Advanced Glycation End Products and Oxidative Stress in Type 2 Diabetes Mellitus
Open accessAbstract
Type 2 diabetes mellitus (T2DM) is a very complex and multifactorial metabolic disease characterized by insulin resistance and β cell failure leading to elevated blood glucose levels. Hyperglycemia is suggested to be the main cause of diabetic complications, which not only decrease life quality and expectancy, but are also becoming a problem regarding the financial burden for health care systems. Therefore, and to counteract the continually increasing prevalence of diabetes, understanding the pathogenesis, the main risk factors, and the underlying molecular mechanisms may establish a basis for prevention and therapy. In this regard, research was performed revealing further evidence that oxidative stress has an important role in hyperglycemia-induced tissue injury as well as in early events relevant for the development of T2DM. The formation of advanced glycation end products (AGEs), a group of modified proteins and/or lipids with damaging potential, is one contributing factor. On the one hand it has been reported that AGEs increase reactive oxygen species formation and impair antioxidant systems, on the other hand the formation of some AGEs is induced per se under oxidative conditions. Thus, AGEs contribute at least partly to chronic stress conditions in diabetes. As AGEs are not only formed endogenously, but also derive from exogenous sources, i.e., food, they have been assumed as risk factors for T2DM. However, the role of AGEs in the pathogenesis of T2DM and diabetic complications—if they are causal or simply an effect—is only partly understood. This review will highlight the involvement of AGEs in the development and progression of T2DM and their role in diabetic complications.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Glycoxidation products form and accumulate during normal conditions and especially under hyperglycemia, hyperlipidemia, and oxidative stress.
“The formation and accumulation of glycoxidation products occurs during normal, but especially under certain physiological conditions, such as hyperglycemia, hyperlipidemia, and oxidative stress.”
From Protein oxidation - Formation mechanisms, detection and relevance as biomarkers in human diseases (2021) · cites this paper as [152]
Section 2, “AGEs in Diabetes: An Overview” (page not specified), says AGE formation occurs as part of physiological metabolism, is accelerated in diabetes by elevated glucose and oxidative stress, and that oxidative stress triggers glycoxidation products. It identifies lipid peroxidation as a pathway to AGE formation, but does not establish that hyperlipidemia itself especially increases their formation or accumulation. (LLM, conf=0.85)
Experimental — accuracy not yet measuredGlycoxidation products are relevant in the progression of metabolic diseases, including neurodegenerative disease, CKD, CVD, and cancer, particularly T2D and related complications.
“This indicates their relevance in the progression of metabolic diseases, including neurodegenerative disease, chronic kidney disease (CDK), CVD, and cancer, but in particular, T2D and related complications as reviewed elsewhere [152].”
From Protein oxidation - Formation mechanisms, detection and relevance as biomarkers in human diseases (2021) · cites this paper as [152]
The Introduction and Section 5 link advanced glycation end products (AGEs) to T2D and diabetic complications, including nephropathy and cardiovascular disease (page numbers unavailable). The copy does not establish their relevance to neurodegenerative disease or cancer, and its kidney-disease discussion focuses on diabetic nephropathy rather than CKD generally. (LLM, conf=0.88)
Experimental — accuracy not yet measuredLevels of glycoxidation products increase as a function of age in several tissues, dependent on dietary intake and hyperglycemic conditions.
“a growing body of evidence reveals that levels of glycoxidation products increase as a function of age in several tissues, dependent on the dietary intake and the presence of hyperglycemic conditions [152,153]”
From Protein oxidation - Formation mechanisms, detection and relevance as biomarkers in human diseases (2021) · cites this paper as [152]
Section 2 (page unavailable) reports increased AGE formation and tissue levels in diabetes, and says dietary AGE intake correlates with serum AGE levels. It does not report that glycoxidation products increase with age across several tissues; the age-related part of the claim is therefore unsupported by this paper's text. (LLM, conf=0.85)
Experimental — accuracy not yet measuredDicarbonyls can also be generated from glucose autoxidation, lipid peroxidation, and the polyol pathway.
“These molecules can also be generated from glucose autoxidation, lipid peroxidation, and the polyol pathway.[18]”
From The Role of Dietary Advanced Glycation End Products in Metabolic Dysfunction (2021) · cites this paper as [18]
AGEs can contribute to both pathogenetic features of T2DM by promoting inflammation and oxidative stress in humans.
“AGEs can contribute to both pathogenetic features of T2DM by promoting inflammation and oxidative stress in humans. [18]”
From The Role of Dietary Advanced Glycation End Products in Metabolic Dysfunction (2021) · cites this paper as [18]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Matthews, D. R., Hosker, J. P., Rudenski, A. S., Naylor, B. A., Treacher, D. F., & Turner, R. C. (1985) · Diabetologia · doi:10.1007/bf00280883 · Cited by 31,502 · see citing works
Toprak, Ö., Kurt, H., Sarı, Y., Şarkış, C., Us, H., & Kırık, A. (2017) · Kidney & Blood Pressure Research · doi:10.1159/000468530 · Cited by 29,769 · see citing works
Global and societal implications of the diabetes epidemic
Zimmet, P., Alberti, K. G. M. M., & Shaw, J. (2001) · Nature · doi:10.1038/414782a · Cited by 5,883 · see citing works
Oxidative stress and diabetic complications
Giacco, F., & Brownlee, M. (2010) · Circulation Research · doi:10.1161/circresaha.110.223545 · Cited by 5,461 · see citing works
The Emerging Risk Factors Collaboration (2010) · The Lancet · doi:10.1016/s0140-6736(10)60484-9 · Cited by 5,125 · see citing works
Gupta, A., & Uribarri, J. (2016) · Hormone Research in Paediatrics · doi:10.1159/000444053 · Cited by 4,019 · see citing works
Role of Oxidative Stress in Development of Complications in Diabetes
Baynes, J. (1991) · Diabetes · doi:10.2337/diab.40.4.405 · Cited by 3,791 · see citing works
Oxidative stress: a concept in redox biology and medicine
Sies, H. (2015) · Redox Biology · doi:10.1016/j.redox.2015.01.002 · Cited by 3,015 · see citing works
Advanced glycation end-products: A review
Singh, R., Barden, A., Mori, T., & Beilin, L. (2001) · Diabetologia · doi:10.1007/s001250051591 · Cited by 2,597 · see citing works
Dehydrated Foods, Chemistry of Browning Reactions in Model Systems
Hodge, J. E. (1953) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf60015a004 · Cited by 1,950 · see citing works
RAGE Mediates a Novel Proinflammatory Axis
Hofmann, M. A., Drury, S., Fu, C., Qu, W., Taguchi, A., Lu, Y., Avila, C., Kambham, N., Bierhaus, A., Nawroth, P., et al. (1999) · Cell · doi:10.1016/s0092-8674(00)80801-6 · Cited by 1,864 · see citing works
Activation of interleukin-6 gene expression through the NF-kappa B transcription factor.
