Subunit Exchange, Conformational Stability, and Chaperone-like Function of the Small Heat Shock Protein 16.5 fromMethanococcus jannaschii
Open Access
- 1 October 2002
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 277 (41) , 38468-38475
- https://doi.org/10.1074/jbc.m205594200
Abstract
No abstract availableKeywords
This publication has 41 references indexed in Scilit:
- α-Crystallin-Type Heat Shock Proteins: Socializing Minichaperones in the Context of a Multichaperone NetworkMicrobiology and Molecular Biology Reviews, 2002
- Small heat-shock protein structures reveal a continuum from symmetric to variable assembliesJournal of Molecular Biology, 2000
- Subunit Exchange of Small Heat Shock ProteinsJournal of Biological Chemistry, 2000
- Site-directed Spin Labeling Study of Subunit Interactions in the α-Crystallin Domain of Small Heat-shock ProteinsJournal of Biological Chemistry, 1999
- Identification of Protein Folding Patterns Using Site-Directed Spin Labeling. Structural Characterization of a β-Sheet and Putative Substrate Binding Regions in the Conserved Domain of αA-CrystallinBiochemistry, 1998
- Genealogy of the α-crystallin—small heat-shock protein superfamilyInternational Journal of Biological Macromolecules, 1998
- Intermolecular Exchange and Stabilization of Recombinant Human αA- and αB-CrystallinJournal of Biological Chemistry, 1998
- Subunit Exchange of αA-CrystallinJournal of Biological Chemistry, 1997
- Structure and Function of the Conserved Domain in αA-Crystallin. Site-Directed Spin Labeling Identifies a β-Strand Located near a Subunit InterfaceBiochemistry, 1997
- Methanococcus jannaschii sp. nov., an extremely thermophilic methanogen from a submarine hydrothermal ventArchiv für Mikrobiologie, 1983