ArticleStructure (London, England : 1993)2022
Deamidation of the human eye lens protein γS-crystallin accelerates oxidative aging.
Article in Structure (London, England : 1993), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 31 citations in OpenAlex.
- Impact of Structural Flexibility on Tunneling Contribution to the Reaction Mechanism of Spontaneous Succinimide Formation in Asn-Gly-Containing Peptides.Biomolecules · 2026Article
- A Peptide-Based Strategy to Disrupt Oxidation-Induced Aggregation of γC-Crystallin Missense Mutant.JACS Au · 2026Article
- Dimerization of natively folded molecules drives misfolding and aggregation in Cys-depleted variants of cataract-associated human lens γD-crystallin.The Journal of biological chemistry · 2026Article
- Deamidation Promotes AGE-Modifications in Human Lens γS-Crystallin.Biochemistry · 2026Article
- Mimicking oxidative damage in γS-crystallin with site-specific incorporation of 5-hydroxytryptophan.Biophysical reports · 2026Article
- Lens aging and disease: Molecular mechanisms, functional consequences, and pharmacological implications.Progress in retinal and eye research · 2026Review
- Identification and functional characterization of a novel CRYBB1 deletion mutation causing autosomal dominant congenital cataract in a Chinese family.BMC ophthalmology · 2026Article
- Disulfide engineering reveals unexpected pro- and anti-aggregation conformers of human α-synuclein.bioRxiv : the preprint server for biology · 2026Article
- Key post-translational modifications of crystallin: from mechanism to target exploration for cataract diagnosis and treatment.Molecular biology reports · 2025Review
- Analysis of mouse lens morphological and proteomic abnormalities following deletion of the βB3-crystallin promoter.Experimental eye research · 2025Article
- Asparagine Deamidation Attenuates Toxicity, Aggregation, and Microglial Responses of Alzheimer's Amyloid-β.ACS chemical neuroscience · 2025Article
- Isomerized and Racemized Aspartyl and Deamidated Asparagine Residues Identified in ɣS-Crystallin.Chembiochem : a European journal of chemical biology · 2025Article
- Lens Proteomics Provide Novel Clues for Cataractogenesis: Original Investigation and a Broad Literature Survey.Journal of clinical medicine · 2025Article
- Identification of Age- and Cataract-Related Changes in High-Density Lens Protein Aggregates.Investigative ophthalmology & visual science · 2025Article
- Article
- The Eye Lens Protein, γS Crystallin, Undergoes Glutathionylation-Induced Disulfide Bonding Between Cysteines 22 and 26.Biomolecules · 2025Article
- Global maintenance of histone post-translational modifications during the transition into anoxia in embryos of the annual killifishEnvironmental epigenetics · 2025Article
- Systemic inflammatory and oxidative stress biomarkers as predictors of pain in sequential bilateral phacoemulsification for age-related cataract.Frontiers in medicine · 2025Article
- Characterization of the Interaction of Human γS Crystallin with Metal Ions and Its Effect on Protein Aggregation.Biomolecules · 2024Article
- Cumulative asparagine to aspartate deamidation fails to perturb γD-crystallin structure and stability.Protein science : a publication of the Protein Society · 2024Article
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Authors and funding
9 authors at 4 institutions in 3 countries.
Funding
Abstract
Cataract, a clouding of the eye lens from protein precipitation, affects millions of people every year. The lens proteins, the crystallins, show extensive post-translational modifications (PTMs) in cataractous lenses. The most common PTMs, deamidation and oxidation, promote crystallin aggregation; however, it is not clear precisely how these PTMs contribute to crystallin insolubilization. Here, we report six crystal structures of the lens protein γS-crystallin (γS): one of the wild-type and five of deamidated γS variants, from three to nine deamidation sites, after sample aging. The deamidation mutations do not change the overall fold of γS; however, increasing deamidation leads to accelerated disulfide-bond formation. Addition of deamidated sites progressively destabilized protein structure, and the deamidated variants display an increased propensity for aggregation. These results suggest that the deamidated variants are useful as models for accelerated aging; the structural changes observed provide support for redox activity of γS-crystallin in the lens.
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