Molecular Basis for Regulation of the Heat Shock Transcription Factor σ32 by the DnaK and DnaJ Chaperones
- 1 November 2008
- journal article
- research article
- Published by Elsevier BV in Molecular Cell
- Vol. 32 (3), 347-358
- https://doi.org/10.1016/j.molcel.2008.09.016
Abstract
No abstract availableKeywords
This publication has 53 references indexed in Scilit:
- Analysis of σ 32 mutants defective in chaperone-mediated feedback control reveals unexpected complexity of the heat shock responseProceedings of the National Academy of Sciences, 2007
- Disulfide cross-linking indicates that FlgM-bound and free σ 28 adopt similar conformationsProceedings of the National Academy of Sciences of the United States of America, 2006
- Investigation of the Interaction between DnaK and DnaJ by Surface Plasmon Resonance SpectroscopyJournal of Molecular Biology, 1999
- A Bipartite Signaling Mechanism Involved in DnaJ-mediated Activation of the Escherichia coli DnaK ProteinJournal of Biological Chemistry, 1996
- Regulatory Region C of theE. coliHeat Shock Transcription Factor, σ32, Constitutes a DnaK Binding Site and is Conserved Among EubacteriaJournal of Molecular Biology, 1996
- Structural Basis of Amino Acid α Helix PropensityScience, 1993
- α-Helix stability in proteinsJournal of Molecular Biology, 1992
- [6] Efficient site-directed mutagenesis using uracil-containing DNAMethods in enzymology, 1991
- A Thermodynamic Scale for the Helix-Forming Tendencies of the Commonly Occurring Amino AcidsScience, 1990
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970