A new mechanism of post-transfer editing by aminoacyl-tRNA synthetases: catalysis of hydrolytic reaction by bacterial-type prolyl-tRNA synthetase-Reference-Cited by-同舟云学术

A new mechanism of post-transfer editing by aminoacyl-tRNA synthetases: catalysis of hydrolytic reaction by bacterial-type prolyl-tRNA synthetase

Published:2016-03-08 Issue:3 Volume:35 Page:669-682
ISSN:0739-1102
Container-title:Journal of Biomolecular Structure and Dynamics
language:en
Short-container-title:Journal of Biomolecular Structure and Dynamics

Author:

Boyarshin Konstantin S.¹²,Priss Anastasia E.²,Rayevskiy Alexsey V.¹²,Ilchenko Mykola M.³,Dubey Igor Ya.³,Kriklivyi Ivan A.¹²,Yaremchuk Anna D.¹²,Tukalo Michael A.¹²

Affiliation:

1. Department of Protein Synthesis Enzymology, Institute of Molecular Biology and Genetics, National Academy of Sciences of Ukraine, 150 Zabolotnogo Str, 03680 Kyiv, Ukraine

2. State Key Laboratory of Molecular and Cellular Biology, Institute of Molecular Biology and Genetics, National Academy of Sciences of Ukraine, 150 Zabolotnogo Str, 03680 Kyiv, Ukraine

3. Department of Synthetic Bioregulators, Institute of Molecular Biology and Genetics, National Academy of Sciences of Ukraine, 150 Zabolotnogo Str, 03680 Kyiv, Ukraine

Funder

Ukrainian Fund for Fundamental Studies

Publisher

Informa UK Limited

Subject

Molecular Biology,General Medicine,Structural Biology

Link

https://www.tandfonline.com/doi/pdf/10.1080/07391102.2016.1155171

Reference42 articles.

1. The strength of the 3′-gauche effect dictates the structure of 3′-O-anthraniloyladenosine and its 5′-phosphate, two analogues of the 3′-end of aminoacyl-tRNA

2. Unexpected edge conduction in mercury telluride quantum wells under broken time-reversal symmetry

3. The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling