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Items: 1 to 20 of 187

2.

Structural basis of the water-assisted asparagine recognition by asparaginyl-tRNA synthetase.

Iwasaki W, Sekine S, Kuroishi C, Kuramitsu S, Shirouzu M, Yokoyama S.

J Mol Biol. 2006 Jul 7;360(2):329-42. Epub 2006 May 15.

PMID:
16753178
3.

Crystal structure of the archaeal asparagine synthetase: interrelation with aspartyl-tRNA and asparaginyl-tRNA synthetases.

Blaise M, Fréchin M, Oliéric V, Charron C, Sauter C, Lorber B, Roy H, Kern D.

J Mol Biol. 2011 Sep 23;412(3):437-52. doi: 10.1016/j.jmb.2011.07.050. Epub 2011 Jul 28.

PMID:
21820443
5.

The structural basis for seryl-adenylate and Ap4A synthesis by seryl-tRNA synthetase.

Belrhali H, Yaremchuk A, Tukalo M, Berthet-Colominas C, Rasmussen B, Bösecke P, Diat O, Cusack S.

Structure. 1995 Apr 15;3(4):341-52.

8.
10.

The 2.9 A crystal structure of T. thermophilus seryl-tRNA synthetase complexed with tRNA(Ser).

Biou V, Yaremchuk A, Tukalo M, Cusack S.

Science. 1994 Mar 11;263(5152):1404-10.

PMID:
8128220
11.

Aminoacyl-tRNA synthetases.

Cusack S.

Curr Opin Struct Biol. 1997 Dec;7(6):881-9. Review.

PMID:
9434910
12.

When contemporary aminoacyl-tRNA synthetases invent their cognate amino acid metabolism.

Roy H, Becker HD, Reinbolt J, Kern D.

Proc Natl Acad Sci U S A. 2003 Aug 19;100(17):9837-42. Epub 2003 Jul 21.

14.

tRNA(Pro) anticodon recognition by Thermus thermophilus prolyl-tRNA synthetase.

Cusack S, Yaremchuk A, Krikliviy I, Tukalo M.

Structure. 1998 Jan 15;6(1):101-8.

15.

Structural and functional analysis of Glutaminyl-tRNA synthetase (TtGlnRS) from Thermus thermophilus HB8 and its complexes.

Nachiappan M, Jain V, Sharma A, Yogavel M, Jeyakanthan J.

Int J Biol Macromol. 2018 Dec;120(Pt B):1379-1386. doi: 10.1016/j.ijbiomac.2018.09.115. Epub 2018 Sep 21.

PMID:
30248426
16.

Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.

Cusack S, Härtlein M, Leberman R.

Nucleic Acids Res. 1991 Jul 11;19(13):3489-98.

19.

Crystals of Thermus thermophilus tRNAAsp complexed with its cognate aspartyl-tRNA synthetase have a solvent content of 75%. Comparison with other aminoacylation systems.

Briand C, Poterszman A, Mitschler A, Yusupov M, Thierry JC, Moras D.

Acta Crystallogr D Biol Crystallogr. 1998 Nov 1;54(Pt 6 Pt 2):1382-6.

PMID:
10089514
20.

The crystal structure of phenylalanyl-tRNA synthetase from thermus thermophilus complexed with cognate tRNAPhe.

Goldgur Y, Mosyak L, Reshetnikova L, Ankilova V, Lavrik O, Khodyreva S, Safro M.

Structure. 1997 Jan 15;5(1):59-68.

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