Libermann, T. A., & Baltimore, D. (1990) · Molecular and Cellular Biology · doi:10.1128/mcb.10.5.2327 · Cited by 1,372 · see citing works
Mortality and causes of death in the WHO Multinational Study of Vascular Disease in Diabetes
and the WHO Multinational Study Group, Morrish, N. J., Wang, S.-L., Stevens, L. K., Fuller, J. H., & Keen, H. (2001) · Diabetologia · doi:10.1007/pl00002934 · Cited by 1,288 · see citing works
Formation of glyoxal, methylglyoxal and 3-deoxyglucosone in the glycation of proteins by glucose
Thornalley, P. J., LANGBORG, A., & Minhas, H. S. (1999) · Biochemical Journal · doi:10.1042/bj3440109 · Cited by 1,209 · see citing works
Bucala, R., Tracey, K. J., & Cerami, A. (1991) · Journal of Clinical Investigation · doi:10.1172/jci115014 · Cited by 1,162 · see citing works
The Receptor for Advanced Glycation End Products (RAGE) Is a Cellular Binding Site for Amphoterin
Hori, O., Brett, J., Slattery, T., Cao, R., Zhang, J., Chen, J. X., Nagashima, M., Lundh, E. R., Vijay, S., Nitecki, D., et al. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.43.25752 · Cited by 1,151 · see citing works
Role of advanced glycation end products in cellular signaling
Ott, C., Jacobs, K., Haucke, E., Navarrete Santos, A., Grune, T., & Simm, A. (2014) · Redox Biology · doi:10.1016/j.redox.2013.12.016 · Cited by 1,150 · see citing works
Self-citationStructure Elucidation of a Senescence Cross-Link from Human Extracellular Matrix
Sell, D. R., & Monnier, V. M. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)88225-8 · Cited by 1,082 · see citing works
Schmidt, A. M., Hori, O., Chen, J. X., Li, J. F., Crandall, J., Zhang, J., Cao, R., Yan, S. D., Brett, J., & Stern, D. (1995) · Journal of Clinical Investigation · doi:10.1172/jci118175 · Cited by 896 · see citing works
Diabetes-Associated Sustained Activation of the Transcription Factor Nuclear Factor-κB
Bierhaus, A., Schiekofer, S., Schwaninger, M., Andrassy, M., Humpert, P. M., Chen, J., Hong, M., Luther, T., Henle, T., Klöting, I., et al. (2001) · Diabetes · doi:10.2337/diabetes.50.12.2792 · Cited by 826 · see citing works
Fu, M.-X., Requena, J. R., Jenkins, A. J., Lyons, T. J., Baynes, J. W., & Thorpe, S. R. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.17.9982 · Cited by 822 · see citing works
Koschinsky, T., He, C.-J., Mitsuhashi, T., Bucala, R., Liu, C., Buenting, C., Heitmann, K., & Vlassara, H. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.12.6474 · Cited by 792 · see citing works
Simple non-invasive assessment of advanced glycation endproduct accumulation
Meerwaldt, R., Graaff, R., Oomen, P. H. N., Links, T. P., Jager, J. J., Alderson, N. L., Thorpe, S. R., Baynes, J., Gans, R. O. B., & Smit, A. J. (2004) · Diabetologia · doi:10.1007/s00125-004-1451-2 · Cited by 767 · see citing works
Advanced glycation endproducts in food and their effects on health
Poulsen, M. W., Hedegaard, R. V., Andersen, J. M., de Courten, B., Bügel, S., Nielsen, J., Skibsted, L. H., & Dragsted, L. O. (2013) · Food and Chemical Toxicology · doi:10.1016/j.fct.2013.06.052 · Cited by 751 · see citing works
Advanced glycoxidation end products in commonly consumed foods
Goldberg, T., Cai, W., Peppa, M., Dardaine, V., Baliga, B. S., Uribarri, J., & Vlassara, H. (2004) · Journal of the American Dietetic Association · doi:10.1016/j.jada.2004.05.214 · Cited by 744 · see citing works
Schleicher, E. D., Wagner, E., & Nerlich, A. G. (1997) · Journal of Clinical Investigation · doi:10.1172/jci119180 · Cited by 714 · see citing works
Vlassara, H., Cai, W., Crandall, J., Goldberg, T., Oberstein, R., Dardaine, V., Peppa, M., & Rayfield, E. J. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.242407999 · Cited by 668 · see citing works
Ahmed, M. U., Frye, E. B., Degenhardt, T. P., Thorpe, S. R., & Baynes, J. (1997) · Biochemical Journal · doi:10.1042/bj3240565 · Cited by 605 · see citing works
Oxidative stress and the etiology of insulin resistance and type 2 diabetes
Henriksen, E. J., Diamond-Stanic, M. K., & Marchionne, E. M. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.12.005 · Cited by 600 · see citing works
Wells‐Knecht, K. J., Zyzak, D. V., Litchfield, J., Thorpe, S. R., & Baynes, J. (1995) · Biochemistry · doi:10.1021/bi00011a027 · Cited by 594 · see citing works
Advanced Glycation End Products (AGE) and Diabetes: Cause, Effect, or Both?
Vlassara, H., & Uribarri, J. (2014) · Current Diabetes Reports · doi:10.1007/s11892-013-0453-1 · Cited by 594 · see citing works
The Pattern Recognition Receptor (RAGE) Is a Counterreceptor for Leukocyte Integrins
Chavakis, T., Bierhaus, A., Al‐Fakhri, N., Schneider, D., Witte, S., Linn, T., Nagashima, M., Morser, J., Arnold, B., Preissner, K. T., et al. (2003) · The Journal of Experimental Medicine · doi:10.1084/jem.20030800 · Cited by 583 · see citing works
Uribarri, J., Cai, W., Peppa, M., Goodman, S., Ferrucci, L., Striker, G., & Vlassara, H. (2007) · The Journals of Gerontology Series A: Biological Sciences and Medical Sciences · doi:10.1093/gerona/62.4.427 · Cited by 570 · see citing works
Maillard reaction products in tissue proteins: New products and new perspectives
Thorpe, S. R., & Baynes, J. (2003) · Amino Acids · doi:10.1007/s00726-003-0017-9 · Cited by 543 · see citing works
Dyer, D. G., Blackledge, J. A., Thorpe, S. R., & Baynes, J. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)99007-1 · Cited by 535 · see citing works
Li, J., & Schmidt, A. M. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.26.16498 · Cited by 525 · see citing works
Eto, K., Tsubamoto, Y., Terauchi, Y., 杉山, 拓., Kishimoto, T. E., Takahashi, N. K., Yamauchi, N., Kubota, N., Murayama, S., Aizawa, T., et al. (1999) · Science · doi:10.1126/science.283.5404.981 · Cited by 491 · see citing works
Pathogenesis of Type 2 Diabetes Mellitus
Leahy, J. L. (2005) · Archives of Medical Research · doi:10.1016/j.arcmed.2005.01.003 · Cited by 469 · see citing works
Oldfield, M. D., Bach, L. A., Forbes, J. M., Nikolic‐Paterson, D. J., McRobert, E. A., Thallas, V., Atkins, R. C., Osicka, T. M., Jerums, G., & Cooper, M. E. (2001) · Journal of Clinical Investigation · doi:10.1172/jci11951 · Cited by 469 · see citing works
Advanced glycation end products increase retinal vascular endothelial growth factor expression.
Lu, M., Kuroki, M., Amano, S., Tolentino, M. J., Keough, K. C., Kim, I. K., Bucala, R., & Adamis, A. P. (1998) · Journal of Clinical Investigation · doi:10.1172/jci1277 · Cited by 422 · see citing works
Activation of Interleukin-6 Gene Expression through the NF-κB Transcription Factor
Libermann, T. A., & Baltimore, D. (1990) · Molecular and Cellular Biology · doi:10.1128/mcb.10.5.2327-2334.1990 · Cited by 404 · see citing works
Further identification of the nature and linkage of the carbohydrate in hemoglobin A1c
Bunn, H. F., Haney, D. N., Gabbay, K. H., & Gallop, P. M. (1975) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(75)90289-2 · Cited by 403 · see citing works
Jung, T., Catalgol, B., & Grune, T. (2009) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2009.04.001 · Cited by 389 · see citing works
Self-citationAn abnormal hemoglobin in red cells of diabetics
Rahbar, S. (1968) · Clinica Chimica Acta · doi:10.1016/0009-8981(68)90372-0 · Cited by 380 · see citing works
Pongor, S., Ulrich, P. C., Bencsath, F. A., & Cerami, A. (1984) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.81.9.2684 · Cited by 373 · see citing works
The Role of TNF-α in Insulin Resistance
Borst, S. E. (2004) · Endocrine · doi:10.1385/endo:23:2-3:177 · Cited by 369 · see citing works
Liang, F.-X., Kume, S., & Koya, D. (2009) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2009.101 · Cited by 356 · see citing works
Uribarri, J., Peppa, Μ., Cai, W., Goldberg, T., Lu, M. M., He, C., & Vlassara, H. (2003) · Journal of the American Society of Nephrology · doi:10.1097/01.asn.0000051593.41395.b9 · Cited by 331 · see citing works
Cai, W., Ramdas, M., Zhu, L., Chen, X., Striker, G. E., & Vlassara, H. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1205847109 · Cited by 330 · see citing works
Restriction of Advanced Glycation End Products Improves Insulin Resistance in Human Type 2 Diabetes
Uribarri, J., Cai, W., Ramdas, M., Goodman, S., Pyzik, R., Chen, X., Zhu, L., Striker, G. E., & Vlassara, H. (2011) · Diabetes Care · doi:10.2337/dc11-0091 · Cited by 320 · see citing works
Transcriptional Regulation of The Human Monocyte Chemoattractant Protein-1 Gene
Ueda, A., Ishigatsubo, Y., Okubo, T., & Yoshimura, T. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.49.31092 · Cited by 309 · see citing works
Yamagishi, S., Inagaki, Y., Okamoto, T., Amano, S., Koga, K., Takeuchi, M., & Makita, Z. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202634200 · Cited by 308 · see citing works
Protein Cross-linking by the Maillard Reaction
Nagaraj, R. H., Shipanova, I. N., & Faust, F. M. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.32.19338 · Cited by 304 · see citing works
Regulation of insulin secretion: role of mitochondrial signalling
Jitrapakdee, S., Wutthisathapornchai, A., Wallace, J. C., & MacDonald, M. J. (2010) · Diabetologia · doi:10.1007/s00125-010-1685-0 · Cited by 296 · see citing works
Kume, S., Takeya, M., Mori, T., Araki, N., Suzuki, H., Horiuchi, S., Kodama, T., Miyauchi, Y., & Takahashi, K. (1995) · Europe PMC (PubMed Central) · Cited by 295 · see citing works
Advanced glycation end products up-regulate gene expression found in diabetic glomerular disease.
