The 2.2 Å Crystal Structure of Hsp33
- 1 May 2001
- Vol. 9 (5), 367-375
- https://doi.org/10.1016/s0969-2126(01)00597-4
Abstract
No abstract availableThis publication has 24 references indexed in Scilit:
- Activation of the Redox-Regulated Molecular Chaperone Hsp33—A Two-Step MechanismStructure, 2001
- Redox Switch of Hsp33 Has a Novel Zinc-binding MotifJournal of Biological Chemistry, 2000
- Mass Spectrometry Unravels Disulfide Bond Formation as the Mechanism That Activates a Molecular ChaperoneJournal of Biological Chemistry, 2000
- Hsp26: a temperature-regulated chaperoneThe EMBO Journal, 1999
- The structural basis for the oriented assembly of a TBP/TFB/promoter complexProceedings of the National Academy of Sciences, 1999
- Chaperone Activity with a Redox SwitchCell, 1999
- Surprising similarities in structure comparisonCurrent Opinion in Structural Biology, 1996
- 3D domain swapping: A mechanism for oligomer assemblyProtein Science, 1995
- Protein Structure Comparison by Alignment of Distance MatricesJournal of Molecular Biology, 1993
- The Structure and Function of the Aspartic ProteinasesAnnual Review of Biophysics, 1990