Crystal structure of heat shock protein 15 (Hsp15) from Vibrio cholerae: Novel mode of trimerization and nucleic acid binding properties-Reference-Cited by-同舟云学术

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Crystal structure of heat shock protein 15 (Hsp15) from Vibrio cholerae: Novel mode of trimerization and nucleic acid binding properties

Published:2018-03 Issue:4 Volume:497 Page:1076-1081
ISSN:0006-291X
Container-title:Biochemical and Biophysical Research Communications
language:en
Short-container-title:Biochemical and Biophysical Research Communications

Author:

Chowdhury Sanghati Roy,Sen Udayaditya

Funder

DAE

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference20 articles.

1. The effect of molecular chaperones on in vivo and in vitro folding processes;Schwarz;Biol. Chem. Hoppe Seyler,1996

2. Escherichia Coli and Salmonella: Cellular and Molecular Biology;Neidhardt,1996

3. Hsp15: a ribosome-associated heat shock protein;Korber;EMBO J.,2000

4. Recycling of aborted ribosomal 50S subunit-nascent Chain-tRNA complexes by the heat shock protein Hsp15;Jiang;J. Mol. Biol.,2009

5. Recycling of aborted ribosomal 50S subunit-nascent Chain-tRNA complexes by the heat shock protein Hsp15;Jiang;J. Mol. Biol.,2009

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