Inhibition of camel lens ζ-crystallin/NADPH:quinone oxidoreductase by pyridoxal-5′-phosphate
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics,Structural Biology
Reference26 articles.
1. Identification and characterization of enzymatic activity of ζ-crystallin from guinea pig lens. A novel NADPH:quinone oxidoreductase;Rao;J. Biol. Chem.,1992
2. ζ-Crystallin, novel lens protein from the guinea-pig;Huang;Curr. Eye Res.,1987
3. ζ-Crystallin is a major protein in the lens of Camelus dromedarius;Garland;Arch. Biochem. Biophys.,1991
4. Eye lens ζ-crystallin relationships to the family of ‘long chain’ alcohol/polyol dehydrogenases. Protein trimming and conservation of stable parts;Borras;Biochemistry,1989
5. Association of hereditary cataracts in strain 13/N guinea pigs with mutation of the gene of ζ-crystallin;Huang;Exp. Eye Res.,1990
Cited by 4 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
1. Inhibition of camel lens ζ-crystallin by aspirin and aspirin-like analgesics;The International Journal of Biochemistry & Cell Biology;2002-01
2. Transcriptional Responses in the Hemiparasitic PlantTriphysaria versicolor to Host Plant Signals,;Plant Physiology;2001-09-01
3. Hydrophobicity of the NADPH binding domain of camel lens ζ-crystallin;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;2001-03
4. NADPH:Quinone reductase;Springer Handbook of Enzymes
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