Detection of key sites of dimer dissociation and unfolding initiation during activation of acid-stress chaperone HdeA at low pH-Reference-Cited by-同舟云学术

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Detection of key sites of dimer dissociation and unfolding initiation during activation of acid-stress chaperone HdeA at low pH

Published:2021-02 Issue:2 Volume:1869 Page:140576
ISSN:1570-9639
Container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

Author:

Widjaja Marlyn A.,Gomez Jafaeth S.,Benson Jonathon M.,Crowhurst Karin A.

Funder

National Science Foundation

National Institutes of Health

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Analytical Chemistry

Reference39 articles.

1. Characterizations of the interactions between Escherichia coli periplasmic chaperone HdeA and its native substrates during acid stress;Yu;Biochemistry,2017

2. Structural basis and mechanism of the unfolding-induced activation of HdeA, a bacterial acid response chaperone;Yu;J. Biol. Chem.,2019

3. Shigellosis;Niyogi;J. Microbiol.,2005

4. Periplasmic protein HdeA exhibits chaperone-like activity exclusively within stomach pH range by transforming into disordered conformation;Hong;J. Biol. Chem.,2005

5. Chaperone-dependent mechanisms for acid resistance in enteric bacteria;Hong;Trends Microbiol.,2012

Cited by 4 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. The Chaperone-Active State of HdeB at pH 4 Arises from Its Conformational Rearrangement and Enhanced Stability Instead of Surface Hydrophobicity;Biochemistry;2024-04-19

2. Structural Disorder in Chaperone Functions Probed by NMR;Biophysics of Molecular Chaperones;2023-11-01

3. Removal of disulfide from acid stress chaperone HdeA does not wholly eliminate structure or function at low pH;Biochemistry and Biophysics Reports;2021-09

4. Removal of disulfide from acid stress chaperone HdeA does not wholly eliminate structure or function at low pH;2021-01-18

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