Organization of the multiaminoacyl-tRNA synthetase complex and the cotranslational protein folding-Reference-Cited by-同舟云学术

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Organization of the multiaminoacyl-tRNA synthetase complex and the cotranslational protein folding

Published:2015-07-14 Issue:9 Volume:24 Page:1475-1485
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Berezovsky Igor N.¹²,Zheng Zejun¹,Kurotani Atsushi³,Tokmakov Alexander A.⁴,Kurochkin Igor V.¹

Affiliation:

1. Bioinformatics Institute (BII); Agency for Science, Technology and Research (a*STAR); Singapore 138671

2. Department of Biological Sciences (DBS); National University of Singapore (NUS); Singapore 117579

3. RIKEN Center for Sustainable Resource Science (CSRS); Yokohama Kanagawa 230-0045 Japan

4. Research Center for Environmental Genomics; Kobe University; Kobe Japan

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/pro.2735/fullpdf

Reference74 articles.

1. Functional expansion of aminoacyl-tRNA synthetases and their interacting factors: new perspectives on housekeepers;Park;Trends Biochem Sci,2005

2. p38 is essential for the assembly and stability of macromolecular tRNA synthetase complex: implications for its physiological significance;Kim;Proc Natl Acad Sci USA,2002

3. Dynamic organization of aminoacyl-tRNA synthetase complexes in the cytoplasm of human cells;Kaminska;J Biol Chem,2009

4. RNA binding targets aminoacyl-tRNA synthetases to translating ribosomes;David;J Biol Chem,2011

5. Existence of two forms of rat liver arginyl-tRNA synthetase suggests channeling of aminoacyl-tRNA for protein synthesis;Sivaram;Proc Natl Acad Sci USA,1990

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1. Human lysyl-tRNA synthetase evolves a dynamic structure that can be stabilized by forming complex;Cellular and Molecular Life Sciences;2022-02

2. Basic units of protein structure, folding, and function;Progress in Biophysics and Molecular Biology;2017-09

3. Protein function machinery: from basic structural units to modulation of activity;Current Opinion in Structural Biology;2017-02

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