Yang, C., Vlassara, H., Peten, E. P., He, C., Striker, G. E., & Striker, L. J. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.20.9436 · Cited by 294 · see citing works
Skin Autofluorescence Is a Strong Predictor of Cardiac Mortality in Diabetes
Meerwaldt, R., Lutgers, H. L., Links, T. P., Graaff, R., Baynes, J., Gans, R. O. B., & Smit, A. J. (2006) · Diabetes Care · doi:10.2337/dc06-1391 · Cited by 287 · see citing works
Quehenberger, P., Bierhaus, A., Fasching, P., Muellner, C., Klevesath, M. S., Hong, M., Stier, G., Sattler, M., Schleicher, E., Speiser, W., et al. (2000) · Diabetes · doi:10.2337/diabetes.49.9.1561 · Cited by 283 · see citing works
Shipanova, I. N., Glomb, M. A., & Nagaraj, R. H. (1997) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1997.0195 · Cited by 279 · see citing works
Diabetes-Induced Oxidative Stress and Low-Grade Inflammation in Porcine Coronary Arteries
Zhang, L., Zalewski, A. A., Liu, Y., Mazurek, T., Cowan, S., Martin, J. L., Hofmann, S. M., Vlassara, H., & Shi, Y. (2003) · Circulation · doi:10.1161/01.cir.0000080378.96063.23 · Cited by 277 · see citing works
Kilhovd, B. K., Berg, T. J., Birkeland, K. I., Thorsby, P. M., & Hanssen, K. F. (1999) · Diabetes Care · doi:10.2337/diacare.22.9.1543 · Cited by 269 · see citing works
Dobler, D., Ahmed, N., Song, L., Eboigbodin, K. E., & Thornalley, P. J. (2006) · Diabetes · doi:10.2337/db05-1634 · Cited by 269 · see citing works
Vlassara, H., Fuh, H., Donnelly, T. M., & Cybulsky, M. I. (1995) · Molecular Medicine · doi:10.1007/bf03401582 · Cited by 243 · see citing works
Burns, W. C., Twigg, S. M., Forbes, J. M., Pete, J., Tikellis, C., Thallas‐Bonke, V., Thomas, M. C., Cooper, M. E., & Kantharidis, P. (2006) · Journal of the American Society of Nephrology · doi:10.1681/asn.2006050525 · Cited by 243 · see citing works
Formation of glyoxal, methylglyoxal and 3-deoxyglucosone in the glycation of proteins by glucose
Thornalley, P. J., LANGBORG, A., & Minhas, H. S. (1999) · Biochemical Journal · doi:10.1042/0264-6021:3440109 · Cited by 243 · see citing works
Chakravarthy, U., Hayes, R., Stitt, A. W., McAuley, E., & Archer, D. B. (1998) · Diabetes · doi:10.2337/diabetes.47.6.945 · Cited by 237 · see citing works
Lu, C., He, J. C., Cai, W., Liu, H., Zhu, L., & Vlassara, H. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401588101 · Cited by 228 · see citing works
Vlassara, H., Cai, W., Goodman, S., Pyzik, R., Yong, A., Chen, X., Zhu, L., Neade, T., Beeri, M. S., Silverman, J. M., et al. (2009) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2009-0089 · Cited by 226 · see citing works
Guimarães, E. L. M., Empsen, C., Geerts, A. E., & van Grunsven, L. A. (2009) · Journal of Hepatology · doi:10.1016/j.jhep.2009.12.007 · Cited by 226 · see citing works
AGEs activate mesangial TGF-β–Smad signaling via an angiotensin II type I receptor interaction
Fukami, K., Ueda, S., Yamagishi, S., Kato, S., Inagaki, Y., Takeuchi, M., Motomiya, Y., Bucala, R., Iida, S., Tamaki, K., et al. (2004) · Kidney International · doi:10.1111/j.1523-1755.2004.66004.x · Cited by 218 · see citing works
Ravichandran, L. V., Esposito, D. L., Chen, J. Y. ‐., & Quon, M. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007231200 · Cited by 217 · see citing works
Li, J., Wang, W., Huang, X. R., Oldfield, M. D., Schmidt, A. M., Cooper, M. E., & Lan, H. Y. (2004) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)63225-7 · Cited by 217 · see citing works
Glucosepane Is a Major Protein Cross-link of the Senescent Human Extracellular Matrix
Sell, D. R., Biemel, K. M., Reihl, O., Lederer, M. O., Strauch, C., & Monnier, V. M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500733200 · Cited by 212 · see citing works
Yamagishi, S., Amano, S., Inagaki, Y., Okamoto, T., Koga, K., Sasaki, N., Yamamoto, H., Takeuchi, M., & Makita, Z. (2002) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.6312 · Cited by 210 · see citing works
Biemel, K. M., Friedl, D. A., & Lederer, M. O. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202681200 · Cited by 210 · see citing works
Assar, S. H., Moloney, C., Lima, M., Magee, R., & Ames, J. M. (2009) · Amino Acids · doi:10.1007/s00726-008-0071-4 · Cited by 206 · see citing works
Impairment of vascular endothelial nitric oxide synthase activity by advanced glycation end products
Biao, X., Chibber, R., Ruggiero, D., Kohner, E., Ritter, J., & Ferro, A. (2003) · The FASEB Journal · doi:10.1096/fj.02-0490fje · Cited by 195 · see citing works
Haitoglou, C., Tsilibary, E. C., Brownlee, M., & CHARONIS, A. S. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42287-9 · Cited by 194 · see citing works
Yamagishi, S., Fujimori, H., Yonekura, H., Yamamoto, Y., & Yamamoto, H. (1998) · Diabetologia · doi:10.1007/s001250051089 · Cited by 193 · see citing works
Tanikawa, T., Okada, Y., Tanikawa, R., & Tanaka, Y. (2009) · Journal of Vascular Research · doi:10.1159/000226225 · Cited by 191 · see citing works
Kilhovd, B. K., Giardino, I., Torjesen, P. A., Birkeland, K. I., Berg, T. J., Thornalley, P. J., Brownlee, M., & Hanssen, K. F. (2003) · Metabolism · doi:10.1053/meta.2003.50035 · Cited by 187 · see citing works
Glycated Proteins Stimulate Reactive Oxygen Species Production in Cardiac Myocytes
Zhang, M., Kho, A. L., Anilkumar, N. P., Chibber, R., Pagano, P. J., Shah, A. M., & Cave, A. C. (2006) · Circulation · doi:10.1161/circulationaha.105.581397 · Cited by 187 · see citing works
Duran-Jimenez, B., Dobler, D., Moffatt, S., Rabbani, N., Streuli, C. H., Thornalley, P. J., Tomlinson, D. R., & Gardiner, N. J. (2009) · Diabetes · doi:10.2337/db09-0320 · Cited by 186 · see citing works
AGEs in foods: do they play a role in uremia?
