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REVIEW ARTICLE

Non-enzymatic glycation of proteins: Mechanisms and roles in biological aging and the pathogenesis of metabolic and neurodegenerative diseases

Agata Jabłońska-Trypuć1* ,  Maciej Gil1 ,  Adam Cudowski2
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1 Department of Chemistry, Biology, and Biotechnology, Faculty of Civil Engineering and Environmental Sciences, Bialystok University of Technology, Bialystok, Podlaskie, Poland
2 Department of Water Ecology, Faculty of Biology, University of Bialystok, Bialystok, Podlaskie, Poland
EJMO 2026, 10(2), 025510528 https://doi.org/10.36922/EJMO025510528
Received: 18 December 2025 | Revised: 21 February 2026 | Accepted: 30 March 2026 | Published online: 4 May 2026
© 2026 by the Author(s). This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution -Noncommercial 4.0 International License (CC-by the license) ( https://creativecommons.org/licenses/by-nc/4.0/ )
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Abstract

Global societies are currently facing a significant demographic challenge characterized by progressive aging and an increase in age-related pathological processes. One of the fundamental mechanisms underlying biological aging and the development of modern non-communicable diseases is the accumulation of harmful metabolic by-products. Particular importance is attributed to advanced glycation end products, which are formed through the non-enzymatic glycation of proteins. This process occurs when reducing sugars, primarily glucose, react with free primary amino groups of N-terminal amino acids or lysine residues. This chemical pathway, known as the Maillard reaction, results in the formation of permanent, pathological cross-links between proteins. These modifications not only alter individual protein structures but also significantly alter the physicochemical properties of the extracellular matrix, leading to tissue stiffness and loss of physiological function. Scientific evidence indicates that glycation plays a critical role in the pathogenesis of a wide spectrum of chronic conditions, including Alzheimer’s disease, atherosclerosis, diabetic nephropathy, heart failure, sarcopenia, and chronic lung diseases. Understanding the dynamics of these molecular interactions is essential for developing novel therapeutic strategies aimed at slowing down the aging process and mitigating metabolic complications in geriatric patients.

Keywords
Glycation
Protein
Biological aging
Carboxymethyllysine
Advanced glycation end products
Maillard reaction
Funding
This work was funded by the Ministry of Education and Science, Poland, under the research project number WZ/ WB-IIŚ/7/2025.
Conflict of interest
The authors declare they have no competing interests.
References
  1. Li Y, Tian X, Luo J, et al. Molecular mechanisms of aging and anti-aging strategies. Cell Commun Signal. 2024;22(1):285. doi: 10.1186/s12964-024-01663-1

 

  1. Trubitsyn AG. The Mechanism of Programmed Aging: The Way to Create a Real Remedy for Senescence. Curr Aging Sci. 2020;13(1):31-41. doi: 10.2174/1874609812666191014111422

 

  1. Kim CS, Park S, Kim J. The role of glycation in the pathogenesis of aging and its prevention through herbal products and physical exercise. J Exerc Nutr Biochem. 2017;21(3):55-61. doi: 10.20463/jenb.2017.0027

 

  1. Fournet M, Bonté F, Desmoulière A. Glycation Damage: A Possible Hub for Major Pathophysiological Disorders and Aging. Aging Dis. 2018;9(5):880. doi: 10.14336/AD.2017.1121

 

  1. Furrer R, Handschin C. Biomarkers of aging: from molecules and surrogates to physiology and function. Physiol Rev. 2025;105(3):1609-1694. doi: 10.1152/physrev.00045.2024

 

  1. Moreno DF, Jenkins K, Morlot S, et al. Proteostasis collapse, a hallmark of aging, hinders the chaperone-Start network and arrests cells in G1. eLife. 2019;8:e48240. doi: 10.7554/eLife.48240

 

  1. Saavedra D, Añé-Kourí AL, Barzilai N, et al. Aging and chronic inflammation: highlights from a multidisciplinary workshop. Immun Ageing. 2023;20(1):25. doi: 10.1186/s12979-023-00352-w

 

  1. Nan L, Guo P, Hui W, et al. Recent advances in dermal fibroblast senescence and skin aging: unraveling mechanisms and pioneering therapeutic strategies. Front Pharmacol. 2025;16:1592596. doi: 10.3389/fphar.2025.1592596

 

  1. Welsh KJ, Kirkman MS, Sacks DB. Role of Glycated Proteins in the Diagnosis and Management of Diabetes: Research Gaps and Future Directions. Diabetes Care. 2016;39(8):1299- 1306. doi: 10.2337/dc15-2727

