Correlation between the Chaperone-like Activity and Aggregate Size of α-Crystallin with Increasing Temperature
- 1 February 2000
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 268 (2) , 426-432
- https://doi.org/10.1006/bbrc.1999.2036
Abstract
No abstract availableKeywords
This publication has 14 references indexed in Scilit:
- Evidence that α-crystallin prevents non-specific protein aggregation in the intact eye lensPublished by Elsevier ,1999
- Studies of the Denaturation Patterns of Bovine Alpha-Crystallin Using an Ionic Denaturant, Guanidine Hydrochloride and a Non-Ionic Denaturant, UreaExperimental Eye Research, 1998
- α-Crystallin: chaperoning and aggregationBiochemical Journal, 1994
- Characterization of the α-γ and α-β Complex: Evidence for an In Vivo Functional Role of α-Crystallin as a Molecular ChaperoneExperimental Eye Research, 1994
- Alpha-crystallin can function as a molecular chaperone.Proceedings of the National Academy of Sciences, 1992
- Tissue distribution and developmental profiles of immunoreactive αB crystallin in the rat determined with a sensitive immunoassay systemBiochimica et Biophysica Acta (BBA) - General Subjects, 1991
- Evolution of a protein superfamily: Relationships between vertebrate lens crystallins and microorganism dormancy proteinsJournal of Molecular Evolution, 1990
- αB subunit of lens-specific protein α-crystallin is present in other ocular and non-ocular tissuesBiochemical and Biophysical Research Communications, 1989
- Four small Drosophila heat shock proteins are related to each other and to mammalian alpha-crystallin.Proceedings of the National Academy of Sciences, 1982
- Effect of Light Scattering on Ultraviolet Difference Spectra1Journal of the American Chemical Society, 1960