Wrapping the α-Crystallin Domain Fold in a Chaperone Assembly
- 1 October 2005
- journal article
- Published by Elsevier BV in Journal of Molecular Biology
- Vol. 353 (1), 68-79
- https://doi.org/10.1016/j.jmb.2005.08.025
Abstract
No abstract availableKeywords
This publication has 52 references indexed in Scilit:
- A Dual Role for the N-terminal Region of Mycobacterium tuberculosis Hsp16.3 in Self-oligomerization and Binding Denaturing Substrate ProteinsJournal of Biological Chemistry, 2005
- Tsp36, a tapeworm small heat‐shock protein with a duplicated α‐crystallin domain, forms dimers and tetramers with good chaperone‐like activityProteins-Structure Function and Bioinformatics, 2004
- Mutants in a Small Heat Shock Protein That Affect the Oligomeric StateJournal of Biological Chemistry, 2004
- Interaction of the Molecular Chaperone αB-Crystallin with α-Synuclein: Effects on Amyloid Fibril Formation and Chaperone ActivityJournal of Molecular Biology, 2004
- Shocking degenerationNature Genetics, 2004
- Desmin Aggregate Formation by R120G αB-Crystallin Is Caused by Altered Filament Interactions and Is Dependent upon Network Status in CellsMolecular Biology of the Cell, 2004
- Chaperone activity of cytosolic small heat shock proteins from wheatEuropean Journal of Biochemistry, 2004
- Chaperone Activity and Homo- and Hetero-oligomer Formation of Bacterial Small Heat Shock ProteinsJournal of Biological Chemistry, 2000
- XtalView/Xfit—A Versatile Program for Manipulating Atomic Coordinates and Electron DensityJournal of Structural Biology, 1999
- CORA—Topological fingerprints for protein structural familiesProtein Science, 1999