Site-directed mutations within the core “α-crystallin” domain of the small heat-shock protein, human αB-crystallin, decrease molecular chaperone functions
- 4 June 1999
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 289 (2), 397-411
- https://doi.org/10.1006/jmbi.1999.2759
Abstract
No abstract availableKeywords
This publication has 48 references indexed in Scilit:
- 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
- Structure and Function of the Conserved Domain in αA-Crystallin. Site-Directed Spin Labeling Identifies a β-Strand Located near a Subunit InterfaceBiochemistry, 1997
- Modulation of the chaperone-like activity of bovine α-crystallinProceedings of the National Academy of Sciences, 1996
- Cloning, Expression, and Chaperone-like Activity of Human αA-CrystallinPublished by Elsevier ,1996
- Conformational Properties of Substrate Proteins Bound to a Molecular Chaperone α-CrystallinPublished by Elsevier ,1996
- 1H NMR spectroscopy reveals that mouse Hsp25 has a flexible C‐terminal extension of 18 amino acidsFEBS Letters, 1995
- The expanding small heat-shock protein family, and structure predictions of the conserved “α-crystallin domain”Journal of Molecular Evolution, 1995
- Identification by 1H NMR spectroscopy of flexible C‐terminal extensions in bovine lens α‐crystallinFEBS Letters, 1992
- The phosphorylation sites of the B2 chain of bovine α-crystallinBiochemical and Biophysical Research Communications, 1987