ArticleJournal of cellular and molecular medicine2018
Racemization at the Asp 58 residue in αA-crystallin from the lens of high myopic cataract patients.
Article in Journal of cellular and molecular medicine, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 23 citations in OpenAlex.
- 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
- Application of Analytical Techniques to Chiral Amino Acid Profiling in Clinical Samples: Bridging Chemistry and Disease Research.Chirality · 2026Review
- Dimerization of natively folded molecules drives misfolding and aggregation in Cys-depleted variants of cataract-associated human lens γD-crystallin.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
- TGF-β1-induced m6A modifications accelerate onset of nuclear cataract in high myopia by modulating the PCP pathway.Nature communications · 2025Article
- Breaking Barriers: Nanomedicine-Based Drug Delivery for Cataract Treatment.International journal of nanomedicine · 2024Review
- Variable fragmentation and ionization of amyloid-beta epimers and isomers.Analytical and bioanalytical chemistry · 2023Article
- Oxidative Stress in the Anterior Ocular Diseases: Diagnostic and Treatment.Biomedicines · 2023Review
- Arrow of Time, Entropy, and Protein Folding: Holistic View on Biochirality.International journal of molecular sciences · 2022Review
- D-Amino Acids and D-Amino Acid-Containing Peptides: Potential Disease Biomarkers and Therapeutic Targets?Biomolecules · 2021Review
- Article
- The l-isoaspartate modification within protein fragments in the aging lens can promote protein aggregation.The Journal of biological chemistry · 2019Article
- Complications of high myopia: An update from clinical manifestations to underlying mechanisms.Advances in ophthalmology practice and researchReview
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Post-translational modifications in lens proteins are key causal factors in cataract. As the most abundant post-translational modification in the lens, racemization may be closely related to the pathogenesis of cataract. Racemization of αA-crystallin, a crucial structural and heat shock protein in the human lens, could significantly influence its structure and function. In previous studies, elevated racemization from l-Asp 58 to d-isoAsp58 in αA-crystallin has been found in age-related cataract (ARC) lenses compared to normal aged human lenses. However, the role of racemization in high myopic cataract (HMC), which is characterized by an early onset of nuclear cataract, remains unknown. In the current study, apparently different from ARC, significantly increased racemization from l-Asp 58 to d-Asp 58 in αA-crystallin was identified in HMC lenses. The average racemization rates for each Asp isoform were calculated in ARC and HMC group. In ARC patients, the conversion of l-Asp 58 to d-isoAsp 58, up to 31.89%, accounted for the main proportion in racemization, which was in accordance with the previous studies. However, in HMC lenses, the conversion of l-Asp 58 to d-Asp 58, as high as 35.44%, accounted for the largest proportion of racemization in αA-crystallin. The different trend in the conversion of αA-crystallin by racemization, especially the elevated level of d-Asp 58 in HMC lenses, might prompt early cataractogenesis and a possible explanation of distinct phenotypes of cataract in HMC.
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