ArticleBiochemistry2013
Acetylation of lysine 92 improves the chaperone and anti-apoptotic activities of human αB-crystallin.
Article in Biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
25 citing papers in PubMed, 38 citations in OpenAlex.
- Evaluation of protein profile in vitreous samples of patients with naive age-related macular degeneration using proteomic approaches.BMC geriatrics · 2025Article
- HuD and alpha-crystallin A axis protects neuro-retinal cells in early diabetes.Molecular and cellular biochemistry · 2025Article
- Thiol-Mediated Enhancement of NACS chemical biology · 2024Article
- Peptain-1 blocks ischemia/reperfusion-induced retinal capillary degeneration in mice.Frontiers in cellular neuroscience · 2024Article
- Article
- 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 minireview on the perturbation effects of polar groups to direct nanoscale hydrophobic interaction and amphiphilic peptide assembly.RSC advances · 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
- Lysine malonylation and propionylation are prevalent in human lens proteins.Experimental eye research · 2020Article
- The absence of SIRT3 and SIRT5 promotes the acetylation of lens proteins and improves the chaperone activity of α-crystallin in mouse lenses.Experimental eye research · 2019Article
- A monoclonal antibody targeted to the functional peptide of αB-crystallin inhibits the chaperone and anti-apoptotic activities.Journal of immunological methods · 2019Article
- Article
- Systemically administered peptain-1 inhibits retinal ganglion cell death in animal models: implications for neuroprotection in glaucoma.Cell death discovery · 2019Article
- Loss of αB-crystallin function in zebrafish reveals critical roles in the development of the lens and stress resistance of the heart.The Journal of biological chemistry · 2018Article
- Effect of Exogenous Alpha-B Crystallin on the Structures and Functions of Trabecular Meshwork Cells.Journal of ophthalmology · 2018Article
- αB-crystallin is essential for the TGF-β2-mediated epithelial to mesenchymal transition of lens epithelial cells.The Biochemical journal · 2016Article
- αB-crystallin: Portrait of a malignant chaperone as a cancer therapeutic target.Pharmacology & therapeutics · 2016Review
- Therapeutic potential of α-crystallin.Biochimica et biophysica acta · 2016Review
- Protective Effects of Acetylation on the Pathological Reactions of the Lens Crystallins with Homocysteine Thiolactone.PloS one · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 5 institutions in 3 countries.
Funding
Abstract
αB-Crystallin is a chaperone and an anti-apoptotic protein that is strongly expressed in many tissues, including the lens, retina, heart, and kidney. In the human lens, several lysine residues in αB-crystallin are acetylated. We have previously shown that such acetylation is predominant at lysine 92 (K92) and lysine 166 (K166). We have investigated the effect of lysine acetylation on the structure and functions of αB-crystallin by the specific introduction of an N(ε)-acetyllysine (AcK) mimic at K92. The introduction of AcK slightly altered the secondary and tertiary structures of the protein. The introduction of AcK also resulted in an increase in the molar mass and hydrodynamic radius of the protein, and the protein became structurally more open and more stable than the native protein. The acetyl protein acquired higher surface hydrophobicity and exhibited 25-55% higher chaperone activity than the native protein. The acetyl protein had more client protein binding per subunit of the protein and higher binding affinity relative to that of the native protein. The acetyl protein was at least 20% more effective in inhibiting chemically induced apoptosis than the native protein. Molecular modeling suggests that acetylation of K92 makes the "α-crystallin domain" more hydrophobic. Together, our results reveal that the acetylation of a single lysine residue in αB-crystallin makes the protein structurally more stable and improves its chaperone and anti-apoptotic activities. Our findings suggest that lysine acetylation of αB-crystallin is an important chemical modification for enhancing αB-crystallin's protective functions in the eye.
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.