ArticleExperimental eye research2019
The absence of SIRT3 and SIRT5 promotes the acetylation of lens proteins and improves the chaperone activity of α-crystallin in mouse lenses.
Article in Experimental eye research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
13 citing papers in PubMed, 18 citations in OpenAlex.
- Article
- Key post-translational modifications of crystallin: from mechanism to target exploration for cataract diagnosis and treatment.Molecular biology reports · 2025Review
- SIRT5: a potential target for discovering bioactive natural products.Journal of natural medicines · 2025Review
- Thiol-Mediated Enhancement of NACS chemical biology · 2024Article
- Neuronal SIRT3 Deletion Predisposes to Female-Specific Alterations in Cellular Metabolism, Memory, and Network Excitability.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2023Article
- Lysine Malonylation and Its Links to Metabolism and Diseases.Aging and disease · 2023Review
- Promotion of Protein Solubility and Reduction in Stiffness in Human Lenses by Aggrelyte-1: Implications for Reversing Presbyopia.International journal of molecular sciences · 2023Article
- Small Heat Shock Proteins in Retinal Diseases.Frontiers in molecular biosciences · 2022Review
- A functional map of genomic HIF1α-DNA complexes in the eye lens revealed through multiomics analysis.BMC genomics · 2021Article
- α-Crystallins in the Vertebrate Eye Lens: Complex Oligomers and Molecular Chaperones.Annual review of physical chemistry · 2021Review
- Glycation-mediated inter-protein cross-linking is promoted by chaperone-client complexes of α-crystallin: Implications for lens aging and presbyopia.The Journal of biological chemistry · 2020Article
- Aspirin inhibits TGFβ2-induced epithelial to mesenchymal transition of lens epithelial cells: selective acetylation of K56 and K122 in histone H3.The Biochemical journal · 2020Article
- Lysine malonylation and propionylation are prevalent in human lens proteins.Experimental eye research · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Acetylation of lysine residues occurs in lens proteins. Previous studies have shown an improvement in the chaperone activity of αA-crystallin upon acetylation. Sirtuins are NAD
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.