A Perspective on the Maillard Reaction and the Analysis of Protein Glycation by Mass Spectrometry: Probing the Pathogenesis of Chronic Disease

Large-scale analysis of the yeast proteome by multidimensional protein identification technology

Washburn, M. P., Wolters, D. A., & Yates, J. R. (2001) · Nature Biotechnology · doi:10.1038/85686 · Cited by 4,759 · see citing works

Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry

Syka, J. E. P., Coon, J. J., Schroeder, M. J., Shabanowitz, J., & Hunt, D. F. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0402700101 · Cited by 2,370 · 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

Cloning and expression of a cell surface receptor for advanced glycosylation end products of proteins.

Neeper, M. P., Schmidt, A. M., Brett, J., Yan, S. D., Wang, F., Pan, Y., Elliston, K. O., Stern, D., & SHAW, A. R. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42138-2 · Cited by 1,542 · see citing works

The Human Plasma Proteome

Anderson, N. L., Polanski, M., Pieper, R., Gatlin, T., Tirumalai, R. S., Conrads, T. P., Veenstra, T. D., Adkins, J., Pounds, J. G., Fagan, R. J., et al. (2004) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m300127-mcp200 · Cited by 1,004 · see citing works

Advanced glycation end products and vascular inflammation: implications for accelerated atherosclerosis in diabetes

Basta, G. (2004) · Cardiovascular Research · doi:10.1016/j.cardiores.2004.05.001 · Cited by 996 · see citing works

The Role of Advanced Glycation End Products in Progression and Complications of Diabetes

Goh, S.-Y., & Cooper, M. E. (2008) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2007-1817 · Cited by 987 · see citing works

Electron Capture Dissociation for Structural Characterization of Multiply Charged Protein Cations

Zubarev, R. A., Horn, D. M., Fridriksson, E. K., Kelleher, N. L., Kruger, N. A., Lewis, M. A., Carpenter, B. K., & McLafferty, F. W. (2000) · Analytical Chemistry · doi:10.1021/ac990811p · Cited by 986 · see citing works

Effect of Collagen Turnover on the Accumulation of Advanced Glycation End Products

Verzijl, N., DeGroot, J., Thorpe, S. R., Bank, R. A., Shaw, J., Lyons, T. J., Bijlsma, J. W. J., Lafeber, F. P. J. G., Baynes, J., & TeKoppele, J. M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m006700200 · Cited by 964 · see citing works

Isolation and characterization of two binding proteins for advanced glycosylation end products from bovine lung which are present on the endothelial cell surface.

Schmidt, A. M., Vianna, M., Gerlach, M. L., Brett, J., Ryan, J., Kao, J. J., Esposito, C., Hegarty, H. M., Hurley, W. L., & Clauss, M. A. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42137-0 · Cited by 833 · see citing works

Orally absorbed reactive glycation products (glycotoxins): an environmental risk factor in diabetic nephropathy

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

Mass spectrometry for proteomics

Han, X., Aslanian, A., & Yates, J. R. (2008) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2008.07.024 · Cited by 743 · see citing works

New Aspects of the Maillard Reaction in Foods and in the Human Body

Ledl, F., & Schleicher, E. D. (1990) · Angewandte Chemie International Edition in English · doi:10.1002/anie.199005653 · Cited by 738 · see citing works

The biology of the receptor for advanced glycation end products and its ligands

Schmidt, A. M., Yan, S. D., Yan, S. F., & Stern, D. M. (2000) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/s0167-4889(00)00087-2 · Cited by 687 · see citing works

Inflammatory mediators are induced by dietary glycotoxins, a major risk factor for diabetic angiopathy

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

Quantitative screening of advanced glycation endproducts in cellular and extracellular proteins by tandem mass spectrometry

Thornalley, P. J., Battah, S., Ahmed, N., Karachalias, N., Agalou, S., Babaei‐Jadidi, R., & Dawnay, A. (2003) · Biochemical Journal · doi:10.1042/bj20030763 · Cited by 659 · see citing works

The dynamic range of protein expression: A challenge for proteomic research

Corthals, G. L., Wasinger, V. C., Hochstrasser, D. F., & Sanchez, J. (2000) · Electrophoresis · doi:10.1002/(sici)1522-2683(20000401)21:6 · Cited by 615 · 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

Alterations in nonenzymatic biochemistry in uremia: Origin and significance of “carbonyl stress” in long-term uremic complications

Miyata, T., de Strihou, C. V. Y., Kurokawa, K., & Baynes, J. (1999) · Kidney International · doi:10.1046/j.1523-1755.1999.00302.x · Cited by 518 · see citing works

Glycoxidation and lipoxidation in atherogenesis

Baynes, J., & Thorpe, S. R. (2000) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00228-8 · Cited by 515 · see citing works

The human serum proteome: Display of nearly 3700 chromatographically separated protein spots on two‐dimensional electrophoresis gels and identification of 325 distinct proteins

Pieper, R., Gatlin, C. L., Makusky, A. J., Russo, P. S., Schatz, C. R., Miller, S. S., Su, Q., McGrath, A. M., Estock, M. A., Parmar, P. P., et al. (2003) · PROTEOMICS · doi:10.1002/pmic.200300449 · Cited by 514 · see citing works

Glycation, Inflammation, and RAGE: A Scaffold for the Macrovascular Complications of Diabetes and Beyond

Yan, S. F., Ramasamy, R., Naka, Y., & Schmidt, A. M. (2003) · Circulation Research · doi:10.1161/01.res.0000103862.26506.3d · Cited by 513 · see citing works

Glycation and Carboxymethyllysine Levels in Skin Collagen Predict the Risk of Future 10-Year Progression of Diabetic Retinopathy and Nephropathy in the Diabetes Control and Complications Trial and Epidemiology of Diabetes Interventions and Complications Participants With Type 1 Diabetes

GENUTH, S. M., Sun, W., Cleary, P. A., Sell, D. R., Dahms, W. T., Malone, J. I., Sivitz, W. I., Monnier, V. M., & for the DCCT Skin Collagen Ancillary Study Group (2005) · Diabetes · doi:10.2337/diabetes.54.11.3103 · Cited by 428 · see citing works

Performance Characteristics of Electron Transfer Dissociation Mass Spectrometry

Good, D. M., Wirtala, M., McAlister, G. C., & Coon, J. J. (2007) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m700073-mcp200 · Cited by 397 · see citing works

Chemical Characterization and Antioxidant Properties of Coffee Melanoidins

Borrelli, R. C., Visconti, A., Mennella, C., Anese, M., & Fogliano, V. (2002) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf025686o · Cited by 384 · see citing works

A Neutral Loss Activation Method for Improved Phosphopeptide Sequence Analysis by Quadrupole Ion Trap Mass Spectrometry

Schroeder, M. J., Shabanowitz, J., Schwartz, J. C., Hunt, D. F., & Coon, J. J. (2004) · Analytical Chemistry · doi:10.1021/ac0497104 · Cited by 376 · see citing works

Effect of Roasting on the Antioxidant Activity of Coffee Brews

del Castillo, M. D., Ames, J. M., & Gordon, M. H. (2002) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf011702q · Cited by 372 · see citing works

Advanced glycation endproducts: what is their relevance to diabetic complications?

