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Links from PubMed

Items: 8

1.

Minimalist aminoacylated RNAs as efficient substrates for elongation factor Tu.

Rudinger J, Blechschmidt B, Ribeiro S, Sprinzl M.

Biochemistry. 1994 May 17;33(19):5682-8.

PMID:
8180193
2.

The ternary complex of aminoacylated tRNA and EF-Tu-GTP. Recognition of a bond and a fold.

Nissen P, Kjeldgaard M, Thirup S, Clark BF, Nyborg J.

Biochimie. 1996;78(11-12):921-33. Review.

PMID:
9150869
3.

Structural features in aminoacyl-tRNAs required for recognition by elongation factor Tu.

Faulhammer HG, Joshi RL.

FEBS Lett. 1987 Jun 15;217(2):203-11. Review.

4.

The ternary complex of EF-Tu and its role in protein biosynthesis.

Clark BF, Nyborg J.

Curr Opin Struct Biol. 1997 Feb;7(1):110-6. Review.

PMID:
9032056
5.

T-armless tRNAs and elongated elongation factor Tu.

Ohtsuki T, Watanabe Y.

IUBMB Life. 2007 Feb;59(2):68-75. Review.

6.
7.

Possible evolution of factors involved in protein biosynthesis.

Nyborg J.

Acta Biochim Pol. 1998;45(4):883-94. Review.

8.

EFTu provides an internal kinetic standard for translational accuracy.

Thompson RC.

Trends Biochem Sci. 1988 Mar;13(3):91-3. Review. No abstract available.

PMID:
3072707

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