Comparative proteomics reveal distinct chaperone–client interactions in supporting bacterial acid resistance
Published 2016 View Full Article
- Home
- Publications
- Publication Search
- Publication Details
Title
Comparative proteomics reveal distinct chaperone–client interactions in supporting bacterial acid resistance
Authors
Keywords
-
Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 113, Issue 39, Pages 10872-10877
Publisher
Proceedings of the National Academy of Sciences
Online
2016-09-13
DOI
10.1073/pnas.1606360113
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- Conditionally and Transiently Disordered Proteins: Awakening Cryptic Disorder To Regulate Protein Function
- (2014) Ursula Jakob et al. CHEMICAL REVIEWS
- HdeB Functions as an Acid-protective Chaperone in Bacteria
- (2014) Jan-Ulrik Dahl et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Genetically Encoded Cleavable Protein Photo-Cross-Linker
- (2014) Shixian Lin et al. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
- Chaperone activation by unfolding
- (2013) L. Foit et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- How bacteria survive an acid trip
- (2013) K. S. Hingorani et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Converting a Solvatochromic Fluorophore into a Protein-Based pH Indicator for Extreme Acidity
- (2012) Maiyun Yang et al. ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
- Genetic Analysis of 15 Protein Folding Factors and Proteases of the Escherichia coli Cell Envelope
- (2012) J. Weski et al. JOURNAL OF BACTERIOLOGY
- Comparative mitochondrial proteomics: perspective in human diseases
- (2012) Yujie Jiang et al. Journal of Hematology & Oncology
- Conditional disorder in chaperone action
- (2012) James C.A. Bardwell et al. TRENDS IN BIOCHEMICAL SCIENCES
- Chaperone-dependent mechanisms for acid resistance in enteric bacteria
- (2012) Weizhe Hong et al. TRENDS IN MICROBIOLOGY
- Evolutionary Silence of the Acid Chaperone Protein HdeB in Enterohemorrhagic Escherichia coli O157:H7
- (2011) Michelle Q. Carter et al. APPLIED AND ENVIRONMENTAL MICROBIOLOGY
- Salt Bridges Regulate Both Dimer Formation and Monomeric Flexibility in HdeB and May Have a Role in Periplasmic Chaperone Function
- (2011) Wenjian Wang et al. JOURNAL OF MOLECULAR BIOLOGY
- A genetically incorporated crosslinker reveals chaperone cooperation in acid resistance
- (2011) Meng Zhang et al. Nature Chemical Biology
- Acid stress response in enteropathogenic gammaproteobacteria: an aptitude for survivalThis paper is one of a selection of papers published in this special issue entitled “Canadian Society of Biochemistry, Molecular & Cellular Biology 52nd Annual Meeting — Protein Folding: Principles and Diseases” and has undergone the Journal's usual peer review process.
- (2010) Boyu Zhao et al. Biochemistry and Cell Biology
- Protein refolding by pH-triggered chaperone binding and release
- (2010) T. L. Tapley et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Differential substrate specificity of group I and group II chaperonins in the archaeonMethanosarcina mazei
- (2009) Angela M. Hirtreiter et al. MOLECULAR MICROBIOLOGY
- Structural plasticity of an acid-activated chaperone allows promiscuous substrate binding
- (2009) T. L. Tapley et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Conserved amphiphilic feature is essential for periplasmic chaperone HdeA to support acid resistance in enteric bacteria
- (2008) Ye E. Wu et al. BIOCHEMICAL JOURNAL
- Structural basis for the regulated protease and chaperone function of DegP
- (2008) Tobias Krojer et al. NATURE
- Tight Regulation of Unstructured Proteins: From Transcript Synthesis to Protein Degradation
- (2008) J. Gsponer et al. SCIENCE
Discover Peeref hubs
Discuss science. Find collaborators. Network.
Join a conversationAsk a Question. Answer a Question.
Quickly pose questions to the entire community. Debate answers and get clarity on the most important issues facing researchers.
Get Started