Ahmed, N., & Thornalley, P. J. (2006) · Diabetes Obesity and Metabolism · doi:10.1111/j.1463-1326.2006.00595.x · Cited by 369 · see citing works

Sites of nonenzymatic glycosylation of human hemoglobin A.

Shapiro, R., McManus, M., Zalut, C., & Bunn, H. F. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)85860-x · Cited by 368 · see citing works

Supplemental Activation Method for High-Efficiency Electron-Transfer Dissociation of Doubly Protonated Peptide Precursors

Swaney, D. L., McAlister, G. C., Wirtala, M., Schwartz, J. C., Syka, J. E. P., & Coon, J. J. (2006) · Analytical Chemistry · doi:10.1021/ac061457f · Cited by 364 · see citing works

Advances and Challenges in Liquid Chromatography-Mass Spectrometry-based Proteomics Profiling for Clinical Applications

Qian, W., Jacobs, J., Liu, T., Camp, D., & Smith, R. D. (2006) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m600162-mcp200 · Cited by 363 · see citing works

Glycation of mitochondrial proteins from diabetic rat kidney is associated with excess superoxide formation

Rosca, M. G., Mustata, T. G., Kinter, M. T., Ozdemir, A. M., Kern, T. S., Szweda, L. I., Brownlee, M., Monnier, V. M., & Weiss, M. F. (2005) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00415.2004 · Cited by 354 · see citing works

Age-related accumulation of Maillard reaction products in human articular cartilage collagen

Verzijl, N., DeGroot, J., OLDEHINKEL, E., Bank, R. A., Thorpe, S. R., Baynes, J., Bayliss, M. T., Bijlsma, J. W. J., Lafeber, F. P. J. G., & TeKoppele, J. M. (2000) · Biochemical Journal · doi:10.1042/bj3500381 · Cited by 345 · see citing works

Relating Electrospray Ionization Response to Nonpolar Character of Small Peptides

Cech, N. B., & Enke, C. G. (2000) · Analytical Chemistry · doi:10.1021/ac9914869 · Cited by 342 · see citing works

Extending Top-Down Mass Spectrometry to Proteins with Masses Greater Than 200 Kilodaltons

Han, X., Jin, M., Breuker, K., & McLafferty, F. W. (2006) · Science · doi:10.1126/science.1128868 · Cited by 328 · see citing works

The principal site of nonenzymatic glycosylation of human serum albumin in vivo.

Garlick, R., & Mazer, J. S. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)32384-6 · Cited by 316 · see citing works

Peptide Mapping Identifies Hotspot Site of Modification in Human Serum Albumin by Methylglyoxal Involved in Ligand Binding and Esterase Activity

Ahmed, N., Dobler, D., Dean, M., & Thornalley, P. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m410973200 · Cited by 314 · see citing works

Advances in proteomics data analysis and display using an accurate mass and time tag approach

Zimmer, J. S. D., Monroe, M. E., Qian, W., & Smith, R. D. (2006) · Mass Spectrometry Reviews · doi:10.1002/mas.20071 · Cited by 305 · see citing works

Improved Insulin Sensitivity Is Associated With Restricted Intake of Dietary Glycoxidation Products in the db / db Mouse

Hofmann, S. M., Dong, H. H., Li, Z., Cai, W., Altomonte, J., Thung, S. N., Zeng, F., Fisher, E. A. A., & Vlassara, H. (2002) · Diabetes · doi:10.2337/diabetes.51.7.2082 · Cited by 296 · see citing works

Maillard Reaction

Nürsten, H. E. (2005) · Royal Society of Chemistry eBooks · doi:10.1039/9781847552570 · Cited by 284 · see citing works

Glyoxalase‐1 prevents mitochondrial protein modification and enhances lifespan in Caenorhabditis elegans

Morcos, M., Du, X., Pfisterer, F., Hutter, H., Sayed, A. A. R., Thornalley, P. J., Ahmed, N., Baynes, J., Thorpe, S. R., Kukudov, G., et al. (2008) · Aging Cell · doi:10.1111/j.1474-9726.2008.00371.x · Cited by 276 · see citing works

Increased Dicarbonyl Metabolism in Endothelial Cells in Hyperglycemia Induces Anoikis and Impairs Angiogenesis by RGD and GFOGER Motif Modification

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

Charge competition and the linear dynamic range of detection in electrospray ionization mass spectrometry

Tang, K., Page, J. S., & Smith, R. (2004) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2004.04.034 · Cited by 262 · see citing works

Protein-bound advanced glycation endproducts (AGEs) as bioactive amino acid derivatives in foods

Henle, T. (2005) · Amino Acids · doi:10.1007/s00726-005-0200-2 · Cited by 253 · see citing works

Structural heterogeneity of human hemoglobin A due to nonenzymatic glycosylation.

Bunn, H. F., Shapiro, R., McManus, M., Garrick, L. M., McDonald, M. J., Gallop, P. M., & Gabbay, K. H. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)50671-2 · Cited by 247 · see citing works

Pervasive combinatorial modification of histone H3 in human cells

Garcia, B. A., Pesavento, J. J., Mizzen, C. A., & Kelleher, N. L. (2007) · Nature Methods · doi:10.1038/nmeth1052 · Cited by 242 · see citing works

Human and rat mesangial cell receptors for glucose-modified proteins: potential role in kidney tissue remodelling and diabetic nephropathy.

