ArticleBiochemistry2012
Structural and biochemical characterization of the childhood cataract-associated R76S mutant of human γD-crystallin.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 31 citations in OpenAlex.
- Human Crystallin Variation and Cataract.Investigative ophthalmology & visual science · 2026Review
- Oxidation of active cysteines mediates protein aggregation of S10R, the cataract-associated mutant of mouse GammaB-crystallin.Proteins · 2022Article
- Chemical Properties Determine Solubility and Stability in βγ-Crystallins of the Eye Lens.Chembiochem : a European journal of chemical biology · 2021Review
- Assessing the Structures and Interactions of γD-Crystallin Deamidation Variants.Structure (London, England : 1993) · 2021Article
- Cumulative deamidations of the major lens protein γS-crystallin increase its aggregation during unfolding and oxidation.Protein science : a publication of the Protein Society · 2020Article
- Divalent Cations and the Divergence ofBiochemistry · 2019Article
- High Expression Achievement of Active and Robust Anti-β2 microglobulin Nanobodies viaMolecules (Basel, Switzerland) · 2019Article
- A molecular dynamics approach to explore the structural characterization of cataract causing mutation R58H on human γD crystallin.Molecular and cellular biochemistry · 2018Article
- A Combined NMR and SAXS Analysis of the Partially Folded Cataract-Associated V75D γD-Crystallin.Biophysical journal · 2017Article
- Modeling phase transitions in mixtures of β-γ lens crystallins.Soft matter · 2016Article
- Nuclear Magnetic Resonance Structure of a Major Lens Protein, Human γC-Crystallin: Role of the Dipole Moment in Protein Solubility.Biochemistry · 2016Article
- Wild-type human γD-crystallin promotes aggregation of its oxidation-mimicking, misfolding-prone W42Q mutant.The Journal of biological chemistry · 2015Article
- Lens β-crystallins: the role of deamidation and related modifications in aging and cataract.Progress in biophysics and molecular biology · 2014Review
- Preferential and specific binding of human αB-crystallin to a cataract-related variant of γS-crystallin.Structure (London, England : 1993) · 2013Article
- Article
- The human W42R γD-crystallin mutant structure provides a link between congenital and age-related cataracts.The Journal of biological chemistry · 2013Article
- Structural integrity of the Greek key motif in βγ-crystallins is vital for central eye lens transparency.PloS one · 2013Article
- Structural analysis of the mutant protein D26G of human γS-crystallin, associated with Coppock cataract.Molecular vision · 2013Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 2 countries.
Funding
Abstract
Although a number of γD-crystallin mutations are associated with cataract formation, there is not a clear understanding of the molecular mechanism(s) that lead to this protein deposition disease. As part of our ongoing studies on crystallins, we investigated the recently discovered Arg76 to Ser (R76S) mutation that is correlated with childhood cataract in an Indian family. We expressed the R76S γD-crystallin protein in E. coli, characterized it by CD, fluorescence, and NMR spectroscopy, and determined its stability with respect to thermal and chemical denaturation. Surprisingly, no significant biochemical or biophysical differences were observed between the wild-type protein and the R76S variant, except a lowered pI (6.8 compared to the wild-type value of 7.4). NMR assessment of the R76S γD-crystallin solution structure, by RDCs, and of its motional properties, by relaxation measurements, also revealed a close resemblance to wild-type crystallin. Further, kinetic unfolding/refolding experiments for R76S and wild-type protein showed similar degrees of off-pathway aggregation suppression by αB-crystallin. Overall, our results suggest that neither structural nor stability changes in the protein are responsible for the R76S γD-crystallin variant's association with cataract. However, the change in pI and the associated surface charge or the altered nature of the amino acid could influence interactions with other lens protein species.
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