Bendazac prevents cyanate binding to soluble lens proteins and cyanate-induced phase-separation opacities in vitro: a possible mechanism by which bendazac could delay cataract
- 1 December 1986
- journal article
- research article
- Published by Elsevier in Experimental Eye Research
- Vol. 43 (6) , 973-979
- https://doi.org/10.1016/0014-4835(86)90075-8
Abstract
No abstract availableKeywords
This publication has 10 references indexed in Scilit:
- DO ASPIRIN-LIKE ANALGESICS PROTECT AGAINST CATARACT?: A Case-control StudyThe Lancet, 1986
- Effects of bendazac l-lysine salt on X-ray-induced cataract in the rabbit lensExperimental Eye Research, 1986
- Opacification of gamma-crystallin solutions from calf lens in relation to cold cataract formation.Proceedings of the National Academy of Sciences, 1985
- Aspirin prevents carbamylation of soluble lens proteins and prevents cyanate-induced phase separation opacities in vitro: A possible mechanism by which aspirin could prevent cataractExperimental Eye Research, 1985
- Conformational changes induced in bovine lens α-crystallin by carbamylation. Relevance to cataractBiochemical Journal, 1984
- DEHYDRATIONAL CRISES FROM SEVERE DIARRHOEA OR HEATSTROKE AND RISK OF CATARACTThe Lancet, 1984
- BASIC DATA SUPPORTING THE USE OF THE L-LYSINE SALT OF BENDAZAC IN CATARACT1983
- PILOT STUDY OF BENDAZAC FOR TREATMENT OF CATARACTThe Lancet, 1982
- Carbamylation of lens proteins: A possible factor in cataractogenesis in some tropical countriesExperimental Eye Research, 1980
- Cytoplasmic phase separation in formation of galactosemic cataract in lenses of young ratsProceedings of the National Academy of Sciences, 1979