Interaction of Camel Lens ζ-Crystallin with Quinones: Portrait of a Substrate by Fluorescence Spectroscopy
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference28 articles.
1. Identification and characterization of the enzymatic activity of zeta-crystallin from guinea pig lens. A novel NADPH:quinone oxidoreductase.
2. Zeta-crystallin, a novel lens protein from the guinea pig
3. ζ-Crystallin is a major protein in the lens of Camelus dromedarius
4. The transcripts of zeta-crystallin, a lens protein related to the alcohol dehydrogenase family, are altered in a guinea-pig hereditary cataract
5. Structural and Sequence Comparisons of Quinone Oxidoreductase, ζ-Crystallin, and Glucose and Alcohol Dehydrogenases
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1. Assessing the inhibition of glycation of ζ-crystallin by thymoquinone: A mechanistic approach using experimental and computational methods;Journal of Molecular Liquids;2023-06
2. Elucidation of kinetic and structural properties of eye lens ζ-crystallin: an in vitro and in silico approach;Journal of Biomolecular Structure and Dynamics;2021-12-20
3. Protection of ζ-crystallin by α-crystallin under thermal stress;International Journal of Biological Macromolecules;2021-01
4. Structural stability and solubility of glycated camel lens ζ-crystallin;International Journal of Biological Macromolecules;2020-09
5. One pot synthesis of aminonaphthoquinone derivatives using Cu(II) immobilized on hyperbranched polyglycerol functionalized graphene oxide as a reusable catalyst under solvent-free conditions;Tetrahedron;2018-05
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