ArticleBiophysical journal2017
A Combined NMR and SAXS Analysis of the Partially Folded Cataract-Associated V75D γD-Crystallin.
Article in Biophysical journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 23 citations in OpenAlex.
- Information theory optimization of signals from small-angle scattering measurements.Biophysical journal · 2025Article
- Cataract-prone variants of γD-crystallin populate a conformation with a partially unfolded N-terminal domain under native conditions.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- A Single-Molecule Strategy to Capture Non-native Intramolecular and Intermolecular Protein Disulfide Bridges.Nano letters · 2022Article
- Quantitative Description of Intrinsically Disordered Proteins Using Single-Molecule FRET, NMR, and SAXS.Journal of the American Chemical Society · 2021Article
- The Proteome Folding Problem and Cellular Proteostasis.Journal of molecular biology · 2021Review
- 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
- Human γS-Crystallin-Copper Binding Helps Buffer against Aggregation Caused by Oxidative Damage.Biochemistry · 2020Article
- Function and Aggregation in Structural Eye Lens Crystallins.Accounts of chemical research · 2020Review
- Aggregation pathways of human γ D crystallin induced by metal ions revealed by time dependent methods.PeerJ · 2020Article
- Evolving SAXS versatility: solution X-ray scattering for macromolecular architecture, functional landscapes, and integrative structural biology.Current opinion in structural biology · 2019Review
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
A cataract is a pathological condition characterized by the clouding of the normally clear eye lens brought about by deposition of crystallin proteins in the lens fiber cells. These protein aggregates reduce visual acuity by scattering or blocking incoming light. Chemical damage to proteins of the crystallin family, accumulated over a lifetime, leads to age-related cataract, whereas inherited mutations are associated with congenital or early-onset cataract. The V75D mutant of γD-crystallin is associated with congenital cataract in mice and was previously shown to un/fold via a partially folded intermediate. Here, we structurally characterized the stable equilibrium urea unfolding intermediate of V75D at the ensemble level using solution NMR and small-angle x-ray scattering. Our data show that, in the intermediate, the C-terminal domain retains a folded conformation that is similar to the native wild-type protein, whereas the N-terminal domain is unfolded and comprises an ensemble of random conformers, without any detectable residual structural propensities.
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