Skolnik, E. Y., Yang, Z., Makita, Z., Radoff, S., Kirstein, M., & Vlassara, H. (1991) · The Journal of Experimental Medicine · doi:10.1084/jem.174.4.931 · Cited by 242 · see citing works

Changes in biomechanical properties, composition of collagen and elastin, and advanced glycation endproducts of the rat aorta in relation to age

Brüel, A., & Oxlund, H. (1996) · Atherosclerosis · doi:10.1016/s0021-9150(96)05947-3 · Cited by 232 · see citing works

Renal catabolism of advanced glycation end products: the fate of pentosidine

Miyata, T., Ueda, Y., Horie, K., Nangaku, M., Tanaka, S., de Strihou, C. V. Y., & Kurokawa, K. (1998) · Kidney International · doi:10.1046/j.1523-1755.1998.00756.x · Cited by 227 · see citing works

Identification and Quantification of Major Maillard Cross-links in Human Serum Albumin and Lens Protein

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

Evaluation of Multiprotein Immunoaffinity Subtraction for Plasma Proteomics and Candidate Biomarker Discovery Using Mass Spectrometry

Liu, T., Qian, W., Mottaz, H. M., Gritsenko, M. A., Norbeck, A. D., Moore, R. J., Purvine, S. O., Camp, D., & Smith, R. D. (2006) · Molecular & Cellular Proteomics · doi:10.1074/mcp.t600039-mcp200 · Cited by 208 · see citing works

Formation of a Nonaoxirane from A2E, a Lipofuscin Fluorophore related to Macular Degeneration, and Evidence of Singlet Oxygen Involvement This work was supported by NIH grant GM 34509 (K.N.), NSF grant NSF-CHE-98-12676 (N.J.T. and S.J.), and NIH grant EY-12951 (J.R.S.).

Ben‐Shabat, S., Itagaki, Y., Steffen Jockusch, B., Sparrow, J. R., Turro, N. J., & Nakanishi, K. (2002) · Angewandte Chemie International Edition · doi:10.1002/1521-3773(20020301)41:5 · Cited by 207 · see citing works

Control of the Maillard reaction in food systems

Ames, J. M. (1990) · Trends in Food Science & Technology · doi:10.1016/0924-2244(90)90113-d · Cited by 207 · see citing works

A study in glycation of a therapeutic recombinant humanized monoclonal antibody: Where it is, how it got there, and how it affects charge-based behavior

Quan, C. P., Alcala, E. W., Petkovska, I., Matthews, D., Canova‐Davis, E., Taticek, R., & Ma, S. (2007) · Analytical Biochemistry · doi:10.1016/j.ab.2007.09.027 · Cited by 206 · see citing works

Formation and Reduction of Acrylamide in Maillard Reaction: A Review Based on the Current State of Knowledge

Zhang, Y., & Zhang, Y. Q. (2007) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408390600920070 · Cited by 194 · see citing works

Metabolic Transit and in Vivo Effects of Melanoidins and Precursor Compounds Deriving from the Maillard Reaction

Faist, V., & Erbersdobler, H. F. (2001) · Annals of Nutrition and Metabolism · doi:10.1159/000046699 · Cited by 192 · see citing works

The Effect of Formulation Excipients on Protein Stability and Aerosol Performance of Spray-Dried Powders of a Recombinant Humanized Anti-IgE Monoclonal Antibody1

Andya, J. D., Maa, Y., Costantino, H. R., Nguyen, P., Dasovich, N., Sweeney, T. D., Hsu, C. C., & Shire, S. J. (1999) · Pharmaceutical Research · doi:10.1023/a:1018805232453 · Cited by 190 · see citing works

Aminoguanidine prevents age-related arterial stiffening and cardiac hypertrophy

Corman, B., Duriez, M., Poitevin, P., Heudes, D., Bruneval, P., Tedgui, A., & Levy, B. I. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.3.1301 · Cited by 189 · see citing works

Analysis and prediction of mammalian protein glycation

Johansen, M. B., Kiemer, L., & Brunak, S. (2006) · Glycobiology · doi:10.1093/glycob/cwl009 · Cited by 189 · see citing works

Oral Glycotoxins Determine the Effects of Calorie Restriction on Oxidant Stress, Age-Related Diseases, and Lifespan

Cai, W., He, C., Zhu, L., Xue, C., Zheng, F., Striker, G. E., & Vlassara, H. (2008) · American Journal Of Pathology · doi:10.2353/ajpath.2008.080152 · Cited by 186 · see citing works

Dicarbonyls linked to damage in the powerhouse: glycation of mitochondrial proteins and oxidative stress

Rabbani, N., & Thornalley, P. J. (2008) · Biochemical Society Transactions · doi:10.1042/bst0361045 · Cited by 185 · see citing works

Accumulation of altered proteins and ageing: Causes and effects☆

Hipkiss, A. R. (2006) · Experimental Gerontology · doi:10.1016/j.exger.2006.03.004 · Cited by 185 · see citing works

The Maillard Reaction

Ames, J. M. (1992) · Springer eBooks · doi:10.1007/978-1-4684-9895-0_4 · Cited by 182 · see citing works

Studies on Absorption and Elimination of Dietary Maillard Reaction Products

FÖRSTER, A., KÜHNE, Y., & HENLE, T. O. (2005) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1333.054 · Cited by 180 · see citing works

The AGE inhibitor pyridoxamine inhibits lipemia and development of renal and vascular disease in Zucker obese rats

Alderson, N. L., Chachich, M. E., Youssef, N., Beattie, R. J., Nachtigal, M., Thorpe, S. R., & Baynes, J. (2003) · Kidney International · doi:10.1046/j.1523-1755.2003.00027.x · Cited by 171 · see citing works

Current and future issues in the manufacturing and development of monoclonal antibodies

Kozlowski, S., & Swann, P. (2006) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2006.05.002 · Cited by 170 · see citing works

Enzymatic digestion and mass spectrometry in the study of advanced glycation end products/peptides

Lapolla, A., Fedele, D., Reitano, R., Aricò, C. N., Seraglia, R., Traldi, P., Marotta, E., & Tonani, R. (2004) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2003.11.014 · Cited by 164 · see citing works

The Effect of Oxygen Radicals Metabolites and Vitamin E on Glycosylation of Proteins

Jain, S. K., & Palmer, M. (1997) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(96)00377-2 · Cited by 164 · see citing works

Enrichment and Analysis of Nonenzymatically Glycated Peptides: Boronate Affinity Chromatography Coupled with Electron-Transfer Dissociation Mass Spectrometry

Zhang, Q., Tang, N., Brock, J. W. C., Mottaz, H. M., Ames, J. M., Baynes, J., Smith, R. D., & Metz, T. (2007) · Journal of Proteome Research · doi:10.1021/pr070112q · Cited by 161 · see citing works

Antibacterial activity of lysozyme and lactoferrin is inhibited by binding of advanced glycation–modified proteins to a conserved motif

Li, Y. M., Tan, A. X., & Vlassara, H. (1995) · Nature Medicine · doi:10.1038/nm1095-1057 · Cited by 153 · see citing works

Increased protein glycation in cerebrospinal fluid of Alzheimer’s disease 2 2Abbreviations: AD, Alzheimer’s disease; AGEs, advanced glycation end products; apo, apolipoprotein; BSA, bovine serum albumin; CSF, cerebrospinal fluid; ELISA, enzyme-linked immunosorbent assay; PBS, phosphate buffer saline.

