Inhibition of camel lens ζ-crystallin/NADPH:quinone oxidoreductase by pyridoxal-5′-phosphate

Author:

Rabbani Nayyar,Duhaiman Ali S.

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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