 

  1. Uceda AB, Mariño L, Casasnovas R, et al. An overview on glycation: molecular mechanisms, impact on proteins, pathogenesis, and inhibition. Biophys Rev. 2024;16(2):189- 218. doi: 10.1007/s12551-024-01188-4

 

  1. Zgutka K, Tkacz M, Tomasiak P, et al. A Role for Advanced Glycation End Products in Molecular Ageing. Int J Mol Sci. 2023;24(12):9881. doi: 10.3390/ijms24129881

 

  1. Younus H, Anwar S. Prevention of non-enzymatic glycosylation (glycation): Implication in the treatment of diabetic complication. Int J Health Sci. 2016;10(2):261-277.

 

  1. Zhang Q, Ames JM, Smith RD, et al. A Perspective on the Maillard Reaction and the Analysis of Protein Glycation by Mass Spectrometry: Probing the Pathogenesis of Chronic Disease. J Proteome Res. 2009;8(2):754-769. doi: 10.1021/pr800858h

 

  1. Twarda-Clapa A, Olczak A, Białkowska AM, et al. Advanced Glycation End-Products (AGEs): Formation, Chemistry, Classification, Receptors, and Diseases Related to AGEs. Cells. 2022;11(8):1312. doi: 10.3390/cells11081312

 

  1. Sibbersen C, Johannsen M. Dicarbonyl derived post-translational modifications: chemistry bridging biology and aging-related disease. Essays Biochem. 2020;64(1):97-110. doi: 10.1042/EBC20190057

 

  1. Sarbacher CA, Halper JT. Connective Tissue and Age-Related Diseases. In: Harris JR, Korolchuk VI, eds. Biochemistry and Cell Biology of Ageing: Part II Clinical Science. Vol 91. Springer; 2019:281-310. doi: 10.1007/978-981-13-3681-2_11

 

  1. Birch HL. Extracellular Matrix and Ageing. In: Harris JR, Korolchuk VI, eds. Biochemistry and Cell Biology of Ageing: Part I Biomedical Science. Vol 90. Springer; 2018:169-190. doi: 10.1007/978-981-13-2835-0_7

 

  1. Goodarzi MT, Ghahraman S, Mirmomeni MH. In vitro Glycation of Human IgG and Its Effect on Interaction with Anti-IgG. Iran J Allergy Asthma Immunol. 2004;3(4):181- 187.

 

  1. Sirangelo I, Iannuzzi C. Understanding the Role of Protein Glycation in the Amyloid Aggregation Process. Int J Mol Sci. 2021;22(12):6609. doi: 10.3390/ijms22126609

 

  1. Stammers M, Ivanova IM, Niewczas IS, et al. Age-related changes in the physical properties, cross-linking, and glycation of collagen from mouse tail tendon. J Biol Chem. 2020;295(31):10562-10571. doi: 10.1074/jbc.RA119.011031

 

  1. Urios P, Grigorova-Borsos AM, Sternberg M. Flavonoids inhibit the formation of the cross-linking AGE pentosidine in collagen incubated with glucose, according to their structure. Eur J Nutr. 2007;46(3):139-146. doi: 10.1007/s00394-007-0644-0

 

  1. Hennet T. Collagen glycosylation. Curr Opin Struct Biol. 2019;56:131-138. doi: 10.1016/j.sbi.2019.01.015

 

  1. Bailey A. Molecular mechanisms of ageing in connective tissues. Mech Ageing Dev. 2001;122(7):735-755. doi: 10.1016/S0047-6374(01)00225-1

 

  1. Avery NC, Bailey AJ. Enzymic and non-enzymic cross-linking mechanisms in relation to turnover of collagen: relevance to aging and exercise. Scand J Med Sci Sports. 2005;15(4):231-240. doi: 10.1111/j.1600-0838.2005.00464.x

 

  1. Avery NC, Bailey AJ. The effects of the Maillard reaction on the physical properties and cell interactions of collagen. Pathol Biol. 2006;54(7):387-395. doi: 10.1016/j.patbio.2006.07.005

 

  1. Glenn JV, Stitt AW. The role of advanced glycation end products in retinal ageing and disease. Biochim Biophys Acta Gen Subj. 2009;1790(10):1109-1116. doi: 10.1016/j.bbagen.2009.04.016

 

  1. Simm A, Müller B, Nass N, et al. Protein glycation — Between tissue aging and protection. Exp Gerontol. 2015;68:71-75. doi: 10.1016/j.exger.2014.12.013

 

  1. Brett J, Schmidt AM, Yan SD, et al. Survey of the distribution of a newly characterized receptor for advanced glycation end products in tissues. Am J Pathol. 1993;143(6):1699-1712.