Shuvaev, V. V., Laffont-Proust, I., Sérot, J., Fujii, J., Taniguchi, N., & Siest, G. (2001) · Neurobiology of Aging · doi:10.1016/s0197-4580(00)00253-0 · Cited by 153 · see citing works

Oxidation-Reduction Properties of Methylglyoxal-modified Protein in Relation to Free Radical Generation

Lee, C., Yim, M. B., Chock, P. B., Yim, H., & Kang, S. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.39.25272 · Cited by 152 · see citing works

Glycosylated minor components of human adult hemoglobin. Purification, identification, and partial structural analysis.

McDonald, M. J., Shapiro, R., Bleichman, M., Solway, J., & Bunn, H. F. (1978) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38076-6 · Cited by 147 · see citing works

Identification of a pathway for the utilization of the Amadori product fructoselysine in Escherichia coli

Wiame, E., Delpierre, G., Collard, F., & Van Schaftingen, E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200863200 · Cited by 140 · see citing works

Age-related changes in the glycation of human aortic elastin

Konova, E. I., Baydanoff, S., Atanasova, M., & Velkova, A. S. (2003) · Experimental Gerontology · doi:10.1016/j.exger.2003.10.003 · Cited by 130 · see citing works

Improved Titanium Dioxide Enrichment of Phosphopeptides from HeLa Cells and High Confident Phosphopeptide Identification by Cross-Validation of MS/MS and MS/MS/MS Spectra

Yu, L., Zhu, Z., Chan, K. C., Issaq, H. J., Dimitrov, D. S., & Veenstra, T. D. (2007) · Journal of Proteome Research · doi:10.1021/pr070152u · Cited by 128 · see citing works

Characterization of glycation adducts on human serum albumin by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry

Wa, C., Cerny, R. L., Clarke, W. A., & Hage, D. S. (2007) · Clinica Chimica Acta · doi:10.1016/j.cca.2007.06.011 · Cited by 121 · see citing works

Oxidative, glycoxidative and lipoxidative damage to rat heart mitochondrial proteins is lower after 4 months of caloric restriction than in age-matched controls

Pamplona, R., Portero‐Otín, M., Requena, J. R., Gredilla, R., & Barja, G. (2002) · Mechanisms of Ageing and Development · doi:10.1016/s0047-6374(02)00076-3 · Cited by 120 · see citing works

Glycation during storage and administration of monoclonal antibody formulations

FISCHER, S., Hoernschemeyer, J., & MAHLER, H. (2008) · European Journal of Pharmaceutics and Biopharmaceutics · doi:10.1016/j.ejpb.2008.04.021 · Cited by 117 · see citing works

Proteomic Profiling of Nonenzymatically Glycated Proteins in Human Plasma and Erythrocyte Membranes

Zhang, Q., Tang, N., Schepmoes, A., Phillips, L. S., Smith, R. D., & Metz, T. (2008) · Journal of Proteome Research · doi:10.1021/pr700763r · Cited by 115 · see citing works

Effect of phosphate on the kinetics and specificity of glycation of protein.

Watkins, N. G., Neglia, C. I., Dyer, D. G., Thorpe, S. R., & Baynes, J. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48224-5 · Cited by 114 · see citing works

Unveiling a Glycation Hot Spot in a Recombinant Humanized Monoclonal Antibody

Boyan, Z., Yang, Y., Yuk, I. H. Y., Pai, R., McKay, P., Eigenbrot, C. W., Dennis, M. S., Katta, V., & Francissen, K. (2008) · Analytical Chemistry · doi:10.1021/ac701810q · Cited by 113 · see citing works

Glycation in food and metabolic transit of dietary AGEs (advanced glycation end-products): studies on the urinary excretion of pyrraline

Foerster, A., & Henle, T. (2003) · Biochemical Society Transactions · doi:10.1042/bst0311383 · Cited by 113 · see citing works

Vitamin C mediates chemical aging of lens crystallins by the Maillard reaction in a humanized mouse model

Fan, X., Reneker, L. W., Obrenovich, M. E., Strauch, C., Cheng, R., Jarvis, S. M., ORTWERTH, B. J., & Monnier, V. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0605101103 · Cited by 113 · see citing works

Metabolic transit of early and advanced Maillard products.

Finot, P. A., & Magnenat, E. M. (1981) · PubMed · Cited by 108 · see citing works

Review of a current role of mass spectrometry for proteome research

Chen, C. (2008) · Analytica Chimica Acta · doi:10.1016/j.aca.2008.06.017 · Cited by 107 · see citing works

Effects of Reducing Sugars on the Chemical Stability of Human Relaxin in the Lyophilized State

Li, S., Patapoff, T. W., Overcashier, D. E., Hsu, C. C., Nguyen, T. H., & Borchardt, R. T. (1996) · Journal of Pharmaceutical Sciences · doi:10.1021/js950456s · Cited by 106 · see citing works

Fragmentation behavior of glycated peptides derived from D ‐glucose, D ‐fructose and D ‐ribose in tandem mass spectrometry

Frolov, A., Hoffmann, P., & Hoffmann, R. (2006) · Journal of Mass Spectrometry · doi:10.1002/jms.1117 · Cited by 105 · see citing works

Biomarker discovery from the plasma proteome using multidimensional fractionation proteomics

Lee, H.-J., Lee, E.-Y., Kwon, M., & Paik, Y. (2006) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2006.01.007 · Cited by 104 · see citing works

Mechanism of Perturbation of Integrin-Mediated Cell-Matrix Interactions by Reactive Carbonyl Compounds and Its Implication for Pathogenesis of Diabetic Nephropathy

Pedchenko, V. K., Chetyrkin, S. V., Chuang, P., Ham, A. L., Saleem, M. A., Mathieson, P. W., Hudson, B. G., & Voziyan, P. (2005) · Diabetes · doi:10.2337/diabetes.54.10.2952 · Cited by 99 · see citing works

Physical/chemical separations in the break-up of highly charged droplets from electrosprays

Tang, K., & Smith, R. (2001) · Journal of the American Society for Mass Spectrometry · doi:10.1016/s1044-0305(01)00222-7 · Cited by 95 · see citing works

Binding of receptor for advanced glycation end products (RAGE) ligands is not sufficient to induce inflammatory signals: lack of activity of endotoxin-free albumin-derived advanced glycation end products

Mone, M. D., Koehne, C., Rediske, J. J., Hughes, T. E., & Valencia, J. (2004) · Diabetologia · doi:10.1007/s00125-004-1392-9 · Cited by 94 · see citing works

Relationships between Antioxidant Activity, Color, and Flavor Compounds of Crystal Malt Extracts

Woffenden, H. M., Ames, J. M., & Chandra, S. (2001) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf010583b · Cited by 88 · see citing works

Increased oxidation, glycoxidation, and lipoxidation of brain proteins in prion disease

