Improving target amino acid selectivity in a permissive aminoacyl tRNA synthetase through counter-selection-Reference-Cited by-同舟云学术

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Improving target amino acid selectivity in a permissive aminoacyl tRNA synthetase through counter-selection

Published:2017 Issue:17 Volume:15 Page:3603-3610
ISSN:1477-0520
Container-title:Organic & Biomolecular Chemistry
language:en
Short-container-title:Org. Biomol. Chem.

Author:

Sungwienwong Itthipol¹²³⁴,Hostetler Zachary M.⁵⁶²³⁴,Blizzard Robert J.⁷⁸⁹⁴,Porter Joseph J.⁷⁸⁹⁴,Driggers Camden M.¹¹⁰¹¹⁴,Mbengi Lea Z.¹¹⁰¹¹⁴,Villegas José A.¹²³⁴,Speight Lee C.¹²³⁴,Saven Jeffery G.¹²³⁴,Perona John J.¹¹⁰¹¹⁴¹²,Kohli Rahul M.⁵⁶²³⁴,Mehl Ryan A.⁷⁸⁹⁴,Petersson E. James¹²³⁴^ORCID

Affiliation:

1. Department of Chemistry

2. University of Pennsylvania

3. Philadelphia

4. USA

5. Department of Medicine

6. Perelman School of Medicine

7. Oregon State University

8. Department of Biochemistry and Biophysics

9. Corvallis

10. Portland State University

11. Portland

12. Department of Biochemistry & Molecular Biology

Abstract

We report the selection and characterization of an improved acridon-2-ylalanine aminoacyl tRNA synthetase.

Funder

NIH Office of the Director

Division of Molecular and Cellular Biosciences

National Science Foundation

National Institutes of Health

Division of Chemistry

National Institute of General Medical Sciences

Publisher

Royal Society of Chemistry (RSC)

Subject

Organic Chemistry,Physical and Theoretical Chemistry,Biochemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2017/OB/C7OB00582B

Reference40 articles.

1. Calmodulin: a prototypical calcium sensor

2. Novel aspects of calmodulin target recognition and activation

3. The bacterial LexA transcriptional repressor

4. Targets for Combating the Evolution of Acquired Antibiotic Resistance

5. The many faces of α-synuclein: from structure and toxicity to therapeutic target

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