 

  1. Morbini P, Villa C, Campo I, et al. The receptor for advanced glycation end products and its ligands: a new inflammatory pathway in lung disease? Mod Pathol. 2006;19(11):1437- 1445. doi: 10.1038/modpathol.3800661

 

  1. Ibrahim AS, El-Remessy AB, Matragoon S, et al. Retinal Microglial Activation and Inflammation Induced by Amadori-Glycated Albumin in a Rat Model of Diabetes. Diabetes. 2011;60(4):1122-1133. doi: 10.2337/db10-1160

 

  1. Pertyńska-Marczewska M, Kiriakidis S, Wait R, et al. Advanced glycation end products upregulate angiogenic and pro-inflammatory cytokine production in human monocyte/macrophages. Cytokine. 2004;28(1):35-47. doi: 10.1016/j.cyto.2004.06.006

 

  1. Hamasaki S, Kobori T, Yamazaki Y, et al. Effects of scavenger receptors-1 class A stimulation on macrophage morphology and highly modified advanced glycation end product-protein phagocytosis. Sci Rep. 2018;8(1):5901. doi: 10.1038/s41598-018-24325-y

 

  1. Roca F, Grossin N, Chassagne P, et al. Glycation: The angiogenic paradox in aging and age-related disorders and diseases. Ageing Res Rev. 2014;15:146-160. doi: 10.1016/j.arr.2014.03.009

 

  1. Fadini GP, Sartore S, Baesso I, et al. Endothelial Progenitor Cells and the Diabetic Paradox. Diabetes Care. 2006;29(3):714-716. doi: 10.2337/diacare.29.03.06.dc05-1834

 

  1. Lu Z, Fan B, Li Y, et al. RAGE plays key role in diabetic retinopathy: a review. Biomed Eng Online. 2023;22(1):128. doi: 10.1186/s12938-023-01194-9

 

  1. Zeng Y, Buonfiglio F, Li J, et al. Mechanisms Underlying Vascular Inflammaging: Current Insights and Potential Treatment Approaches. Aging Dis. 2025;16(4):1889. doi: 10.14336/AD.2024.0922

 

  1. Arredouani MS, Yang Z, Imrich A, et al. The Macrophage Scavenger Receptor SR-AI/II and Lung Defense against Pneumococci and Particles. Am J Respir Cell Mol Biol. 2006;35(4):474-478. doi: 10.1165/rcmb.2006-0128OC

 

  1. Wang B, Jiang T, Qi Y, et al. AGE-RAGE Axis and Cardiovascular Diseases: Pathophysiologic Mechanisms and Prospects for Clinical Applications. Cardiovasc Drugs Ther. 2025;39(6):1489-1506. doi: 10.1007/s10557-024-07639-0

 

  1. Riuzzi F, Sorci G, Sagheddu R, et al. RAGE in the pathophysiology of skeletal muscle. J Cachexia Sarcopenia Muscle. 2018;9(7):1213-1234. doi: 10.1002/jcsm.12350

 

  1. Reddy VP, Beyaz A. Inhibitors of the Maillard reaction and AGE breakers as therapeutics for multiple diseases. Drug Discov Today. 2006;11(13-14):646-654. doi: 10.1016/j.drudis.2006.05.016

 

  1. Olson LC, Nguyen TM, Heise RL, et al. Advanced Glycation End Products Are Retained in Decellularized Muscle Matrix Derived from Aged Skeletal Muscle. Int J Mol Sci. 2021;22(16):8832. doi: 10.3390/ijms22168832

 

  1. Sant S, Wang D, Agarwal R, et al. Glycation alters the mechanical behavior of kidney extracellular matrix. Matrix Biol Plus. 2020;8:100035. doi: 10.1016/j.mbplus.2020.100035

 

  1. Soldatos G, Cooper ME. Advanced glycation end products and vascular structure and function. Curr Hypertens Rep. 2006;8(6):472-478. doi: 10.1007/s11906-006-0025-8

 

  1. Kurowski R, Manitius J. Produkty zaawansowanej glikacji białek (AGEs) a niewydolność nerek. Advanced glycation end products (AGEs) and renal failure. Przegl Lek. 2006;63(4):203-208. [In Polish].