Pamplona, R., Naudí, A., Gavı́n, R., Pastrana, M. A., Sajnani, G., Ilieva, E. V., del Rı́o, J. A., Portero‐Otín, M., Ferrer, I., & Requena, J. R. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.07.009 · Cited by 85 · see citing works

Characterization of the Chemical Structure of Novel Colored Maillard Reaction Products from Furan-2-carboxaldehyde and Amino Acids

Hofmann, T. F. (1998) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf970732j · Cited by 85 · see citing works

RAGE Expression and AGE-Induced MAP Kinase Activation in Caco-2 Cells

Zill, H., Günther, R., Erbersdobler, H. F., Fölsch, U. R., & Faist, V. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.5901 · Cited by 84 · see citing works

Application of electron transfer dissociation mass spectrometry in analyses of non‐enzymatically glycated peptides

Zhang, Q., Frolov, A., Tang, N., Hoffmann, R., van de Goor, T., Metz, T., & Smith, R. D. (2007) · Rapid Communications in Mass Spectrometry · doi:10.1002/rcm.2884 · Cited by 83 · see citing works

Aging and glycoxidant stress

Peppa, Μ., Uribarri, J., & Vlassara, H. (2008) · HORMONES · doi:10.1007/bf03401503 · Cited by 83 · see citing works

Nε‐carboxymethyllysine‐modified proteins are unable to bind to RAGE and activate an inflammatory response

Buetler, T. M., Leclerc, E., Baumeyer, A., Latado, H., Newell, J. W., Adolfsson, O., Parisod, V., Richoz, J., Maurer, S., Foata, F., et al. (2008) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.200700101 · Cited by 82 · see citing works

Proteomic Analysis of the Site Specificity of Glycation and Carboxymethylation of Ribonuclease

Brock, J. W. C., Hinton, D. J. S., Cotham, W. E., Metz, T., Thorpe, S. R., Baynes, J., & Ames, J. M. (2003) · Journal of Proteome Research · doi:10.1021/pr0340173 · Cited by 82 · see citing works

The Dicarbonyl Proteome

Rabbani, N., & Thornalley, P. J. (2008) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1433.043 · Cited by 81 · see citing works

Screening and Sequencing of Glycated Proteins by Neutral Loss Scan LC/MS/MS Method

Gadgil, H. S., Bondarenko, P. V., Treuheit, M. J., & Ren, D. (2007) · Analytical Chemistry · doi:10.1021/ac070619k · Cited by 77 · see citing works

Effect of Kilning on the Antioxidant and Pro-oxidant Activities of Pale Malts

Woffenden, H. M., Ames, J. M., Chandra, S., Anese, M., & Nicoli, M. C. (2002) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf020312g · Cited by 74 · see citing works

Matrix-assisted laser desorption/ionization mass spectrometry, enzymatic digestion, and molecular modeling in the study of nonenzymatic glycation of IgG

Lapolla, A., Fedele, D., Garbeglio, M., Martano, L., Tonani, R., Seraglia, R., Favretto, D., Fedrigo, M. A., & Traldi, P. (2000) · Journal of the American Society for Mass Spectrometry · doi:10.1016/s1044-0305(99)00134-8 · Cited by 74 · see citing works

Production of Nε-(Carboxymethyl)Lysine Is Impaired in Mice Deficient in NADPH Oxidase

Anderson, M. M., & Heinecke, J. W. (2003) · Diabetes · doi:10.2337/diabetes.52.8.2137 · Cited by 73 · see citing works

Tissue-Specific Expression and Post-Translational Modification of Histone H3 Variants

Garcia, B. A., Thomas, C. E., Kelleher, N. L., & Mizzen, C. A. (2008) · Journal of Proteome Research · doi:10.1021/pr800044q · Cited by 71 · see citing works

Characterization of Nonenzymatic Glycation on a Monoclonal Antibody

Brady, L. J., Martinez, T., & Balland, A. (2007) · Analytical Chemistry · doi:10.1021/ac7017469 · Cited by 70 · see citing works

Advanced Glycation End Products of DNA: Quantification of N 2 -(1-Carboxyethyl)-2′-deoxyguanosine in Biological Samples by Liquid Chromatography Electrospray Ionization Tandem Mass Spectrometry

Synold, T. W., Xi, B., Wuenschell, G. E., Tamae, D., Figarola, J. L., Rahbar, S., & Termini, J. S. (2008) · Chemical Research in Toxicology · doi:10.1021/tx800224y · Cited by 69 · see citing works

Depletion of reactive advanced glycation endproducts from diabetic uremic sera using a lysozyme-linked matrix.

Mitsuhashi, T., Li, Y. M., Fishbane, S., & Vlassara, H. (1997) · Journal of Clinical Investigation · doi:10.1172/jci119600 · Cited by 68 · see citing works

The effects of ageing on glycation and the interpretation of glycaemic control in Type 2 diabetes

Kilpatrick, E. S., Dominiczak, M. H., & SMALL, M. P. (1996) · QJM · doi:10.1093/qjmed/89.4.307 · Cited by 65 · see citing works

Identification of Amadori-Modified Plasma Proteins in Type 2 Diabetes and the Effect of Short-Term Intensive Insulin Treatment

Jaleel, A., Halvatsiotis, P., Williamson, B. D., Juhász, P., Martin, S. A., & Nair, K. S. (2005) · Diabetes Care · doi:10.2337/diacare.28.3.645 · Cited by 65 · see citing works

Development of novel free radicals during the amino-carbonyl reaction of sugars with amino acids

Namiki, M., & Hayashi, T. (1975) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf60199a024 · Cited by 64 · see citing works

Use of lyoprotectants in the freeze-drying of a model protein, ribonuclease A.

Townsend, M. W., & DeLuca, P. P. (1989) · PubMed · Cited by 63 · see citing works

Chemical modification of muscle protein in diabetes

Alt, N., Carson, J. A., Alderson, N. L., Wang, Y., Nagai, R., Henle, T., Thorpe, S. R., & Baynes, J. (2004) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2004.03.012 · Cited by 62 · see citing works

Advanced glycation end-products and methionine sulphoxide in skin collagen of patients with type 1 diabetes

Yu, Y., Thorpe, S. R., Jenkins, A. J., Shaw, J., Sochaski, M. A., McGee, D., Aston, C. E., Orchard, T. J., Silvers, N., Peng, Y., et al. (2006) · Diabetologia · doi:10.1007/s00125-006-0355-8 · Cited by 59 · 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

Characterization of melanoidins from a glucose-glycine model system

Borrelli, R. C., Fogliano, V., Monti, S. M., & Ames, J. M. (2002) · European Food Research and Technology · doi:10.1007/s00217-002-0531-0 · Cited by 57 · see citing works

A new effective method for the evaluation of glycated intact plasma proteins in diabetic subjects

Lapolla, A., Fedele, D., Seraglia, R., Catinella, S., Baldo, L., Aronica, R., & Traldi, P. (1995) · Diabetologia · doi:10.1007/bf00402178 · Cited by 55 · see citing works

A novel nanospray capillary zone electrophoresis/mass spectrometry interface

Hsieh, F., Baronas, E., Muir, C., & Martin, S. A. (1999) · Rapid Communications in Mass Spectrometry · doi:10.1002/(sici)1097-0231(19990115)13:1 · Cited by 50 · see citing works

Electrospray ionization suppression, a physical or a chemical phenomenon?

