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Items: 1 to 20 of 388

1.

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
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.

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.

5.

A conserved domain within Arc1p delivers tRNA to aminoacyl-tRNA synthetases.

Simos G, Sauer A, Fasiolo F, Hurt EC.

Mol Cell. 1998 Jan;1(2):235-42.

6.
7.

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.

8.

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
9.

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
10.

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.

11.

A C-truncated glutamyl-tRNA synthetase specific for tRNA(Glu) is stimulated by its free complementary distal domain: mechanistic and evolutionary implications.

Dubois DY, Blais SP, Huot JL, Lapointe J.

Biochemistry. 2009 Jun 30;48(25):6012-21. doi: 10.1021/bi801690f. Erratum in: Biochemistry. 2009 Aug 4;48(30):7352.

PMID:
19496540
12.

Structures of the interacting domains from yeast glutamyl-tRNA synthetase and tRNA-aminoacylation and nuclear-export cofactor Arc1p reveal a novel function for an old fold.

Simader H, Hothorn M, Suck D.

Acta Crystallogr D Biol Crystallogr. 2006 Dec;62(Pt 12):1510-9. Epub 2006 Nov 23.

PMID:
17139087
13.

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.

14.

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.

15.

Arc1p is required for cytoplasmic confinement of synthetases and tRNA.

Golinelli-Cohen MP, Mirande M.

Mol Cell Biochem. 2007 Jun;300(1-2):47-59. Epub 2006 Nov 25.

PMID:
17131041
16.

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.

17.

Glutamyl-tRNA sythetase.

Freist W, Gauss DH, Söll D, Lapointe J.

Biol Chem. 1997 Nov;378(11):1313-29. Review.

PMID:
9426192
18.

Kinetic and mechanistic characterization of Mycobacterium tuberculosis glutamyl-tRNA synthetase and determination of its oligomeric structure in solution.

Paravisi S, Fumagalli G, Riva M, Morandi P, Morosi R, Konarev PV, Petoukhov MV, Bernier S, Chênevert R, Svergun DI, Curti B, Vanoni MA.

FEBS J. 2009 Mar;276(5):1398-417. doi: 10.1111/j.1742-4658.2009.06880.x.

19.

A 2-thiouridine derivative in tRNAGlu is a positive determinant for aminoacylation by Escherichia coli glutamyl-tRNA synthetase.

Sylvers LA, Rogers KC, Shimizu M, Ohtsuka E, Söll D.

Biochemistry. 1993 Apr 20;32(15):3836-41.

PMID:
8385989
20.

tRNAGlu increases the affinity of glutamyl-tRNA synthetase for its inhibitor glutamyl-sulfamoyl-adenosine, an analogue of the aminoacylation reaction intermediate glutamyl-AMP: mechanistic and evolutionary implications.

Blais SP, Kornblatt JA, Barbeau X, Bonnaure G, Lagüe P, Chênevert R, Lapointe J.

PLoS One. 2015 Apr 10;10(4):e0121043. doi: 10.1371/journal.pone.0121043. eCollection 2015. Erratum in: PLoS One. 2015;10(6):e0130238.

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