42445-52. Epub 2004 Jul 22.

16.

Modulating the Structure and Function of an Aminoacyl-tRNA Synthetase Cofactor by Biotinylation.

Chang CY, Chang CP, Chakraborty S, Wang SW, Tseng YK, Wang CC.

J Biol Chem. 2016 Aug 12;291(33):17102-11. doi: 10.1074/jbc.M116.734343. Epub 2016 Jun 21.

17.
18.

Adaptation to tRNA acceptor stem structure by flexible adjustment in the catalytic domain of class I tRNA synthetases.

Liu C, Sanders JM, Pascal JM, Hou YM.

RNA. 2012 Feb;18(2):213-21. doi: 10.1261/rna.029983.111. Epub 2011 Dec 19.

19.

Position of aminoacylation of individual Escherichia coli and yeast tRNAs.

Hecht SM, Chinualt AC.

Proc Natl Acad Sci U S A. 1976 Feb;73(2):405-9.

20.

Arginine-395 is required for efficient in vivo and in vitro aminoacylation of tRNAs by Escherichia coli methionyl-tRNA synthetase.

Ghosh G, Kim HY, Demaret JP, Brunie S, Schulman LH.

Biochemistry. 1991 Dec 24;30(51):11767-74.

PMID:
1751493

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