Beaudry, F., & Vachon, P. (2005) · Biomedical Chromatography · doi:10.1002/bmc.553 · Cited by 47 · see citing works

Non Enzymatic Glycated Proteins in the Blood and Cardiovascular Disease

Misciagna, G., Michele, G. D., & Trevisan, M. (2007) · Current Pharmaceutical Design · doi:10.2174/138161207783018545 · Cited by 43 · see citing works

Detection and identification of arginine modifications on methylglyoxal‐modified ribonuclease by mass spectrometric analysis

Brock, J. W. C., Cotham, W. E., Thorpe, S. R., Baynes, J., & Ames, J. M. (2006) · Journal of Mass Spectrometry · doi:10.1002/jms.1144 · Cited by 40 · see citing works

Structure of the human adult hemoglobin minor fraction A1b by electrospray and secondary ion mass spectrometry. Pyruvic acid as amino-terminal blocking group

Promé, D., Blouquit, Y., Ponthus, C., Promé, J., & Rosa, J. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98801-0 · Cited by 39 · see citing works

Analysis of non‐enzymatically glycated peptides: neutral‐loss‐triggered MS 3 versus multi‐stage activation tandem mass spectrometry

Zhang, Q., Petyuk, V., Schepmoes, A., Orton, D., Monroe, M. E., Yang, F., Smith, R. D., & Metz, T. (2008) · Rapid Communications in Mass Spectrometry · doi:10.1002/rcm.3703 · Cited by 39 · see citing works

Application of phenylboronic acid modified hydrogel affinity chips for high‐throughput mass spectrometric analysis of glycated proteins

Gontarev, S. V., Shmanai, V. V., Frey, S. K., Kvach, M. V., & Schweigert�, F. J. (2006) · Rapid Communications in Mass Spectrometry · doi:10.1002/rcm.2793 · Cited by 38 · see citing works

Identification of Glucose-Derived Cross-Linking Sites in Ribonuclease A

Dai, Z., Wang, B., Sun, G., Fan, X., Anderson, V. E., & Monnier, V. M. (2008) · Journal of Proteome Research · doi:10.1021/pr700874a · Cited by 32 · see citing works

Analysis of glycated insulin by MALDI-TOF mass spectrometry

Farah, M. A., Bose, S., Lee, J., Jung, H.-C., & Kim, Y. (2005) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2005.05.028 · Cited by 32 · see citing works

Evidence for the role of lipid peroxides on glycation of hemoglobin and plasma proteins in non-diabetic asthma patients

Sathiyapriya, V., Bobby, Z., Kumar, S. V., Selvaraj, N., Parthibane, V., & Gupta, S. (2005) · Clinica Chimica Acta · doi:10.1016/j.cca.2005.11.001 · Cited by 31 · see citing works

The antioxidant effect of a diet rich in Maillard reaction products is attenuated after consumption by healthy male adolescents. In vitro and in vivo comparative study

Seiquer, I., Ruiz‐Roca, B., Mesías, M., Muñoz‐Hoyos, A., Galdó, G., Ochoa, J. J., & Navarro, M. P. (2008) · Journal of the Science of Food and Agriculture · doi:10.1002/jsfa.3213 · Cited by 31 · see citing works

Reassessing the increased glycation of hemoglobin in nondiabetic chronic renal failure patients: A hypothesis on the role of lipid peroxides

Selvaraj, N., Bobby, Z., Koner, B. C., & Das, A. K. (2005) · Clinica Chimica Acta · doi:10.1016/j.cccn.2005.04.015 · Cited by 29 · see citing works

Glycation of interferon-beta-1b and human serum albumin in a lyophilized glucose formulation

Zheng, X., Wu, S., & Hancock, W. S. (2006) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2006.06.038 · Cited by 27 · see citing works

Fructosamine 3-kinase and other enzymes involved in protein deglycation

SCHAFTINGEN, E. V., Delpierre, G., Collard, F., Fortpied, J., Gemayel, R., Wiame, E., & Veiga‐da‐Cunha, M. (2007) · Advances in Enzyme Regulation · doi:10.1016/j.advenzreg.2006.12.002 · Cited by 25 · see citing works

Susceptibility of rhDNase I to Glycation in the Dry-Powder State

Quan, C. P., Wu, S., Dasovich, N., Hsu, C. C., Patapoff, T., & Canova‐Davis, E. (1999) · Analytical Chemistry · doi:10.1021/ac9900580 · Cited by 25 · see citing works

A comparative study of proteolysis methods for the measurement of 3-nitrotyrosine residues: Enzymatic digestion versus hydrochloric acid-mediated hydrolysis

Delatour, T., Fenaille, F., Parisod, V., Richoz, J., Vuichoud, J., Mottier, P., & Buetler, T. M. (2006) · Journal of Chromatography B · doi:10.1016/j.jchromb.2006.11.005 · Cited by 21 · see citing works

Application of Semiquantitative Proteomics Techniques to the Maillard Reaction

Ames, J. M. (2005) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1333.028 · Cited by 12 · see citing works

BROWNING | Nonenzymatic

Ames, J. M. (2003) · Elsevier eBooks · doi:10.1016/b0-12-227055-x/00128-0 · Cited by 12 · see citing works

GLYCOSYLATED HAEMOGLOBIN IN GLUCOSE-6-PHOSPHATE DEHYDROGENASE DEFICIENCY

Donde, U., Baxi, A. J., Tawil, H. E., & Ghwarsha, K. (1985) · The Lancet · doi:10.1016/s0140-6736(85)90102-3 · Cited by 7 · see citing works

Advanced Glycation End Products and Diabetic Complications

Singh, V. P., Bali, A., Singh, N., & Jaggi, A. S. (2014) · The Korean Journal of Physiology & Pharmacology · doi:10.4196/kjpp.2014.18.1.1 · Cited by 1,518 · 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

RAGE (Receptor for Advanced Glycation Endproducts), RAGE Ligands, and their role in Cancer and Inflammation

