Protection of enzymes by α-crystallin acting as a molecular chaperone
- 1 May 1998
- journal article
- review article
- Published by Elsevier in International Journal of Biological Macromolecules
- Vol. 22 (3-4), 295-306
- https://doi.org/10.1016/s0141-8130(98)00027-0
Abstract
No abstract availableKeywords
This publication has 54 references indexed in Scilit:
- Inactivation of glucose-6-phosphate dehydrogenase by glycationBiochemical Society Transactions, 1994
- Glycation (non-enzymic glycosylation) inactivates glutathione reductaseBiochemical Journal, 1992
- Alpha-crystallin can function as a molecular chaperone.Proceedings of the National Academy of Sciences, 1992
- Immunoreactive αA crystallin in rat non-lenticular tissues detected with a sensitive immunoassay methodBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1991
- Cellular distribution of alpha B-crystallin in non-lenticular tissues.Journal of Histochemistry & Cytochemistry, 1990
- αB-crystallin is expressed in non-lenticular tissues and accumulates in Alexander's disease brainCell, 1989
- αB subunit of lens-specific protein α-crystallin is present in other ocular and non-ocular tissuesBiochemical and Biophysical Research Communications, 1989
- High-molecular-weight crystallin aggregate formation resulting from non-enzymic carbamylation of lens crystallins: Relevance to cataract formationExperimental Eye Research, 1987
- Conformational changes induced in lens α- and γ-crystallins by modification with glucose 6-phosphate. Implications for cataractBiochemical Journal, 1987
- Four small Drosophila heat shock proteins are related to each other and to mammalian alpha-crystallin.Proceedings of the National Academy of Sciences, 1982