A retroviral-like metal binding motif in an aminoacyl-tRNA synthetase is important for tRNA recognition.-Reference-Cited by-同舟云学术

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A retroviral-like metal binding motif in an aminoacyl-tRNA synthetase is important for tRNA recognition.

Published:1992-03-15 Issue:6 Volume:89 Page:2032-2035
ISSN:0027-8424
Container-title:Proceedings of the National Academy of Sciences
language:en
Short-container-title:Proceedings of the National Academy of Sciences

Author:

Miller W. T.,Schimmel P.

Publisher

Proceedings of the National Academy of Sciences

Subject

Multidisciplinary

Cited by 30 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. Dispensability of zinc and the putative zinc-binding domain in bacterial glutamyl-tRNA synthetase;Bioscience Reports;2015-03-31

2. Aminoacyl-tRNA Synthetases: Occurrence, Structure, and Function;tRNA;2014-04-30

3. Characterization of Zinc-Depleted Alanyl-tRNA Synthetase from Escherichia coli: Role of Zinc;Archives of Biochemistry and Biophysics;1999-08

4. Cysteine, glutathione (GSH) and zinc and copper ions together are effective, natural, intracellular inhibitors of (AIDS) viruses;Medical Hypotheses;1999-06

5. A biologically active 53 kDa fragment of overproduced alanyl-tRNA synthetase from Thermus thermophilus HB8 specifically interacts with tRNA Ala acceptor helix;Nucleic Acids Research;1997-07-15

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