Sparvero, L. J., Asafu-Adjei, D. A., Kang, R., Tang, D., Amin, N., Im, J., Rutledge, R., Lin, B., Amoscato, A. A., Zeh, H. J., et al. (2009) · Journal of Translational Medicine · doi:10.1186/1479-5876-7-17 · Cited by 625 · see citing works

Advanced glycation end products (AGEs) and other adducts in aging-related diseases and alcohol-mediated tissue injury

Rungratanawanich, W., Qu, Y., Wang, X., Essa, M. M., & Song, B.-J. (2021) · Experimental & Molecular Medicine · doi:10.1038/s12276-021-00561-7 · Cited by 411 · see citing works

Dietary Advanced Glycation End Products and Aging

Luevano-Contreras, C., & Chapman-Novakofski, K. (2010) · Nutrients · doi:10.3390/nu2121247 · Cited by 396 · see citing works

Review: Glycation of human serum albumin

Anguizola, J. A., Matsuda, R., Barnaby, O. S., Hoy, K. S., Wa, C., DeBolt, E., Koke, M., & Hage, D. S. (2013) · Clinica Chimica Acta · doi:10.1016/j.cca.2013.07.013 · Cited by 395 · see citing works

AGE restriction in diabetes mellitus: a paradigm shift

Vlassara, H., & Striker, G. E. (2011) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2011.74 · Cited by 277 · see citing works

Advanced glycation End-products (AGEs): an emerging concern for processed food industries

Sharma, C., Kaur, A., Thind, S. S., Singh, B., & Raina, S. (2015) · Journal of Food Science and Technology · doi:10.1007/s13197-015-1851-y · Cited by 254 · see citing works

Cooking‐Induced Protein Modifications in Meat

Yu, T., Morton, J. D., Clerens, S., & Dyer, J. M. (2016) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/1541-4337.12243 · Cited by 242 · see citing works

Advanced glycation end‐products and the kidney

Busch, M., Franke, S., Rüster, C., & Wolf, G. (2010) · European Journal of Clinical Investigation · doi:10.1111/j.1365-2362.2010.02317.x · Cited by 226 · see citing works

Melanoidins Formed by Maillard Reaction in Food and Their Biological Activity

Echavarría, A. P., Pagán, J., & Ibarz, A. (2012) · Food Engineering Reviews · doi:10.1007/s12393-012-9057-9 · Cited by 224 · 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

MXene-Based Nanocomposite Sensors

Riazi, H., Taghizadeh, G., & Soroush, M. (2021) · ACS Omega · doi:10.1021/acsomega.0c05828 · Cited by 202 · see citing works

An Overview of Pharmaceutical Excipients: Safe or Not Safe?

Abrantes, C. G., Duarte, D. M., & Reis, C. P. (2016) · Journal of Pharmaceutical Sciences · doi:10.1016/j.xphs.2016.03.019 · Cited by 168 · see citing works

The Oncogenic Action of NRF2 Depends on De-glycation by Fructosamine-3-Kinase

Sanghvi, V. R., Leibold, J., Mina, M., Mohan, P., Berishaj, M., Li, Z., Miele, M. M., Lailler, N., Zhao, C., de Stanchina, E., et al. (2019) · Cell · doi:10.1016/j.cell.2019.07.031 · Cited by 155 · see citing works

Advanced glycation end products mediated cellular and molecular events in the pathology of diabetic nephropathy

Kumar Pasupulati, A., Chitra, P. S., & Reddy, G. B. (2016) · Biomolecular Concepts · doi:10.1515/bmc-2016-0021 · Cited by 163 · 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

A review on mechanism of inhibition of advanced glycation end products formation by plant derived polyphenolic compounds

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

Aquatic polymer-based edible films of fish gelatin crosslinked with alginate dialdehyde having enhanced physicochemical properties

Park, J., Nam, J., Yun, H., Jin, H., & Kwak, H. W. (2020) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2020.117317 · Cited by 148 · see citing works

Comparison of modification sites formed on human serum albumin at various stages of glycation

Barnaby, O. S., Cerny, R. L., Clarke, W. A., & Hage, D. S. (2010) · Clinica Chimica Acta · doi:10.1016/j.cca.2010.10.018 · Cited by 144 · see citing works

Modulation of Gut Microbiota in the Management of Metabolic Disorders: The Prospects and Challenges

Erejuwa, O. O., Sulaiman, S. A., & Wahab, M. S. A. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms15034158 · Cited by 137 · see citing works

A compendium of wheat germ: Separation, stabilization and food applications

Boukid, F., Folloni, S., Ranieri, R., & Vittadini, E. (2018) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2018.06.001 · Cited by 131 · see citing works

Prevention of Non-Enzymatic Glycosylation (Glycation) : Implication in the Treatment of Diabetic Complication

Younus, H., & Anwar, S. (2016) · International Journal of Health Sciences · doi:10.12816/0048818 · Cited by 129 · see citing works

Thermal aggregation of glycated bovine serum albumin

Rondeau, P., Navarra, G., Cacciabaudo, F., Leone, M., Bourdon, E., & Militello, V. (2009) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2009.12.003 · Cited by 120 · see citing works

Emerging role of post-translational modifications in chronic kidney disease and cardiovascular disease

Gajjala, P. R., Fliser, D., Speer, T., Jankowski, V., & Jankowski, J. (2015) · Nephrology Dialysis Transplantation · doi:10.1093/ndt/gfv048 · Cited by 110 · see citing works

Glycative stress from advanced glycation end products (AGEs) and dicarbonyls: An emerging biological factor in cancer onset and progression

Lin, J., Wu, C., Lu, C., Hsia, S., & Yen, G. (2016) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201500759 · Cited by 105 · see citing works

proBDNF is modified by advanced glycation end products in Alzheimer’s disease and causes neuronal apoptosis by inducing p75 neurotrophin receptor processing

Fleitas, C., Piñol‐Ripoll, G., Marfull‐Oromí, P., Rocandio, D., Ferrer, I., Rampon, C., Egea, J., & Espinet, C. (2018) · Molecular Brain · doi:10.1186/s13041-018-0411-6 · Cited by 105 · see citing works

Comprehensive Identification of Glycated Peptides and Their Glycation Motifs in Plasma and Erythrocytes of Control and Diabetic Subjects

Zhang, Q., Monroe, M. E., Schepmoes, A., Clauss, T. R., Gritsenko, M. A., Meng, D., Petyuk, V., Smith, R. D., & Metz, T. (2011) · Journal of Proteome Research · doi:10.1021/pr200040j · Cited by 104 · see citing works

Dihydrochalcones: Implication in resistance to oxidative stress and bioactivities against advanced glycation end-products and vasoconstriction

de Bernonville, T. D., Guyot, S., Paulin, J. P., Gaucher, M., Loufrani, L., Henrion, D., Derbré, S., Guilet, D., Richomme, P., Dat, J. F., et al. (2009) · Phytochemistry · doi:10.1016/j.phytochem.2009.11.004 · Cited by 102 · see citing works