 

  1. Matsunaga N, Anan I, Rosenberg P, et al. Advanced glycation end product is implicated in amyloid-related kidney complications. Scand J Clin Lab Invest. 2005;65(4):263-272. doi: 10.1080/00365510510013794

 

  1. Padival S, Nagaraj RH. Pyridoxamine Inhibits Maillard Reactions in Diabetic Rat Lenses. Ophthalmic Res. 2006;38(5):294-302. doi: 10.1159/000095773

 

  1. Stitt AW. The Maillard Reaction in Eye Diseases. Ann N Y Acad Sci. 2005;1043(1):582-597. doi: 10.1196/annals.1338.066

 

  1. Muntané G, Dalfó E, Martínez A, et al. Glial fibrillary acidic protein is a major target of glycoxidative and lipoxidative damage in Pick’s disease. J Neurochem. 2006;99(1):177-185. doi: 10.1111/j.1471-4159.2006.04032.x

 

  1. Semba RD, Fink JC, Sun K, et al. Serum Carboxymethyl- Lysine, a Dominant Advanced Glycation End Product, Is Associated With Chronic Kidney Disease: The Baltimore Longitudinal Study of Aging. J Ren Nutr. 2010;20(2):74-81. doi: 10.1053/j.jrn.2009.08.001

 

  1. Damasiewicz-Bodzek A, Łabuz-Roszak B, Kumaszka B, et al. Carboxymethyllysine and carboxyethyllysine in multiple sclerosis patients. Arch Med Sci. 2020;20(3):736-742. doi: 10.5114/aoms.2020.95654

 

  1. Bellmunt MJ, Portero M, Pamplona R, et al. Age-related fluorescence in rat lung collagen. Lung. 1995;173(3):177- 185. doi: 10.1007/BF00175658

 

  1. Nowotny K, Grune T. Degradation of oxidized and glycoxidized collagen: Role of collagen cross-linking. Arch Biochem Biophys. 2014;542:56-64. doi: 10.1016/j.abb.2013.12.007

 

  1. Wang ZQ, Sun Z. Dietary Nε-(carboxymethyl) lysine affects cardiac glucose metabolism and myocardial remodeling in mice. World J Diabetes. 2022;13(11):972-985. doi: 10.4239/wjd.v13.i11.972

 

  1. Vos PAJM, Mastbergen SC, Huisman AM, et al. In end stage osteoarthritis, cartilage tissue pentosidine levels are inversely related to parameters of cartilage damage. Osteoarthritis Cartilage. 2012;20(3):233-240. doi: 10.1016/j.joca.2011.12.007

 

  1. Matsumine M, Shibata N, Ishitani K, et al. Pentosidine Accumulation in Human Oocytes and Their Correlation to Age-Related Apoptosis. Acta Histochem Cytochem. 2008;41(4):97-104. doi: 10.1267/ahc.08014

 

  1. Sivan SS, Tsitron E, Wachtel E, et al. Age-related accumulation of pentosidine in aggrecan and collagen from normal and degenerate human intervertebral discs. Biochem J. 2006;399(1):29-35. doi: 10.1042/BJ20060579

 

  1. Eekhoff JD, Fang F, Lake SP. Multiscale mechanical effects of native collagen cross-linking in tendon. Connect Tissue Res. 2018;59(5):410-422. doi: 10.1080/03008207.2018.1449837

 

  1. Miyata T, Sugiyama S, Suzuki D, et al. Increased carbonyl modification by lipids and carbohydrates in diabetic nephropathy. Kidney Int. 1999;56:S54-S56. doi: 10.1046/j.1523-1755.1999.07114.x

 

  1. Horie K, Miyata T, Yasuda T, et al. Immunohistochemical Localization of Advanced Glycation End Products, Pentosidine, and Carboxymethyllysine in Lipofuscin Pigments of Alzheimer’s Disease and Aged Neurons. Biochem Biophys Res Commun. 1997;236(2):327-332. doi: 10.1006/bbrc.1997.6944

 

  1. Zhang W, Xiao D, Mao Q, et al. Role of neuroinflammation in neurodegeneration development. Signal Transduct Target Ther. 2023;8(1):267. doi: 10.1038/s41392-023-01486-5

 

  1. Ashraf G, Greig N, Khan T, et al. Protein Misfolding and Aggregation in Alzheimer’s Disease and Type 2 Diabetes Mellitus. CNS Neurol Disord Drug Targets. 2014;13(7):1280- 1293. doi: 10.2174/1871527313666140917095514

 

