ArticleProtein science : a publication of the Protein Society2013
Age-dependent racemization of serine residues in a human chaperone protein.
Article in Protein science : a publication of the Protein Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 49 citations in OpenAlex.
- Deep Characterization of Isomerization in the Human Eye Lens Proteome by Crystallin-Depleted Data-Independent Acquisition.Aging cell · 2025Article
- Stability of Protein Pharmaceuticals: Recent Advances.Pharmaceutical research · 2024Review
- Localizing Isomerized Residue Sites in Peptides with Tandem Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2024Article
- Article
- Insights into the biochemical and biophysical mechanisms mediating the longevity of the transparent optics of the eye lens.The Journal of biological chemistry · 2022Review
- Predicting Reaction Mechanisms for the Threonine-Residue Stereoinversion Catalyzed by a Dihydrogen Phosphate Ion.ACS omega · 2022Article
- PIMT-Mediated Labeling of l-Isoaspartic Acid with Tris Facilitates Identification of Isomerization Sites in Long-Lived Proteins.Journal of the American Society for Mass Spectrometry · 2022Article
- Fundamental Clock of Biological Aging: Convergence of Molecular, Neurodegenerative, Cognitive and Psychiatric Pathways: Non-Equilibrium Thermodynamics Meet Psychology.International journal of molecular sciences · 2021Review
- Tau Is Truncated in Five Regions of the Normal Adult Human Brain.International journal of molecular sciences · 2021Article
- Racemization in Post-Translational Modifications Relevance to Protein Aging, Aggregation and Neurodegeneration: Tip of the Iceberg.Symmetry · 2021Article
- Mechanisms of Deamidation of Asparagine Residues and Effects of Main-Chain Conformation on Activation Energy.International journal of molecular sciences · 2020Article
- Spatiotemporal changes in the human lens proteome: Critical insights into long-lived proteins.Progress in retinal and eye research · 2020Review
- Accelerated identification of serine racemase inhibitor from Centella asiatica.Scientific reports · 2020Article
- Structural and functional consequences of age-related isomerization in α-crystallins.The Journal of biological chemistry · 2019Article
- Differences in α-Crystallin isomerization reveal the activity of protein isoaspartyl methyltransferase (PIMT) in the nucleus and cortex of human lenses.Experimental eye research · 2018Article
- Metabolic characterization of human aqueous humor in the cataract progression after pars plana vitrectomy.BMC ophthalmology · 2018Article
- Isoaspartic acid is present at specific sites in myelin basic protein from multiple sclerosis patients: could this represent a trigger for disease onset?Acta neuropathologica communications · 2016Article
- Old Proteins in Man: A Field in its Infancy.Trends in biochemical sciences · 2016Review
- The etiology of human age-related cataract. Proteins don't last forever.Biochimica et biophysica acta · 2016Review
- Biophysical chemistry of the ageing eye lens.Biophysical reviews · 2015Review
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Authors and funding
3 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Racemization is one of the most abundant modifications in long-lived proteins. It has been proposed that the accumulation of such modifications over time could lead to changes in tissues and ultimately human age-related diseases. Serine is one of the main amino acids involved in racemization; however, the site of D-Ser in any aged protein has yet to be reported. In this study, racemization of two residues, Ser 59 and Ser 62, has been demonstrated in an unstructured region of the small heat shock protein, αA-crystallin. αA-crystallin is also the most abundant structural protein in the human lens. D-Ser increased linearly with age in normal lenses, until it accounted for approximately 35% of the Ser at both sites by the age of 75 years. In agreement with a possible role in human age-related disease, levels were significantly higher in cataract lenses. It is likely that such prevalent age-related changes contribute to the denaturation of α-crystallin, and therefore its ability to act as a chaperone. Racemization of amino acids, such as serine, in flexible regions of long-lived proteins, could be associated with the development of human age-related conditions such as cataract.
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