Bleach Activates a Redox-Regulated Chaperone by Oxidative Protein Unfolding
- 14 November 2008
- journal article
- research article
- Published by Elsevier BV in Cell
- Vol. 135 (4), 691-701
- https://doi.org/10.1016/j.cell.2008.09.024
Abstract
No abstract availableKeywords
This publication has 39 references indexed in Scilit:
- Quantifying changes in the thiol redox proteome upon oxidative stress in vivoProceedings of the National Academy of Sciences of the United States of America, 2008
- Effects of Protein Oxidation on the Structure and Stability of Model Discoidal High-Density LipoproteinsBiochemistry, 2008
- The redox-switch domain of Hsp33 functions as dual stress sensorNature Structural & Molecular Biology, 2007
- Toothpicks, Serendipity and the Emergence of the Escherichia coli DnaK (Hsp70) and GroEL (Hsp60) Chaperone MachinesGenetics, 2006
- Severe Oxidative Stress Causes Inactivation of DnaK and Activation of the Redox-Regulated Chaperone Hsp33Molecular Cell, 2005
- Protein Thiol Modifications Visualized In VivoPLoS Biology, 2004
- Activation of the Redox-regulated Chaperone Hsp33 by Domain UnfoldingOnline Journal of Public Health Informatics, 2004
- Pathways of Oxidative DamageAnnual Review of Microbiology, 2003
- Hypochlorite-induced oxidation of amino acids, peptides and proteinsAmino Acids, 2003
- Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpBThe EMBO Journal, 1999