Henle, T. (2003) · Kidney International · doi:10.1046/j.1523-1755.63.s84.16.x · Cited by 184 · see citing works
Scheijen, J. L. J. M., & Schalkwijk, C. G. (2013) · Clinical Chemistry and Laboratory Medicine (CCLM) · doi:10.1515/cclm-2012-0878 · Cited by 184 · see citing works
Glycation Products as Markers and Predictors of the Progression of Diabetic Complications
Monnier, V. M., Sell, D. R., & GENUTH, S. M. (2005) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1333.065 · Cited by 182 · see citing works
Advanced Glycation End-Products Induce Tubular CTGF via TGF-β–Independent Smad3 Signaling
Chung, A. C. K., Zhang, H., Kong, Y.-Z., Jia-ju, T., Huang, X. R., Kopp, J. B., & Lan, H. Y. (2009) · Journal of the American Society of Nephrology · doi:10.1681/asn.2009010018 · Cited by 180 · see citing works
Throckmorton, D. C., Brogden, A. P., Min, B., Rasmussen, H., & Kashgarian, M. J. (1995) · Kidney International · doi:10.1038/ki.1995.274 · Cited by 174 · see citing works
Ishibashi, Y., Matsui, T., Takeuchi, M., & Yamagishi, S. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.12.075 · Cited by 173 · see citing works
The Role of Advanced Glycation End Products in Retinal Microvascular Leukostasis
Moore, T., Moore, J. E., Kaji, Y., Frizzell, N., Usui, T., Poulaki, V., Campbell, I. L., Stitt, A. W., Gardiner, T. A., ARCHER, D. B., et al. (2003) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.02-1063 · Cited by 172 · see citing works
Kilhovd, B. K., Juutilainen, A., Lehto, S., Rönnemaa, T., Torjesen, P. A., Hanssen, K. F., & Laakso, M. (2007) · Diabetologia · doi:10.1007/s00125-007-0687-z · Cited by 165 · see citing works
Ishibashi, Y., Matsui, T., Maeda, S., Higashimoto, Y., & Yamagishi, S. (2013) · Cardiovascular Diabetology · doi:10.1186/1475-2840-12-125 · Cited by 164 · see citing works
Nitric oxide and arterial disease
Barbato, J. E., & Tzeng, E. (2004) · Journal of Vascular Surgery · doi:10.1016/j.jvs.2004.03.043 · Cited by 162 · see citing works
Aso, Y., Inukai, T., Tayama, K., & Takemura, Y. (2000) · Acta Diabetologica · doi:10.1007/s005920070025 · Cited by 157 · see citing works
Hanssen, N. M. J., Beulens, J. W. J., van Dieren, S., Scheijen, J. L. J. M., van der A, D. L., Spijkerman, A. M. W., van der Schouw, Y. T., Stehouwer, C. D. A., & Schalkwijk, C. G. (2014) · Diabetes · doi:10.2337/db13-1864 · Cited by 156 · see citing works
An update on advanced glycation endproducts and atherosclerosis
Turco, S. D., & Basta, G. (2012) · BioFactors · doi:10.1002/biof.1018 · Cited by 154 · see citing works
Yamagishi, S., Inagaki, Y., Okamoto, T., Amano, S., Koga, K., & Takeuchi, M. (2003) · Kidney International · doi:10.1046/j.1523-1755.2003.00752.x · Cited by 151 · see citing works
Advanced Glycation End Products Are Direct Modulators of β-Cell Function
Coughlan, M. T., Yap, F. Y. T., Tong, D. C. K., Andrikopoulos, S., Gasser, A., Thallas‐Bonke, V., Webster, D. E., Miyazaki, J., Kay, T. W. H., Slattery, R. M., et al. (2011) · Diabetes · doi:10.2337/db10-1033 · Cited by 149 · see citing works
Miele, C., Riboulet, A., Maitan, M. A., Oriente, F., Romano, C., Formisano, P., Giudicelli, J., Bèguinot, F., & OBBERGHEN, E. V. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301088200 · Cited by 140 · see citing works
Zhao, Z., Zhao, C., Zhang, X. H., Zheng, F., Cai, W., Vlassara, H., & Ma, Z. A. (2009) · Endocrinology · doi:10.1210/en.2008-1342 · Cited by 132 · see citing works
Hirose, A., Tanikawa, T., Mori, H., Okada, Y., & Tanaka, Y. (2010) · FEBS Letters · doi:10.1016/j.febslet.2009.11.082 · Cited by 129 · see citing works
Increased serum levels of advanced glycation end-products and diabetic complications
Ono, Y., Aoki, S., Ohnishi, K., Yasuda, T., Kawano, K., & Tsukada, Y. (1998) · Diabetes Research and Clinical Practice · doi:10.1016/s0168-8227(98)00074-6 · Cited by 128 · see citing works
Advanced Glycation End Products Induce Blood–Retinal Barrier Dysfunction in Normoglycemic Rats
Stitt, A. W., Bhaduri, T., McMullen, C. B. T., Gardiner, T. A., & ARCHER, D. B. (2000) · Molecular Cell Biology Research Communications · doi:10.1006/mcbr.2000.0243 · Cited by 127 · see citing works
Kiuchi, K., Nejima, J., Takano, T., Ohta, M., & Hashimoto, H. (2001) · Heart · doi:10.1136/heart.85.1.87 · Cited by 127 · see citing works
Nakamura, K., Nakazawa, Y., & Ienaga, K. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.6262 · Cited by 122 · see citing works
Fosmark, D. S., Torjesen, P. A., Kilhovd, B. K., Berg, T. J., Sandvik, L., Hanssen, K. F., Agardh, C., & Agardh, E. (2006) · Metabolism · doi:10.1016/j.metabol.2005.08.017 · Cited by 122 · see citing works
Structural and functional changes in human insulin induced by methylglyoxal
Jia, X., Olson, D. J. H., Ross, A. R. S., & Wu, L. (2006) · The FASEB Journal · doi:10.1096/fj.05-5478fje · Cited by 122 · see citing works
Inagaki, Y., Yamagishi, S., Okamoto, T., Takeuchi, M., & Amano, S. (2003) · Diabetologia · doi:10.1007/s00125-002-1013-4 · Cited by 121 · see citing works
Xu, X., & Stern, D. F. (2003) · The FASEB Journal · doi:10.1096/fj.03-0310com · Cited by 120 · see citing works
N(carboxymethyl)lysine as a biomarker for microvascular complications in type 2 diabetic patients
Wautier, M.-P., Massin, P., Guillausseau, P.-J., Huijberts, M. S., Levy, B. I., Boulanger, É., Laloi-Michelin, M., & Wautier, J. (2003) · Diabetes & Metabolism · doi:10.1016/s1262-3636(07)70006-x · Cited by 120 · see citing works
Boehm, B. O., Schilling, S., Rosinger, S., Lang, G. E., Lang, G. K., Kientsch-Engel, R., & Stahl, P. (2004) · Diabetologia · doi:10.1007/s00125-004-1455-y · Cited by 119 · see citing works
Study of the urinary and faecal excretion of N ε-carboxymethyllysine in young human volunteers
Delgado‐Andrade, C., Tessier, F. J., Niquet‐Léridon, C., Seiquer, I., & Navarro, M. P. (2011) · Amino Acids · doi:10.1007/s00726-011-1107-8 · Cited by 118 · see citing works
Hanssen, N. M. J., Engelen, L., Ferreira, I., Scheijen, J. L. J. M., Huijberts, M. S., van Greevenbroek, M. M. J., Kallen, C., Dekker, J. M., Nijpels, G., Stehouwer, C. D. A., et al. (2013) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2013-1068 · Cited by 117 · see citing works
Tahara, N., Yamagishi, S., Matsui, T., Takeuchi, M., Nitta, Y., Kodama, N., Mizoguchi, M., & Imaizumi, T. (2012) · Cardiovascular Therapeutics · doi:10.1111/j.1755-5922.2010.00177.x · Cited by 116 · cited 3× · see citing works
“Insulin resistance was estimated by the homeostatic model assessment index (HOMA-IR) which is based on the calculation of fasting insulin and glucose concentration [76].”
BackgroundCassese, A., Esposito, I., Fiory, F., Barbagallo, A., Paturzo, F., Mirra, P., Ulianich, L., Giacco, F., Iadicicco, C., Lombardi, A., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801698200 · Cited by 116 · see citing works
Serum advanced glycation end products (AGEs) are associated with insulin resistance
Tan, K. C. B., Shiu, S. W. M., Wong, Y., & Tam, X. (2011) · Diabetes/Metabolism Research and Reviews · doi:10.1002/dmrr.1188 · Cited by 111 · see citing works
Hunter, S. J., Boyd, A. C., O'Harte, F. P. M., McKillop, A. M., Wiggam, M. I., Mooney, M. H., McCluskey, J. T., Lindsay, J. R., Ennis, C. N., Gamble, R., et al. (2003) · Diabetes · doi:10.2337/diabetes.52.2.492 · Cited by 111 · see citing works
α11 integrin stimulates myofibroblast differentiation in diabetic cardiomyopathy
Talior‐Volodarsky, I., Connelly, K. A., Arora, P. D., Gullberg, D., & McCulloch, C. A. (2012) · Cardiovascular Research · doi:10.1093/cvr/cvs259 · Cited by 110 · see citing works
Isolation and Characterization of Glyoxal−Arginine Modifications
Glomb, M. A., & Lang, G. (2001) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf001082d · Cited by 109 · see citing works
Connective Tissue Growth Factor Is Increased in Plasma of Type 1 Diabetic Patients With Nephropathy
