ArticleFEBS letters2012
Cataract-linked γD-crystallin mutants have weak affinity to lens chaperones α-crystallins.
Article in FEBS letters, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
13 citing papers in PubMed, 20 citations in OpenAlex.
- Zebrafish as a model for crystallin-associated congenital cataracts in humans.Frontiers in cell and developmental biology · 2025Review
- Article
- α-Crystallins in the Vertebrate Eye Lens: Complex Oligomers and Molecular Chaperones.Annual review of physical chemistry · 2021Review
- Proteinaceous Transformers: Structural and Functional Variability of Human sHsps.International journal of molecular sciences · 2020Review
- Human αB-crystallin discriminates between aggregation-prone and function-preserving variants of a client protein.Biochimica et biophysica acta. General subjects · 2020Article
- Transgenic zebrafish models reveal distinct molecular mechanisms for cataract-linked αA-crystallin mutants.PloS one · 2018Article
- RNA aptamers targeted for human αA-crystallin do not bind αB-crystallin, and spare the α-crystallin domain.Biochemical and biophysical research communications · 2017Article
- A Combined NMR and SAXS Analysis of the Partially Folded Cataract-Associated V75D γD-Crystallin.Biophysical journal · 2017Article
- Expression of Cataract-linked γ-Crystallin Variants in Zebrafish Reveals a Proteostasis Network That Senses Protein Stability.The Journal of biological chemistry · 2016Article
- Species-Specific Structural and Functional Divergence of α-Crystallins: Zebrafish αBa- and Rodent αA(ins)-Crystallin Encode Activated Chaperones.Biochemistry · 2015Article
- A conserved role of αA-crystallin in the development of the zebrafish embryonic lens.Experimental eye research · 2015Article
- Degradation of an old human protein: age-dependent cleavage of γS-crystallin generates a peptide that binds to cell membranes.The Journal of biological chemistry · 2012Article
- Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
To test the hypothesis that α-crystallin chaperone activity plays a central role in maintenance of lens transparency, we investigated its interactions with γ-crystallin mutants that cause congenital cataract in mouse models. Although the two substitutions, I4F and V76D, stabilize a partially unfolded γD-crystallin intermediate, their affinities to α-crystallin are marginal even at relatively high concentrations. Detectable binding required further reduction of γD-crystallin stability which was achieved by combining the two mutations. Our results demonstrate that mutants and possibly age-damaged γ-crystallin can escape quality control by lens chaperones rationalizing the observation that they nucleate protein aggregation and lead to cataract.
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Registered trials
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