ArticlePloS one2015
Glycation of H1 Histone by 3-Deoxyglucosone: Effects on Protein Structure and Generation of Different Advanced Glycation End Products.
Article in PloS one, 2015. 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
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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.
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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
25 citing papers in PubMed, 66 citations in OpenAlex.
- Salubrious effects ofFood & nutrition research · 2026Article
- Double Peptide-Functionalized Carboxymethyl Chitosan-Coated Liposomes Loaded with Dexamethasone as a Potential Strategy for Active Targeting Drug Delivery.International journal of molecular sciences · 2025Article
- Synthesis, Characterization, Antiglycation Evaluation, Molecular Docking, and ADMET Studies of 4-Thiazolidinone Derivatives.ACS omega · 2024Article
- The AGE-RAGE Axis and the Pathophysiology of Multimorbidity in COPD.Journal of clinical medicine · 2023Review
- Leveraging histone glycation for cancer diagnostics and therapeutics.Trends in cancer · 2023Review
- Nutriepigenomics in Environmental-Associated Oxidative Stress.Antioxidants (Basel, Switzerland) · 2023Review
- Green tea catechin-grafted silk fibroin hydrogels with reactive oxygen species scavenging activity for wound healing applications.Biomaterials research · 2022Article
- Dietary Advanced Glycation End Products Shift the Gut Microbiota Composition and Induce Insulin Resistance in Mice.Diabetes, metabolic syndrome and obesity : targets and therapy · 2022Article
- The Expanding Constellation of Histone Post-Translational Modifications in the Epigenetic Landscape.Genes · 2021Review
- Role of Advanced Glycation End-Products and Other Ligands for AGE Receptors in Thyroid Cancer Progression.Journal of clinical medicine · 2021Review
- Non-enzymatic Covalent Modifications as a New Chapter in the Histone Code.Trends in biochemical sciences · 2021Review
- The roles of inducible chromatin and transcriptional memory in cellular defense system responses to redox-active pollutants.Free radical biology & medicine · 2021Review
- Effect of methylglyoxal on the alteration in structure and digestibility of α-lactalbumin, and the formation of advanced glycation end products under simulated thermal processing.Food science & nutrition · 2021Article
- Advances in Nutritional Epigenetics-A Fresh Perspective for an Old Idea. Lessons Learned, Limitations, and Future Directions.Epigenetics insights · 2020Article
- Modulated Protein Binding Ability of Anti-Diabetic Drugs in Presence of Monodispersed Gold Nanoparticles and its Inhibitory Potential towards Advanced Glycated End (AGE) Product Formation.Journal of fluorescence · 2020Article
- Oxidative, Reductive, and Nitrosative Stress Effects on Epigenetics and on Posttranslational Modification of Enzymes in Cardiometabolic Diseases.Oxidative medicine and cellular longevity · 2020Review
- Pathological Mechanisms Linking Diabetes Mellitus and Alzheimer's Disease: the Receptor for Advanced Glycation End Products (RAGE).Frontiers in aging neuroscience · 2020Article
- High Dietary Advanced Glycation End Products Impair Mitochondrial and Cognitive Function.Journal of Alzheimer's disease : JAD · 2020Article
- Aging and cancer: Is glucose a mediator between them?Oncotarget · 2019Article
- Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Advanced glycation end products (AGEs) culminate from the non-enzymatic reaction between a free carbonyl group of a reducing sugar and free amino group of proteins. 3-deoxyglucosone (3-DG) is one of the dicarbonyl species that rapidly forms several protein-AGE complexes that are believed to be involved in the pathogenesis of several diseases, particularly diabetic complications. In this study, the generation of AGEs (Nε-carboxymethyl lysine and pentosidine) by 3-DG in H1 histone protein was characterized by evaluating extent of side chain modification (lysine and arginine) and formation of Amadori products as well as carbonyl contents using several physicochemical techniques. Results strongly suggested that 3-DG is a potent glycating agent that forms various intermediates and AGEs during glycation reactions and affects the secondary structure of the H1 protein. Structural changes and AGE formation may influence the function of H1 histone and compromise chromatin structures in cases of secondary diabetic complications.
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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.