Design of an Active Fragment of a Class II Aminoacyl-tRNA Synthetase and Its Significance for Synthetase Evolution-Reference-Cited by-同舟云学术

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Design of an Active Fragment of a Class II Aminoacyl-tRNA Synthetase and Its Significance for Synthetase Evolution

Published:1997-03-01 Issue:12 Volume:36 Page:3473-3482
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Augustine John¹,Francklyn Christopher¹

Affiliation:

1. Department of Biochemistry, University of Vermont College of Medicine, Health Sciences Complex, Burlington, Vermont 05405

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi962395y

Reference61 articles.

1. Crystal structure of histidyl-tRNA synthetase from Escherichia coli complexed with histidyl-adenylate.

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1. Biochemistry of Aminoacyl tRNA Synthetase and tRNAs and Their Engineering for Cell-Free and Synthetic Cell Applications;Frontiers in Bioengineering and Biotechnology;2022-07-01

2. The evolutionary history of class I aminoacyl-tRNA synthetases indicates early statistical translation;2022-06-11

3. Rational Design of Aptamer-Tagged tRNAs;International Journal of Molecular Sciences;2020-10-21

4. Chimeric design of pyrrolysyl-tRNA synthetase/tRNA pairs and canonical synthetase/tRNA pairs for genetic code expansion;Nature Communications;2020-06-22

5. Aminoacyl-tRNA synthetases;RNA;2020-04-17

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