ArticleFrontiers in molecular biosciences2022
Cataract-Causing S93R Mutant Destabilized Structural Conformation of βB1 Crystallin Linking With Aggregates Formation and Cellular Viability.
Article in Frontiers in molecular biosciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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2 citing papers in PubMed, 7 citations in OpenAlex.
- Oxidative Stress and Cataract Formation: Evaluating the Efficacy of Antioxidant Therapies.Biomolecules · 2024Review
- Grand Challenges and Opportunities in Surgical Ophthalmology: Together for a Shared Future.Frontiers in ophthalmology · 2022Article
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10 authors at 4 institutions in 1 country.
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Abstract
Cataract, opacity of the eye lens, is the leading cause of visual impairment worldwide. The crucial pathogenic factors that cause cataract are misfolding and aggregation of crystallin protein. βB1-crystallin, which is the most abundant water-soluble protein in mammalian lens, is essential for lens transparency. A previous study identified the missense mutation βB1-S93R being responsible for congenital cataract. However, the exact pathogenic mechanism causing cataract remains unclear. The S93 residue, which is located at the first Greek-key motif of βB1-crystallin, is highly conserved, and its substitution to Arginine severely impaired hydrogen bonds and structural conformation, which were evaluated
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