Roestenberg, P., van Nieuwenhoven, F. A., Wieten, L., de Boer, P., Diekman, T., Tiller, A. M., Wiersinga, W. M., Oliver, N., Usinger, W. R., Weitz, S., et al. (2004) · Diabetes Care · doi:10.2337/diacare.27.5.1164 · Cited by 108 · see citing works
Henle, T., Walter, A. W., Hae�ner, R., & Klostermeyer, H. (1994) · European Food Research and Technology · doi:10.1007/bf01192954 · Cited by 107 · see citing works
Schalkwijk, C. G., Baidoshvili, A., Stehouwer, C. D. A., van Hinsbergh, V. W. M., & Niessen, H. W. M. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2003.07.002 · Cited by 107 · see citing works
Chen, J., Song, M., Yu, S., Gao, P., Yu, Y., Wang, H., & Huang, L. J. (2009) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-009-0250-y · Cited by 105 · see citing works
Advanced glycation end-products induce injury to pancreatic beta cells through oxidative stress
Lin, N., Zhang, H., & Su, Q. (2012) · Diabetes & Metabolism · doi:10.1016/j.diabet.2012.01.003 · Cited by 103 · see citing works
Guo, Q., Mori, T., Jiang, Y., Hu, C., Osaki, Y., Yoneki, Y., Sun, Y., Hosoya, T., Kawamata, A., Ogawa, S., et al. (2009) · Journal of Hypertension · doi:10.1097/hjh.0b013e32832c419a · Cited by 103 · see citing works
Nakajima, K., Yamauchi, K., Shigematsu, S., Ikeo, S., Komatsu, M., Aizawa, T., & Hashizume, K. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m905410199 · Cited by 103 · see citing works
Wells‐Knecht, K. J., Brinkmann, E., & Baynes, J. (1995) · The Journal of Organic Chemistry · doi:10.1021/jo00125a001 · Cited by 93 · see citing works
Grimm, S., Ott, C., Hörlacher, M., Weber, D., Höhn, A., & Grune, T. (2012) · Biochemical Journal · doi:10.1042/bj20120298 · Cited by 87 · see citing works
Self-citationChromatographic evidence for pyrraline formation during protein glycation in vitro and in vivo
Portero‐Otín, M., Nagaraj, R. H., & Monnier, V. M. (1995) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(94)00209-y · Cited by 86 · see citing works
Nɛ-(carboxymethyl)lysine in atherosclerotic vascular lesions as a marker for local oxidative stress
Nerlich, M. L. (1999) · Atherosclerosis · doi:10.1016/s0021-9150(99)00038-6 · Cited by 84 · see citing works
Glycation of Insulin in the Islets of Langerhans of Normal and Diabetic Animals
Abdel‐Wahab, Y. H. A., O'Harte, F. P. M., Ratcliff, H., McClenaghan, N. H., Barnett, C. R., & Flatt, P. R. (1996) · Diabetes · doi:10.2337/diab.45.11.1489 · Cited by 83 · see citing works
Methylglyoxal-modified collagen promotes myofibroblast differentiation
Yuen, A., Laschinger, C. A., Talior‐Volodarsky, I., Lee, W., Chan, M. K. W., Birek, J., Young, E. W. K., Sivagurunathan, K. S., Won, E., Simmons, C. A., et al. (2010) · Matrix Biology · doi:10.1016/j.matbio.2010.04.004 · Cited by 81 · see citing works
Lim, M., Park, L., Shin, G., Hong, H., Kang, I., & Park, Y. (2008) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1447.011 · Cited by 81 · see citing works
Inhibition of the receptor for advanced glycation endproducts (RAGE) protects pancreatic β-cells
Zhu, Y., Shu, T., Yan, L., Wang, H., Yang, J., Shi, Y., & Han, X. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.11.085 · Cited by 79 · see citing works
Cai, W., Torreggiani, M., Zhu, L., Chen, X., He, C., Striker, G. E., & Vlassara, H. (2009) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00463.2009 · Cited by 78 · see citing works
CHARONIS, A. S., Tsilibary, E. C., Saku, T., & Furthmayr, H. (1986) · The Journal of Cell Biology · doi:10.1083/jcb.103.5.1689 · Cited by 72 · see citing works
Identification of the site of glycation of human insulin
O'Harte, F. P. M., Højrup, P., Barnett, C. R., & Flatt, P. R. (1996) · Peptides · doi:10.1016/s0196-9781(96)00231-8 · Cited by 69 · see citing works
Mamputu, J., & Renier, G. (2002) · Journal of Diabetes and its Complications · doi:10.1016/s1056-8727(01)00229-x · Cited by 68 · see citing works
Sell, D. R., Carlson, E. C., & Monnier, V. M. (1993) · Diabetologia · doi:10.1007/bf02374476 · Cited by 67 · see citing works
Busch, M., Franke, S., Wolf, G., Brandstädt, A., Ott, U., Gerth, J., Hunsicker, L. G., & Stein, G. (2006) · American Journal of Kidney Diseases · doi:10.1053/j.ajkd.2006.07.009 · Cited by 63 · see citing works
Stitt, A. W., Hughes, S.-J., Canning, P., Lynch, O. T., Cox, Ó. T., Frizzell, N., Thorpe, S. R., Cotter, T. G., Curtis, T. M., & Gardiner, T. A. (2004) · Diabetologia · doi:10.1007/s00125-004-1523-3 · Cited by 62 · see citing works
Thornalley, P. J. (2007) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.200700017 · Cited by 62 · see citing works
Torreggiani, M., Liu, H., Wu, J. C., Zheng, F., Cai, W., Striker, G. E., & Vlassara, H. (2009) · American Journal Of Pathology · doi:10.2353/ajpath.2009.090138 · Cited by 60 · see citing works
Grimm, S., Ernst, L., Grötzinger, N., Höhn, A., Breusing, N., Reinheckel, T., & Grune, T. (2010) · Free Radical Research · doi:10.3109/10715762.2010.495127 · Cited by 59 · see citing works
Self-citationArguing for the motion: yes, RAGE is a receptor for advanced glycation endproducts
Ramasamy, R., Yan, S. F., & Schmidt, A. M. (2007) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.200700008 · Cited by 58 · see citing works
Boyd, A. C., Abdel‐Wahab, Y. H. A., McKillop, A. M., McNulty, H., Barnett, C. R., O'Harte, F. P. M., & Flatt, P. R. (2000) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/s0304-4165(00)00113-6 · Cited by 58 · see citing works
Methylglyoxal Inhibits the Binding Step of Collagen Phagocytosis
Chong, S., Lee, W., Arora, P. D., Laschinger, C. A., Young, E. W. K., Simmons, C. A., Manolson, M. F., Sodek, J., & McCulloch, C. A. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m609859200 · Cited by 58 · see citing works
Unoki‐Kubota, H., Yamagishi, S., Takeuchi, M., Bujo, H., & Saitō, Y. (2010) · Protein and Peptide Letters · doi:10.2174/092986610791760423 · Cited by 54 · see citing works
Cathepsins D and L reduce the toxicity of advanced glycation end products
Grimm, S., Hörlacher, M., Catalgol, B., Höhn, A., Reinheckel, T., & Grune, T. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.12.021 · Cited by 53 · see citing works
Self-citationShu, T., Zhu, Y., Wang, H., Lin, Y., Ma, Z., & Han, X. (2011) · PLoS ONE · doi:10.1371/journal.pone.0018782 · Cited by 51 · see citing works
Jono, T. (2004) · The Journal of Biochemistry · doi:10.1093/jb/mvh124 · Cited by 51 · see citing works
Effect of Dicarbonyl Modification of Fibronectin on Retinal Capillary Pericytes
Liu, B.-F., Bhat, M. B., Padival, A. K., Smith, D. G., & Nagaraj, R. H. (2004) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.03-0995 · Cited by 44 · see citing works
Modification of Collagen IV by Glucose or Methylglyoxal Alters Distinct Mesangial Cell Functions
Pozzi, A., Zent, R., Chetyrkin, S. V., Borza, C. M., Bulus, N. M., Chuang, P., Chen, D., Hudson, B. G., & Voziyan, P. (2009) · Journal of the American Society of Nephrology · doi:10.1681/asn.2008080900 · Cited by 43 · see citing works
Glycated fetal calf serum affects the viability of an insulin-secreting cell line in vitro
Viviani, G. L., Puddu, A., Sacchi, G., Garuti, A., Storace, D., Durante, A., Monacelli, F., & Odetti, P. R. (2008) · Metabolism · doi:10.1016/j.metabol.2007.08.020 · Cited by 42 · see citing works
Characterization of insulin glycation in insulin-secreting cells maintained in tissue culture
Abdel‐Wahab, Y. H. A., O'Harte, F. P. M., Barnett, C. R., & Flatt, P. R. (1997) · Journal of Endocrinology · doi:10.1677/joe.0.1520059 · Cited by 41 · see citing works
Degradation of oxidized and glycoxidized collagen: Role of collagen cross-linking
Nowotny, K., & Grune, T. (2013) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2013.12.007 · Cited by 41 · see citing works
Self-citationAdvanced Glycation End-Products affect transcription factors regulating insulin gene expression
Puddu, A., Storace, D., Odetti, P. R., & Viviani, G. L. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.03.152 · Cited by 40 · see citing works
Glycated Collagen Induces α11 Integrin Expression Through TGF‐β2 and Smad3
