A biologically active 53 kDa fragment of overproduced alanyl-tRNA synthetase from Thermus thermophilus HB8 specifically interacts with tRNA Ala acceptor helix-Reference-Cited by-同舟云学术

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A biologically active 53 kDa fragment of overproduced alanyl-tRNA synthetase from Thermus thermophilus HB8 specifically interacts with tRNA Ala acceptor helix

Published:1997-07-15 Issue:14 Volume:25 Page:2737-2744
ISSN:1362-4962
Container-title:Nucleic Acids Research
language:
Short-container-title:

Author:

Lechler A

Publisher

Oxford University Press (OUP)

Subject

Genetics

Link

http://academic.oup.com/nar/article-pdf/25/14/2737/4180578/25-14-2737.pdf

Cited by 15 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Application of solid-phase DNA probe method with cleavage by deoxyribozyme for analysis of long non-coding RNAs;The Journal of Biochemistry;2020-05-03

2. Reconstitution of translation from Thermus thermophilus reveals a minimal set of components sufficient for protein synthesis at high temperatures and functional conservation of modern and ancient translation components;Nucleic Acids Research;2012-06-21

3. Allosteric Interaction of Nucleotides and tRNAala with E. coli Alanyl-tRNA Synthetase;Biochemistry;2011-10-19

4. Tryptophanyl-tRNA Synthetase Urzyme;Journal of Biological Chemistry;2010-12

5. Alanyl-tRNA Synthetase Crystal Structure and Design for Acceptor-Stem Recognition;Molecular Cell;2004-03

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