  1. Ajmal MR. Protein Misfolding and Aggregation in Proteinopathies: Causes, Mechanism and Cellular Response. Diseases. 2023;11(1):30. doi: 10.3390/diseases11010030

 

  1. Demontis F, Piccirillo R, Goldberg AL, et al. Mechanisms of skeletal muscle aging: insights from Drosophila and mammalian models. Dis Model Mech. 2013;6(6):1339-1352. doi: 10.1242/dmm.012559

 

  1. Kjær M, Magnusson P, Krogsgaard M, et al. Extracellular matrix adaptation of tendon and skeletal muscle to exercise. J Anat. 2006;208(4):445-450. doi: 10.1111/j.1469-7580.2006.00549.x

 

  1. Dall’Olio F. Glycobiology of Aging. In: Harris JR, Korolchuk VI, eds. Biochemistry and Cell Biology of Ageing: Part I Biomedical Science. Vol 90. Springer; 2018:505-526. doi: 10.1007/978-981-13-2835-0_17

 

  1. Sen CK, Friday A, Khanna S, et al. Collagen-Based Products in Wound, Skin, and Health Care. Adv Wound Care. 2025;14(8):479-495. doi: 10.1177/21621918251361118

 

  1. Khalilgharibi N, Mao Y. To form and function: on the role of basement membrane mechanics in tissue development, homeostasis and disease. Open Biol. 2021;11(2):200360. doi: 10.1098/rsob.200360

 

  1. Kesava Reddy G. AGE-related cross-linking of collagen is associated with aortic wall matrix stiffness in the pathogenesis of drug-induced diabetes in rats. Microvasc Res. 2004;68(2):132-142. doi: 10.1016/j.mvr.2004.04.002

 

  1. Obrenovich ME, Monnier VM. Apoptotic killing of fibroblasts by matrix-bound advanced glycation endproducts. Sci Aging Knowledge Environ. 2005;2005(4):pe3. doi: 10.1126/sageke.2005.4.pe3

 

  1. Pageon H, Bakala H, Monnier VM, et al. Collagen glycation triggers the formation of aged skin in vitro. Eur J Dermatol. 2007;17(1):12-20. doi: 10.1684/ejd.2007.0102

 

  1. Harding JJ, Ganea E. Protection against glycation and similar post-translational modifications of proteins. Biochim Biophys Acta. 2006;1764(9):1436-1446. doi: 10.1016/j.bbapap.2006.08.001

 

  1. Hadley J, Malik N, Meek K. Collagen as a model system to investigate the use of aspirin as an inhibitor of protein glycation and crosslinking. Micron. 2001;32(3):307-315. doi: 10.1016/s0968-4328(00)00032-9

 

  1. Urios P, Grigorova-Borsos AM, Sternberg M. Aspirin inhibits the formation of pentosidine, a cross-linking advanced glycation end product, in collagen. Diabetes Res Clin Pract. 2007;77(2):337-340. doi: 10.1016/j.diabres.2006.12.024

 

  1. Finamore F, Priego-Capote F, Nolli S, et al. Characterisation of the influences of aspirin-acetylation and glycation on human plasma proteins. J Proteomics. 2015;114:125-135. doi: 10.1016/j.jprot.2014.11.005

 

  1. Gao J, Liu Y, Si C, et al. Aspirin inhibits proteasomal degradation and promotes α-synuclein aggregate clearance through K63 ubiquitination. Nat Commun. 2025;16(1):1438. doi: 10.1038/s41467-025-56737-6

 

  1. Kontoghiorghes GJ. New Insights into Aspirin’s Anticancer Activity: The Predominant Role of Its Iron-Chelating Antioxidant Metabolites. Antioxidants. 2024;14(1):29. doi: 10.3390/antiox14010029

 

  1. Maria MKM, Bashir MH, Fares AE, et al. The prophylactic anti-aging effect of aspirin (acetylsalicylic acid) on oxidative stress-induced damage in the buccal mucosa of D-galactose-induced aged rats. Sci Rep. 2025;15(1):13053. doi: 10.1038/s41598-025-94566-1

 

  1. Plater ML, Goode D, Crabbe JC. Ibuprofen Protects Alpha-Crystallin against Posttranslational Modification by Preventing Protein Cross-Linking. Ophthalmic Res. 1997;29(6):421-428. doi: 10.1159/000268043

 

  1. Cervantes-Laurean D, Schramm DD, Jacobson EL, et al. Inhibition of advanced glycation end product formation on collagen by rutin and its metabolites. J Nutr Biochem. 2006;17(8):531-540. doi: 10.1016/j.jnutbio.2005.10.002