Talior‐Volodarsky, I., Arora, P. D., Wang, Y., Zeltz, C., Connelly, K. A., Gullberg, D., & McCulloch, C. A. (2014) · Journal of Cellular Physiology · doi:10.1002/jcp.24708 · Cited by 38 · see citing works
Inhibition of Fibronectin Binding to Matrix Components by Nonenzymatic Glycosylation
Cohen, M. P., & Ku, L. (1984) · Diabetes · doi:10.2337/diab.33.10.970 · Cited by 35 · see citing works
Miwa, S. (2008) · Humana Press eBooks · doi:10.1007/978-1-59745-420-9 · Cited by 34 · see citing works
Heizmann, C. W. (2007) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.200600284 · Cited by 32 · see citing works
Sassi‐Gaha, S., Loughlin, D. T., Kappler, F., Schwartz, M. L., Su, B.-W., Tobia, A. M., & Artlett, C. M. (2009) · Matrix Biology · doi:10.1016/j.matbio.2009.09.007 · Cited by 31 · see citing works
Naitoh, T., Kitahara, M., & Tsuruzoe, N. (2001) · Cellular Signalling · doi:10.1016/s0898-6568(01)00152-8 · Cited by 30 · see citing works
Zhou, Y., Wang, J. H., & Zhang, J. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.03.167 · Cited by 28 · see citing works
Al‐Abed, Y., & Bucala, R. (1995) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/0960-894x(95)00375-4 · Cited by 27 · see citing works
N-Terminal pyrazinones: a new class of peptide-bound advanced glycation end-products
Krause, R., K�hn, J., Penndorf, I., Knoll, K., & Henle, T. (2004) · Amino Acids · doi:10.1007/s00726-004-0102-8 · Cited by 26 · see citing works
Ghayur, M. N., Krepinsky, J. C., & Janssen, L. J. (2008) · PubMed · Cited by 21 · see citing works
Eye vessels saved by rescuing their pericyte partners
Antonetti, D. A. (2009) · Nature Medicine · doi:10.1038/nm1109-1248 · Cited by 19 · see citing works
Inhibitory effect of atorvastatin on AGE-induced HCAEC apoptosis by upregulating HSF-1 protein
Li, Y., Li, J., Cui, L., Lai, Y., Yao, Y., Zhang, Y., Pang, X., Wang, J., & Liu, X. (2013) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2013.03.035 · Cited by 17 · see citing works
Oxidative Stress in Type 2 Diabetes Mellitus
Abdul‐Ghani, M. A., & DeFronzo, R. A. (2008) · Humana Press eBooks · doi:10.1007/978-1-59745-420-9_11 · Cited by 10 · see citing works
Advanced glycation end products impair glucose‐induced insulin secretion from rat pancreatic β‐cells
Hachiya, H., Miura, Y., Inoue, K.-I., Park, K. H., Takeuchi, M., & Kubota, K. (2013) · Journal of Hepato-Biliary-Pancreatic Sciences · doi:10.1002/jhbp.12 · Cited by 10 · see citing works
Flagged first, then by citations
1 of the 172 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Association between insulin resistance and the development of cardiovascular disease
Ormazábal, V., Nair, S., Elfeky, O. W. M., Aguayo, C. R., Salomón, C., & Zuñiga, F. A. (2018) · Cardiovascular Diabetology · doi:10.1186/s12933-018-0762-4 · Cited by 2,344 · see citing works
Advanced Glycation End Products and Diabetes Mellitus: Mechanisms and Perspectives
Khalid, M., Petroianu, G. A., & Adem, A. (2022) · Biomolecules · doi:10.3390/biom12040542 · Cited by 931 · see citing works
González, P., Lozano, P., Ros, G., & Solano, F. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24119352 · Cited by 888 · see citing works
Twarda‐Clapa, A., Olczak, A., Białkowska, A. M., & Koziołkiewicz, M. (2022) · Cells · doi:10.3390/cells11081312 · Cited by 792 · see citing works
Giri, B., Dey, S., Das, T., Sarkar, M., Banerjee, J., & Dash, S. K. (2018) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2018.07.157 · Cited by 674 · see citing works
Sarcopenia and type 2 diabetes mellitus: a bidirectional relationship
Mesinovic, J., Zengin, A., de Courten, B. V., Ebeling, P. R., & Scott, D. S. (2019) · Diabetes Metabolic Syndrome and Obesity · doi:10.2147/dmso.s186600 · Cited by 584 · see citing works
Rehman, K., & Akash, M. S. H. (2017) · Journal of Cellular Biochemistry · doi:10.1002/jcb.26097 · Cited by 475 · see citing works
Perrone, A., Giovino, A., Benny, J., & Martinelli, F. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/3818196 · Cited by 459 · see citing works
Correlation between Oxidative Stress, Nutrition, and Cancer Initiation
Saha, S. K., Lee, S. B., Won, J., Choi, H. Y., Kim, K., Yang, G., Dayem, A. A., & Cho, S. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18071544 · Cited by 399 · see citing works
Insulin resistance and cardiovascular disease
Kosmas, C. E., Bousvarou, M. D., Kostara, C. E., Papakonstantinou, E. J., Salamou, E., & Guzman, E. (2023) · Journal of International Medical Research · doi:10.1177/03000605231164548 · Cited by 413 · see citing works
Oxidative stress: Normal pregnancy versus preeclampsia
Chiarello, D. I., Abad, C., Rojas, D., Toledo, F., Vázquez, C. M., Mate, A., Sobrevía, L., & Marı́n, R. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.12.005 · Cited by 394 · see citing works
Protein oxidation - Formation mechanisms, detection and relevance as biomarkers in human diseases
Kehm, R., Baldensperger, T., Raupbach, J., & Höhn, A. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101901 · Cited by 348 · see citing works
“This indicates their relevance in the progression of metabolic diseases, including neurodegenerative disease, chronic kidney disease (CDK), CVD, and cancer, but in particular, T2D and related complications as reviewed elsewhere [152].”
BackgroundSelf-citationNani, A., Murtaza, B., Sayed Khan, A., Khan, N. A., & Hichami, A. (2021) · Molecules · doi:10.3390/molecules26040985 · Cited by 321 · see citing works
Alzheimer's disease and type 2 diabetes: a critical assessment of the shared pathological traits
Chatterjee, S., & Mudher, A. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00383 · Cited by 270 · see citing works
Dietary advanced glycation end products and their relevance for human health
Nowotny, K., Schröter, D., Schreiner, M., & Grune, T. (2018) · Ageing Research Reviews · doi:10.1016/j.arr.2018.06.005 · Cited by 255 · see citing works
Self-citationChen, Y., Zhao, X., & Wu, H. (2020) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.120.313131 · Cited by 251 · see citing works
Pathophysiology of RAGE in inflammatory diseases
Dong, H., Zhang, Y., Huang, Y., & Deng, H. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.931473 · Cited by 245 · see citing works
Inflammation and Premature Ageing in Chronic Kidney Disease
Ebert, T., Pawelzik, S., Witasp, A., Arefin, S., Hobson, S., Kublickiene, K. R., Shiels, P. G., Bäck, M., & Stenvinkel, P. (2020) · Toxins · doi:10.3390/toxins12040227 · Cited by 242 · see citing works
Vitamin B12 in Relation to Oxidative Stress: A Systematic Review
van de Lagemaat, E. E., de Groot, C. P. G. M., & van den Heuvel, E. G. H. M. (2019) · Nutrients · doi:10.3390/nu11020482 · Cited by 238 · see citing works
Redox Signaling in Diabetic Wound Healing Regulates Extracellular Matrix Deposition
Kunkemoeller, B. H., & Kyriakides, T. R. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7263 · Cited by 236 · see citing works
Insulin Signal Transduction Perturbations in Insulin Resistance
Khalid, M., Alkaabi, J., Khan, M. A. B., & Adem, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22168590 · Cited by 233 · see citing works
Advanced Glycation End Products (AGEs) May Be a Striking Link Between Modern Diet and Health
Gill, V., Kumar, V., Singh, K., Kumar, A., & Kim, J.-J. (2019) · Biomolecules · doi:10.3390/biom9120888 · Cited by 232 · see citing works
Endogenous advanced glycation end products in the pathogenesis of chronic diabetic complications
Mengstie, M. A., Abebe, E. C., Teklemariam, A. B., Mulu, A. T., Agidew, M. M., Azezew, M. T., Zewde, E. A., & Teshome, A. A. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.1002710 · Cited by 209 · see citing works
Chaudhary, M. R., Chaudhary, S., Sharma, Y., Singh, T. A., Mishra, A. K., Sharma, S. G., & Mehdi, M. M. (2023) · Biogerontology · doi:10.1007/s10522-023-10050-1 · Cited by 210 · see citing works
Activation of Nrf2 signaling by natural products-can it alleviate diabetes?
