ArticleBiomolecular NMR assignments2012
¹H, ¹³C, and ¹⁵N assignments of wild-type human γS-crystallin and its cataract-related variant γS-G18V.
Article in Biomolecular NMR assignments, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Mimicking oxidative damage in γS-crystallin with site-specific incorporation of 5-hydroxytryptophan.Biophysical reports · 2026Article
- Mini-αA-crystallin protects a client lens protein from catastrophic aggregation due to heat stress.Protein science : a publication of the Protein Society · 2025Article
- The Eye Lens Protein, γS Crystallin, Undergoes Glutathionylation-Induced Disulfide Bonding Between Cysteines 22 and 26.Biomolecules · 2025Article
- Characterization of the Interaction of Human γS Crystallin with Metal Ions and Its Effect on Protein Aggregation.Biomolecules · 2024Article
- A simple vapor-diffusion method enables protein crystallization inside the HARE serial crystallography chip.Acta crystallographica. Section D, Structural biology · 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
- 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
- Human αB-crystallin discriminates between aggregation-prone and function-preserving variants of a client protein.Biochimica et biophysica acta. General subjects · 2020Article
- Divalent Cations and the Divergence ofBiochemistry · 2019Article
- Altered Protein Dynamics and Increased Aggregation of Human γS-Crystallin Due to Cataract-Associated Deamidations.Biochemistry · 2019Article
- Multiple Aggregation Pathways in Human γS-Crystallin and Its Aggregation-Prone G18V Variant.Investigative ophthalmology & visual science · 2017Article
- Calcium Binding Dramatically Stabilizes an Ancestral Crystallin Fold in Tunicate βγ-Crystallin.Biochemistry · 2016Article
- Stability of Protein-Specific Hydration Shell on Crowding.Journal of the American Chemical Society · 2016Article
- Structural study of the G57W mutant of human gamma-S-crystallin, associated with congenital cataract.Molecular vision · 2016Article
- The cataract-associated V41M mutant of human γS-crystallin shows specific structural changes that directly enhance local surface hydrophobicity.Biochemical and biophysical research communications · 2014Article
- Preferential and specific binding of human αB-crystallin to a cataract-related variant of γS-crystallin.Structure (London, England : 1993) · 2013Article
- Exploring the aggregation propensity of γS-crystallin protein variants using two-dimensional spectroscopic tools.The journal of physical chemistry. B · 2013Article
- Structural analysis of the mutant protein D26G of human γS-crystallin, associated with Coppock cataract.Molecular vision · 2013Article
- The mutation V42M distorts the compact packing of the human gamma-S-crystallin molecule, resulting in congenital cataract.PloS one · 2012Article
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Abstract
We present the backbone and sidechain NMR assignments and a structural analysis of the 178-residue wild-type γS-crystallin and the cataract-related point mutant, γS-G18V. γS-crystallin is a structural component of the eye lens, which maintains its solubility and stability over many years. NMR assignments and continued structural investigations of γS-crystallin and aggregation-prone variants will advance understanding of cataract formation.
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