Fort CnoX: Protecting Bacterial Proteins From Misfolding and Oxidative Damage
Published 2021 View Full Article
- Home
- Publications
- Publication Search
- Publication Details
Title
Fort CnoX: Protecting Bacterial Proteins From Misfolding and Oxidative Damage
Authors
Keywords
-
Journal
Frontiers in Molecular Biosciences
Volume 8, Issue -, Pages -
Publisher
Frontiers Media SA
Online
2021-05-04
DOI
10.3389/fmolb.2021.681932
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- CnoX Is a Chaperedoxin: A Holdase that Protects Its Substrates from Irreversible Oxidation
- (2018) Camille V. Goemans et al. MOLECULAR CELL
- Myeloperoxidase targets oxidative host attacks to Salmonella and prevents collateral tissue damage
- (2017) Nura Schürmann et al. Nature Microbiology
- Protein unfolding as a switch from self-recognition to high-affinity client binding
- (2016) Bastian Groitl et al. Nature Communications
- Polyphosphate Is a Primordial Chaperone
- (2014) Michael J. Gray et al. MOLECULAR CELL
- Activation of RidA chaperone function by N-chlorination
- (2014) Alexandra Müller et al. Nature Communications
- Sulfenic acid chemistry, detection and cellular lifetime
- (2013) Vinayak Gupta et al. BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS
- NemR Is a Bleach-sensing Transcription Factor
- (2013) Michael J. Gray et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- What really happens in the neutrophil phagosome?
- (2012) James K. Hurst FREE RADICAL BIOLOGY AND MEDICINE
- DnaK Functions as a Central Hub in the E. coli Chaperone Network
- (2012) Giulia Calloni et al. Cell Reports
- DNA replication defects in a mutant deficient in the thioredoxin homolog YbbN
- (2011) Hai-Tuong Le et al. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
- Escherichia coliThioredoxin-like Protein YbbN Contains an Atypical Tetratricopeptide Repeat Motif and Is a Negative Regulator of GroEL
- (2011) Jiusheng Lin et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Structure, Function, and Mechanism of Thioredoxin Proteins
- (2010) Jean-Francois Collet et al. ANTIOXIDANTS & REDOX SIGNALING
- Versatile TPR domains accommodate different modes of target protein recognition and function
- (2010) Rudi Kenneth Allan et al. CELL STRESS & CHAPERONES
- The thioredoxin homolog YbbN functions as a chaperone rather than as an oxidoreductase
- (2008) Fatoum Kthiri et al. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
- Bleach Activates a Redox-Regulated Chaperone by Oxidative Protein Unfolding
- (2008) J. Winter et al. CELL
Become a Peeref-certified reviewer
The Peeref Institute provides free reviewer training that teaches the core competencies of the academic peer review process.
Get StartedAsk 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