Matzinger, M., Fischhuber, K., & Heiß, E. H. (2017) · Biotechnology Advances · doi:10.1016/j.biotechadv.2017.12.015 · Cited by 205 · see citing works
Lima, J. E. B. F., Moreira, N. C. S., & Sakamoto-Hojo, E. T. (2022) · Mutation Research/Genetic Toxicology and Environmental Mutagenesis · doi:10.1016/j.mrgentox.2021.503437 · Cited by 203 · see citing works
The Role of Dietary Advanced Glycation End Products in Metabolic Dysfunction
Sergi, D., Boulestin, H., Campbell, F. M., & Williams, L. M. (2021) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201900934 · Cited by 194 · see citing works
Barone, E., Domenico, F. D., Perluigi, M., & Butterfield, D. (2021) · Free Radical Biology & Medicine · doi:10.1016/j.freeradbiomed.2021.09.006 · Cited by 155 · see citing works
Sodium—Glucose cotransporter inhibitors and oxidative stress: An update
Yaribeygi, H., Atkin, S. L., Butler, A. E., & Sahebkar, A. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.26760 · Cited by 167 · see citing works
Chen, J.-H., Lin, X., Bu, C., & Zhang, X.-G. (2018) · Nutrition and Metabolism · doi:10.1186/s12986-018-0306-7 · Cited by 154 · see citing works
Byon, C. H., Heath, J. M., & Chen, Y. (2016) · Redox Biology · doi:10.1016/j.redox.2016.08.015 · Cited by 164 · see citing works
Multifaceted Mechanisms of Vascular Calcification in Aging
Pescatore, L. A., Gamarra, L. F., & Liberman, M. (2019) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.118.311576 · Cited by 164 · see citing works
Molecular mechanisms associated with diabetic endothelial–erectile dysfunction
Castela, Â., & Costa, C. (2016) · Nature Reviews Urology · doi:10.1038/nrurol.2016.23 · Cited by 160 · see citing works
Glycemic variability in the development of cardiovascular complications in diabetes
Nusca, A., Tuccinardi, D., Albano, M., Cavallaro, C., Ricottini, E., Manfrini, S., Pozzilli, P., & Sciascio, G. D. (2018) · Diabetes/Metabolism Research and Reviews · doi:10.1002/dmrr.3047 · Cited by 157 · see citing works
Recent advances in the neurobiology and neuropharmacology of Alzheimer’s disease
Kumar, K., Kumar, A., Keegan, R. M., & Deshmukh, R. R. (2017) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2017.12.053 · Cited by 153 · see citing works
Anwar, S., Khan, A. A., Almatroudi, A., Khan, A. A., Alsahli, M. A., Almatroodi, S. A., & Rahmani, A. H. (2021) · Molecular Biology Reports · doi:10.1007/s11033-020-06084-0 · Cited by 158 · see citing works
Ferlita, S., Yegiazaryan, A., Noori, N., Lal, G., Nguyen, T. K., To, K., & Venketaraman, V. (2019) · Journal of Clinical Medicine · doi:10.3390/jcm8122219 · Cited by 151 · see citing works
Recent Advances in Diabetic Kidney Diseases: From Kidney Injury to Kidney Fibrosis
Hung, P., Hsu, Y., Chen, T., & Lin, C. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222111857 · Cited by 152 · see citing works
The impact of diabetes on corneal nerve morphology and ocular surface integrity
Markoulli, M. P., Flanagan, J., Tummanapalli, S. S., Wu, J., & Willcox, M. D. P. (2017) · The Ocular Surface · doi:10.1016/j.jtos.2017.10.006 · Cited by 149 · see citing works
Caffeine and Its Antioxidant Properties—It Is All about Dose and Source
Ősz, B.-E., Jîtcă, G., Ștefănescu, R., Puşcaş, A., Tero-Vescan, A., & Vari, C.-E. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232113074 · Cited by 146 · see citing works
The Regulation of Selenoproteins in Diabetes: A New Way to Treat Diabetes
Liang, J., He, Y., Huang, C., Ji, F., Zhou, X., & Yin, Y. (2024) · Current Pharmaceutical Design · doi:10.2174/0113816128302667240422110226 · Cited by 146 · see citing works
An overview on glycation: molecular mechanisms, impact on proteins, pathogenesis, and inhibition
Uceda, A. B., Mariño, L., Casasnovas, R., & Adrover, M. (2024) · Biophysical Reviews · doi:10.1007/s12551-024-01188-4 · Cited by 162 · see citing works
Vitamin B6 and Diabetes: Relationship and Molecular Mechanisms
Mascolo, E., & Vernı̀, F. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21103669 · Cited by 143 · see citing works
Dowey, R., Iqbal, A., Heller, S. R., Sabroe, I., & Prince, L. R. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.678771 · Cited by 144 · see citing works
Caturano, A., Rocco, M. P., Tagliaferri, G., Piacevole, A., Nilo, D., Lorenzo, G. D., Iadicicco, I., Donnarumma, M., Galiero, R., Acierno, C., et al. (2025) · Antioxidants · doi:10.3390/antiox14010072 · Cited by 162 · see citing works
Oxidative stress in cardiac hypertrophy: From molecular mechanisms to novel therapeutic targets
Ramachandra, C. J. A., Cong, S., Chan, X., Yap, E. P., Fan, Y., & Hausenloy, D. J. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.02.040 · Cited by 140 · see citing works
Physical activity and exercise attenuate neuroinflammation in neurological diseases
Spielman, L. J., Little, J. P., & Klegeris, A. (2016) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2016.03.012 · Cited by 136 · see citing works
Tessier, F. J., Niquet‐Léridon, C., Jacolot, P., Jouquand, C., Génin, M., Schmidt, A., Grossin, N., & Boulanger, É. (2016) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201600140 · Cited by 132 · see citing works
AGE-RAGE synergy influences programmed cell death signaling to promote cancer
Waghela, B. N., Vaidya, F. U., Ranjan, K., Chhipa, A. S., Tiwari, B. S., & Pathak, C. (2020) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-020-03928-y · Cited by 134 · see citing works
Role of advanced glycation end products in carcinogenesis and their therapeutic implications
Schröter, D., & Höhn, A. (2019) · Current Pharmaceutical Design · doi:10.2174/1381612825666190130145549 · Cited by 126 · see citing works
Self-citationRole of Cellular Senescence in Type II Diabetes
Narasimhan, A., Flores, R. R., Robbins, P. D., & Niedernhofer, L. J. (2021) · Endocrinology · doi:10.1210/endocr/bqab136 · Cited by 133 · see citing works
The importance of nutritional factors and dietary management of Hashimoto’s thyroiditis
Ihnatowicz, P., Drywień, M. E., Wątor, P., & Wojsiat, J. (2019) · Annals of Agricultural and Environmental Medicine · doi:10.26444/aaem/112331 · Cited by 129 · see citing works
Feng, J., Wang, J., Wang, Y., Huang, X., Shao, T., Deng, X., Cao, Y., Zhou, M., & Zhao, C. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.898657 · Cited by 126 · see citing works
Influence of diabetes mellitus on anterior segment of the eye
Han, S. B., Yang, H. K., & Hyon, J. Y. (2018) · Clinical Interventions in Aging · doi:10.2147/cia.s190713 · Cited by 121 · see citing works
Mitochondrial ROS and mitochondria-targeted antioxidants in the aged heart
Bou‐Teen, D., Kaludercic, N., Weissman, D., Turan, B., Maack, C., Lisa, F. D., & Ruiz‐Meana, M. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.02.043 · Cited by 119 · see citing works
Autophagy and its link to type II diabetes mellitus
Yang, J., Lu, C., Kuo, S., Hsu, Y., Tsai, S. C., Chen, S.-Y., Chen, Y., Lin, Y.-J., Huang, Y.-C., Chen, C., et al. (2017) · Biomedicine · doi:10.1051/bmdcn/2017070201 · Cited by 116 · see citing works
Jubaidi, F. F., Zainalabidin, S., Taib, I. S., Hamid, Z. A., Anuar, N. N. M., Jalil, J., Nor, N. A. M., & Budin, S. B. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23158582 · Cited by 114 · see citing works
Reynaert, N. L., Gopal, P., Rutten, E. P. A., Wouters, E. F. �., & Schalkwijk, C. G. (2016) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2016.06.016 · Cited by 111 · see citing works
The Warburg Effect in Diabetic Kidney Disease
Zhang, G., Darshi, M., & Sharma, K. (2018) · Seminars in Nephrology · doi:10.1016/j.semnephrol.2018.01.002 · Cited by 106 · see citing works
Urbaniak, S. K., Boguszewska, K., Szewczuk, M., Kaźmierczak-Barańska, J., & Karwowski, B. T. (2020) · Molecules · doi:10.3390/molecules25010202 · Cited by 100 · see citing works
Can Meat and Meat-Products Induce Oxidative Stress?
