Carnosine inhibits modifications and decreased molecular chaperone activity of lens alpha-crystallin induced by ribose and fructose 6-phosphate.

Abstract

PURPOSE Alpha-crystallin, a major structural protein in the lens, prevents heat- and oxidative stress-induced aggregation of proteins and inactivation of enzymes by acting as a molecular chaperone. Modification of alpha-crystallin by some posttranslational modifications results in conformational changes and decreases in chaperone activity, which may… (More)

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Cite this paper

@article{Yan2006CarnosineIM, title={Carnosine inhibits modifications and decreased molecular chaperone activity of lens alpha-crystallin induced by ribose and fructose 6-phosphate.}, author={Hong Yan and John J. Harding}, journal={Molecular vision}, year={2006}, volume={12}, pages={205-14} }