Folding and Domain Interactions of Three Orthologs of Hsp90 Studied by Single-Molecule Force Spectroscopy-Reference-Cited by-同舟云学术

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Folding and Domain Interactions of Three Orthologs of Hsp90 Studied by Single-Molecule Force Spectroscopy

Published:2018-01 Issue:1 Volume:26 Page:96-105.e4
ISSN:0969-2126
Container-title:Structure
language:en
Short-container-title:Structure

Author:

Jahn Markus,Tych Katarzyna,Girstmair Hannah,Steinmaßl Maximilian,Hugel Thorsten,Buchner Johannes,Rief Matthias

Funder

German Research Foundation

HFSP

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference62 articles.

1. Contour length and refolding rate of a small protein controlled by engineered disulfide bonds;Ainavarapu;Biophys. J.,2007

2. Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex;Ali;Nature,2006

3. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs;Altschul;Nucleic Acids Res.,1997

4. Basic local alignment search tool;Altschul;J. Mol. Biol.,1990

5. Ancient heat shock gene is dispensable;Bardwell;J. Bacteriol.,1988

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