Chaperone Activity and Homo- and Hetero-oligomer Formation of Bacterial Small Heat Shock Proteins
Open Access
- 1 November 2000
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 275 (47) , 37212-37218
- https://doi.org/10.1074/jbc.m004701200
Abstract
No abstract availableKeywords
This publication has 36 references indexed in Scilit:
- Small heat shock proteins, IbpA and IbpB, are involved in resistances to heat and superoxide stresses inEscherichia coliFEMS Microbiology Letters, 2000
- Heterologous Expression of a Plant Small Heat-Shock Protein Enhances Escherichia coliViability under Heat and Cold Stress1Plant Physiology, 1999
- Crystal structure of a small heat-shock proteinNature, 1998
- Genealogy of the α-crystallin—small heat-shock protein superfamilyInternational Journal of Biological Macromolecules, 1998
- The small heat-shock protein, αb-crystallin, has a variable quaternary structureJournal of Molecular Biology, 1998
- Subunit Exchange of αA-CrystallinJournal of Biological Chemistry, 1997
- A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent stateThe EMBO Journal, 1997
- Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivationThe EMBO Journal, 1997
- Alpha-crystallin can function as a molecular chaperone.Proceedings of the National Academy of Sciences, 1992
- Four small Drosophila heat shock proteins are related to each other and to mammalian alpha-crystallin.Proceedings of the National Academy of Sciences, 1982