Macho‐González, A., Garcimartín, A., López‐Oliva, M. E., Bastida, S., Benedı́, J., Ros, G., Nieto, G., & Sánchez-Muniz, F. J. (2020) · Antioxidants · doi:10.3390/antiox9070638 · Cited by 106 · see citing works
Barteková, M., Adameová, A., Görbe, A., Ferenczyová, K., Pecháňová, O., Lazou, A., Dhalla, N. S., Ferdinandy, P., & Giricz, Z. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.03.045 · Cited by 98 · see citing works
Role of advanced glycation end products and insulin resistance in diabetic nephropathy
Parwani, K., & Mandal, P. (2020) · Archives of Physiology and Biochemistry · doi:10.1080/13813455.2020.1797106 · Cited by 97 · see citing works
Vascular endothelium in diabetes
Goligorsky, M. S. (2016) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00473.2016 · Cited by 96 · see citing works
Metabolic Effects of Metformin in the Failing Heart
Dziubak, A., Wójcicka, G., Wojtak, A., & Bełtowski, J. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19102869 · Cited by 96 · see citing works
Cellular senescence of renal tubular epithelial cells in acute kidney injury
Chen, J., Zhang, H., Yi, X., Dou, Q., Yang, X., Chen, J., Chen, J., & Chen, K. (2024) · Cell Death Discovery · doi:10.1038/s41420-024-01831-9 · Cited by 97 · see citing works
The Role of Mitochondria in Diabetic Kidney Disease
Hallan, S. I., & Sharma, K. (2016) · Current Diabetes Reports · doi:10.1007/s11892-016-0748-0 · Cited by 94 · see citing works
Shpakov, A. O., Derkach, K. V., & Berstein, L. M. (2015) · Future Science OA · doi:10.4155/fso.15.23 · Cited by 92 · see citing works
Accumulation of carboxymethyl-lysine (CML) in human cortical bone
Thomas, C. J., Cleland, T. P., Sroga, G. E., & Vashishth, D. (2018) · Bone · doi:10.1016/j.bone.2018.01.028 · Cited by 92 · see citing works
Zepeda-Hernández, A., García-Amezquita, L. E., Requena, T., & García‐Cayuela, T. (2021) · Food Research International · doi:10.1016/j.foodres.2021.110208 · Cited by 92 · see citing works
Exploring inflammatory and fibrotic mechanisms driving diabetic nephropathy progression
Ansari, Z., Chaurasia, A., Neha, Sharma, N., Bachheti, R. K., & Gupta, P. C. (2025) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2025.05.007 · Cited by 91 · see citing works
Advanced glycation end products promote osteoporosis by inducing ferroptosis in osteoblasts
Ge, W., Jie, J., Yao, J., Li, W., Cheng, Y., & Lu, W. (2022) · Molecular Medicine Reports · doi:10.3892/mmr.2022.12656 · Cited by 84 · see citing works
López-Pedrosa, J. M., Camprubí-Robles, M., Rolo, G. G., Lopez-Gonzalez, A., García‐Almeida, J. M., Sanz‐París, A., & Rueda, R. (2024) · Nutrients · doi:10.3390/nu16010172 · Cited by 91 · see citing works
mTORC1 Overactivation as a Key Aging Factor in the Progression to Type 2 Diabetes Mellitus
Guillén, C., & Benito, M. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00621 · Cited by 81 · see citing works
Salleh, N. N. H. N., Othman, F. A., Kamarudin, N. A., & Tan, S. C. (2020) · Molecules · doi:10.3390/molecules25235677 · Cited by 88 · see citing works
Ansari, P., Khan, J. T., Chowdhury, S., Reberio, A. D., Kumar, S., Seidel, V., Abdel‐Wahab, Y. H. A., & Flatt, P. R. (2024) · Nutrients · doi:10.3390/nu16213709 · Cited by 106 · see citing works
Rohowetz, L. J., Kraus, J. G., & Koulen, P. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19113362 · Cited by 89 · see citing works
SGLT2 Inhibitors as Potential Anticancer Agents
Basak, D., Gamez, D., & Deb, S. (2023) · Biomedicines · doi:10.3390/biomedicines11071867 · Cited by 87 · see citing works
Diabetes, a Contemporary Risk for Parkinson’s Disease: Epidemiological and Cellular Evidences
Sergi, D., Renaud, J., Simola, N., & Martinoli, M. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00302 · Cited by 85 · see citing works
Gembillo, G., Ingrasciotta, Y., Crisafulli, S., Luxi, N., Siligato, R., Santoro, D., & Trifirò, G. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094824 · Cited by 96 · see citing works
An Update on Type 2 Diabetes Mellitus as a Risk Factor for Dementia
Li, W., & Huang, E. S. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160114 · Cited by 87 · see citing works
Borujeni, M. J. S., Esfandiary, E., Baradaran, A., Valiani, A., Ghanadian, M., Codoñer‐Franch, P., Basirat, R., Alonso‐Iglesias, E., Mirzaei, H., & Yazdani, A. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.27755 · Cited by 86 · see citing works
β cell aging and age-related diabetes
Zhu, M., Liu, X., Liu, W., Lu, Y., Cheng, J., & Chen, Y. (2021) · Aging · doi:10.18632/aging.202593 · Cited by 85 · see citing works
Sampath, C., Rashid, M. R., Sang, S., & Ahmedna, M. (2017) · Food Chemistry · doi:10.1016/j.foodchem.2017.01.056 · Cited by 85 · see citing works
Zhang, S., Qi, Z., Wang, Y., Song, D., & Zhu, D. (2023) · Frontiers in Endocrinology · doi:10.3389/fendo.2023.1203666 · Cited by 86 · see citing works
Mitochondrial Dysfunction: Cause or Consequence of Vascular Calcification?
Phadwal, K., Vrahnas, C., Ganley, I. G., & MacRae, V. E. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.611922 · Cited by 83 · see citing works
Mechanisms of Diabetes-Induced Endothelial Cell Senescence: Role of Arginase 1
Shosha, E., Xu, Z., Narayanan, S. P., Lemtalsi, T., Fouda, A. Y., Rojas, M., Ji, X., Fulton, D. J., Caldwell, R. W., & Caldwell, R. B. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19041215 · Cited by 82 · see citing works
Fighting Oxidative Stress with Sulfur: Hydrogen Sulfide in the Renal and Cardiovascular Systems
Scammahorn, J. J., Nguyen, I., Bos, E. M., van Goor, H., & Joles, J. A. (2021) · Antioxidants · doi:10.3390/antiox10030373 · Cited by 82 · see citing works
Antognelli, C., Trapani, E., Monache, S. D., Perrelli, A., Daga, M., Pizzimenti, S., Barrera, G., Cassoni, P., Angelucci, A., Trabalzini, L., et al. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.11.014 · Cited by 81 · see citing works
Samakkarnthai, P., Sfeir, J. G., Atkinson, E. J., Achenbach, S. J., Wennberg, P. W., Dyck, P. J. B., Tweed, A. J., Volkman, T. L., Amin, S., Farr, J. N., et al. (2020) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/clinem/dgaa388 · Cited by 82 · see citing works
Role of Pyroptosis in Diabetes and Its Therapeutic Implications
Mamun, A. A., Wu, Y., Nasrin, F., Akter, A., Taniya, M. A., Munir, F., Jia, C., & Xiao, J. (2021) · Journal of Inflammation Research · doi:10.2147/jir.s291453 · Cited by 81 · see citing works
Gentile, D., Fornai, M., Pellegrini, C., Colucci, R., Blandizzi, C., & Antonioli, L. (2018) · Nutrition Research Reviews · doi:10.1017/s0954422418000082 · Cited by 80 · see citing works
Understanding the Role of Protein Glycation in the Amyloid Aggregation Process
Sirangelo, I., & Iannuzzi, C. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22126609 · Cited by 82 · see citing works
Dutta, S., Saha, S., Mahalanobish, S., Sadhukhan, P., & Sil, P. C. (2018) · Food and Chemical Toxicology · doi:10.1016/j.fct.2018.05.032 · Cited by 78 · see citing works
Olive Oil Nutraceuticals in the Prevention and Management of Diabetes: From Molecules to Lifestyle
AlKhatib, A. H., Tsang, C., & Tuomilehto, J. O. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19072024 · Cited by 79 · see citing works
Advanced Glycation End-Products and Their Effects on Gut Health
Phuong-Nguyen, K., McNeill, B. A., Aston‐Mourney, K., & Rivera, L. R. (2023) · Nutrients · doi:10.3390/nu15020405 · Cited by 78 · see citing works
The Effects of Dietary Advanced Glycation End-Products on Neurocognitive and Mental Disorders
D'Cunha, N. M., Sergi, D., Lane, M. M., Naumovski, N., Gamage, E., Rajendran, A., Kouvari, M., Gauci, S., Dissanayaka, T. D., Marx, W., et al. (2022) · Nutrients · doi:10.3390/nu14122421 · Cited by 80 · see citing works
Ellagic Acid as a Tool to Limit the Diabetes Burden: Updated Evidence
Amor, A. J., Gómez‐Guerrero, C., Ortega, E., Sala‐Vila, A., & Lázaro, I. (2020) · Antioxidants · doi:10.3390/antiox9121226 · Cited by 74 · see citing works
Kong, Y., Wang, F., Wang, J., Liu, C., Zhou, Y., Xu, Z., Zhang, C., Sun, B., & Guan, Y. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.00217 · Cited by 74 · see citing works
Da Moura Semedo, C., Webb, M., Waller, H., Khunti, K., & Davies, M. (2017) · Postgraduate Medical Journal · doi:10.1136/postgradmedj-2016-134579 · Cited by 81 · see citing works
- Authors
- Nowotny, K., Jung, T., Höhn, A., Weber, D., & Grune, T.
- Affiliations
- German Institute of Human Nutrition (DE)
- Corresponding author
- Grune, Tilman
- Venue
- Biomolecules
- Publisher
- MDPI AG
- Published
- 2015-03-16
- Volume
- 5
- Issue
- 1
- Pages
- 194-222
- ISSN
- 2218-273X (ISSN-L)
- PMC
- PMC4384119
- OpenAlex
- W1986014108
- Cited by
- 1,095
- References
- 172
- Citations by year
- 2026: 59 · 2025: 93 · 2024: 106 · 2023: 138 · 2022: 132 · 2021: 118 · 2020: 106 · 2019: 99 · 2018: 99 · 2017: 68 · 2016: 61 · 2015: 14
- FWCI
- 8.00
- Type
- journal article
- Language
- en
- Open access
- gold
- dx.doi.org
- Licence
- Locations
- Biomolecules (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Informationszentrum Lebenswissenschaften (ZB MED) (submittedVersion, cc-by)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
- Life Sciences › Agricultural and Biological Sciences › Food Science › Potato Plant Research
- Health Sciences › Medicine › Nephrology › Chronic Kidney Disease and Diabetes
- Keywords
- advanced glycation end products, oxidative stress, type 2 diabetes, hyperglycemia, reactive oxygen species, antioxidant defense, diabetes complications, insulin resistance, beta-cell failure
- MeSH terms
- Animals, Diabetes Mellitus, Type 2, Humans, Insulin Resistance, Cell Death, Glycation End Products, Advanced, Oxidative Stress, Insulin-Secreting Cells
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