 

  1. Monnier VM. Bacterial enzymes that can deglycate glucose-and fructose-modified lysine. Biochem J. 2005;392(Pt 2):e1- e3. doi: 10.1042/BJ20051625

 

  1. Monnier VM, Sell DR. Prevention and repair of protein damage by the Maillard reaction in vivo. Rejuvenation Res. 2006;9(2):264-273. doi: 10.1089/rej.2006.9.264

 

  1. Van Schaftingen E, Collard F, Wiame E, et al. Enzymatic repair of Amadori products. Amino Acids. 2012;42(4):1143- 1150. doi: 10.1007/s00726-010-0780-3

 

  1. Brings S, Fleming T, Freichel M, et al. Dicarbonyls and Advanced Glycation End-Products in the Development of Diabetic Complications and Targets for Intervention. Int J Mol Sci. 2017;18(5):984. doi: 10.3390/ijms18050984

 

  1. Sartore G, Ragazzi E, Burlina S, et al. Role of fructosamine-3- kinase in protecting against the onset of microvascular and macrovascular complications in patients with T2DM. BMJ Open Diabetes Res Care. 2020;8(1):e001256. doi: 10.1136/bmjdrc-2020-001256

 

  1. De Decker I, Notebaert M, Speeckaert MM, et al. Enzymatic Deglycation of Damaged Skin by Means of Combined Treatment of Fructosamine-3-Kinase and Fructosyl-Amino Acid Oxidase. Int J Mol Sci. 2023;24(10):8981. doi: 10.3390/ijms24108981

 

  1. Choi JY, Ha NG, Lee WJ, et al. Synthetic and Natural Agents Targeting Advanced Glycation End-Products for Skin Anti- Aging: A Comprehensive Review of Experimental and Clinical Studies. Antioxidants. 2025;14(4):498. doi: 10.3390/antiox14040498

 

  1. Komsa-Penkova R, Dimitrov B, Todinova S, et al. Early Stages of Ex Vivo Collagen Glycation Disrupt the Cellular Interaction and Its Remodeling by Mesenchymal Stem Cells—Morphological and Biochemical Evidence. Int J Mol Sci. 2024;25(11):5795. doi: 10.3390/ijms25115795

 

  1. Mikulíková K, Eckhardt A, Kunes J, et al. Advanced glycation end-product pentosidine accumulates in various tissues of rats with high fructose intake. Physiol Res. 2008;57(1):89-94. doi: 10.33549/physiolres.931093

 

  1. Yamaguchi H, Nagai R. Insights from the fructose-derived product glucoselysine: Revisiting the polyol pathway in diabetic complications. J Diabetes Investig. 2025;16(4):569- 577. doi: 10.1111/jdi.70000

 

  1. Yan L. Redox imbalance stress in diabetes mellitus: Role of the polyol pathway. Anim Models Exp Med. 2018;1(1):7-13. doi: 10.1002/ame2.12001

 

  1. Kuliczkowska-Płaksej J, Bednarek-Tupikowska G, Płaksej R, et al. Wpływ cukrzycy i insulinooporności na ekspresje receptora CD36. Cześć II. Udział receptora CD36 w patomechanizmie powikłań cukrzycy. The influence of diabetes mellitus and insulin resistance on receptor CD36 expression. Part II. The role of receptor CD36 in the pathomechanism of diabetes complications. Postepy Hig Med Dosw (Online). 2006;60:152-162. [In Polish].

 

  1. Robert L, Labat-Robert J. The metabolic syndrome and the Maillard reaction. An introduction. Pathol Biol (Paris). 2006;54(7):371-374. doi: 10.1016/j.patbio.2006.07.014

 

  1. Chen S, Xie Y, Alvarez MR, et al. Quantitative Glycan- Protein Cross-Linking Mass Spectrometry Using Enrichable Linkers Reveals Extensive Glycan-Mediated Protein Interaction Networks. Anal Chem. 2025;97(3):1584-1593. doi: 10.1021/acs.analchem.4c04134

 

  1. Illiano A, Pinto G, Melchiorre C, et al. Protein Glycosylation Investigated by Mass Spectrometry: An Overview. Cells. 2020;9(9):1986. doi: 10.3390/cells9091986

 

  1. Kennedy-Darling J, Smith LM. Measuring the Formaldehyde Protein–DNA Cross-Link Reversal Rate. Anal Chem. 2014;86(12):5678-5681. doi: 10.1021/ac501354y
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