ζ-Crystallin displays strong selectivity for salicylic acid over aspirin
- 26 April 2002
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 293 (1) , 440-445
- https://doi.org/10.1016/s0006-291x(02)00248-6
Abstract
No abstract availableKeywords
This publication has 30 references indexed in Scilit:
- High-affinity binding of NADPH to camel lens ζ-crystallinBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 2001
- The Reaction of Bovine Lens αA-Crystallin with AspirinExperimental Eye Research, 1993
- Mutant zeta-crystallin from guinea-pig hereditary cataracts has altered structural and enzymatic propertiesExperimental Eye Research, 1992
- Prevention of cataract in diabetic rats by aspirin, paracetamol (acetaminophen) and ibuprofenExperimental Eye Research, 1992
- ζ-Crystallin is a major protein in the lens of Camelus dromedariusArchives of Biochemistry and Biophysics, 1991
- The transcripts of zeta-crystallin, a lens protein related to the alcohol dehydrogenase family, are altered in a guinea-pig hereditary cataractExperimental Eye Research, 1990
- Association of hereditary cataracts in strain guinea-pigs with mutation of the gene for ζ-crystallinExperimental Eye Research, 1990
- Protection against cataract by aspirin, paracetamol and ibuprofenActa Ophthalmologica, 1989
- Eye lens .zeta.-crystallin relationships to the family of "long-chain" alcohol/polyol dehydrogenases. Protein trimming and conservation of stable partsBiochemistry, 1989
- Zeta-crystallin, a novel lens protein from the guinea pigCurrent Eye Research, 1987