Functional decorations: post-translational modifications and heart disease delineated by targeted proteomics

Liddy, K. A., White, M. Y., & Cordwell, S. J. (2013) · Genome Medicine · doi:10.1186/gm424 · Cited by 102 · see citing works

Effect of transglutaminase-catalyzed glycosylation on the allergenicity and conformational structure of shrimp (Metapenaeus ensis) tropomyosin

Yuan, F., Lv, L., Li, Z., Mi, N., Chen, H., & Lin, H. (2016) · Food Chemistry · doi:10.1016/j.foodchem.2016.09.139 · Cited by 99 · see citing works

Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update for the period 2005–2006

Harvey, D. J. (2010) · Mass Spectrometry Reviews · doi:10.1002/mas.20265 · Cited by 98 · see citing works

Type 2 Diabetes Mellitus: Limitations of Conventional Therapies and Intervention with Nucleic Acid-Based Therapeutics

Kokil, G. R., Veedu, R. N., Ramm, G. A., Prins, J. B., & Parekh, H. S. (2015) · Chemical Reviews · doi:10.1021/cr5002832 · Cited by 98 · see citing works

Potential Clinical Error Arising From Use of HbA1c in Diabetes: Effects of the Glycation Gap

Nayak, A., Singh, B. M., & Dunmore, S. (2019) · Endocrine Reviews · doi:10.1210/er.2018-00284 · Cited by 92 · see citing works

N ϵ -(carboxymethyl)lysine: A Review on Analytical Methods, Formation, and Occurrence in Processed Food, and Health Impact

Nguyen, H. T., van der Fels‐Klerx, H. J., & van Boekel, M. A. J. S. (2013) · Food Reviews International · doi:10.1080/87559129.2013.853774 · Cited by 92 · see citing works

Complementary middle‐down and intact monoclonal antibody proteoform characterization by capillary zone electrophoresis – mass spectrometry

Belov, A. M., Zang, L., Sebastiano, R., Santos, M. R., Bush, D. R., Karger, B. L., & Ivanov, A. R. (2018) · ELECTROPHORESIS · doi:10.1002/elps.201800067 · Cited by 88 · see citing works

The Mechanisms of Inhibition of Advanced Glycation End Products Formation through Polyphenols in Hyperglycemic Condition

Khangholi, S., Majid, F. A. A., Berwary, N. J. A., Ahmad, F., & Aziz, R. (2015) · Planta Medica · doi:10.1055/s-0035-1558086 · Cited by 93 · see citing works

Natural Flavonoids as Potential Herbal Medication for the Treatment of Diabetes Mellitus and its Complications

Chen, J., Mangelinckx, S., Adams, A., Wang, Z., Li, W., & KIMPE, N. D. (2015) · Natural Product Communications · doi:10.1177/1934578x1501000140 · Cited by 86 · see citing works

Assessment of the Concentrations of Various Advanced Glycation End-Products in Beverages and Foods That Are Commonly Consumed in Japan

Takeuchi, M., Takino, J.-I., Furuno, S., Shirai, H., Kawakami, M., Muramatsu, M., Kobayashi, Y., & Yamagishi, S. (2015) · PLoS ONE · doi:10.1371/journal.pone.0118652 · Cited by 85 · see citing works

Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update for 2009–2010

Harvey, D. J. (2014) · Mass Spectrometry Reviews · doi:10.1002/mas.21411 · Cited by 84 · see citing works

Non‐enzymatic glycation and glycoxidation protein products in foods and diseases: An interconnected, complex scenario fully open to innovative proteomic studies

Arena, S., Salzano, A. M., Renzone, G., DˈAmbrosio, C., & Scaloni, A. (2013) · Mass Spectrometry Reviews · doi:10.1002/mas.21378 · Cited by 84 · see citing works

Antiglycation therapy: Discovery of promising antiglycation agents for the management of diabetic complications

Abbas, G., Al-Harrasi, A. S., Hussain, H., Hussain, J., Rashid, R., & Choudhary, M. I. (2015) · Pharmaceutical Biology · doi:10.3109/13880209.2015.1028080 · Cited by 81 · see citing works

Maillard Reaction in Flour Product Processing: Mechanism, Impact on Quality, and Mitigation Strategies of Harmful Products

Qi, Y., Wang, W., Yang, T., Ding, W., & Xu, B. (2025) · Foods · doi:10.3390/foods14152721 · Cited by 80 · see citing works

Redox proteomics: Methods for the identification and enrichment of redox‐modified proteins and their applications

Lennicke, C., Rahn, J., Heimer, N., Lichtenfels, R., Wessjohann, L. A., & Seliger, B. (2015) · PROTEOMICS · doi:10.1002/pmic.201500268 · Cited by 80 · see citing works

Fructose-Asparagine Is a Primary Nutrient during Growth of Salmonella in the Inflamed Intestine

Ali, M. M., Newsom, D. L., González, J. F., Sabag-Daigle, A., Stahl, C. C., Steidley, B. L., Dubena, J., Dyszel, J. L., Smith, J. N., Dieye, Y., et al. (2014) · PLoS Pathogens · doi:10.1371/journal.ppat.1004209 · Cited by 77 · see citing works

Human transferrin: An inorganic biochemistry perspective

Silva, A. M. N., Moniz, T., de Castro, B., & Rangel, M. (2021) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2021.214186 · Cited by 77 · see citing works

Forensic proteomics

Parker, G. J., McKiernan, H. E., Legg, K. M., & Goecker, Z. C. (2021) · Forensic Science International Genetics · doi:10.1016/j.fsigen.2021.102529 · Cited by 78 · 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

Investigation of betaine as a novel psychotherapeutic for schizophrenia

Ohnishi, T., Balan, S., Toyoshima, M., Maekawa, M., Ohba, H., Watanabe, A., Iwayama, Y., Fujita, Y., Tan, Y., Hisano, Y., et al. (2019) · EBioMedicine · doi:10.1016/j.ebiom.2019.05.062 · Cited by 78 · see citing works

Dietary Advanced Glycation End Products and Cardiometabolic Risk

Luévano‐Contreras, C., Gómez-Ojeda, A., Macías-Cervantes, M. H., & Garay‐Sevilla, M. E. (2017) · Current Diabetes Reports · doi:10.1007/s11892-017-0891-2 · Cited by 78 · see citing works

Glycation Isotopic Labeling with 13C-Reducing Sugars for Quantitative Analysis of Glycated Proteins in Human Plasma

Priego‐Capote, F., Scherl, A., Möller, M., Waridel, P., Lisacek, F., & Sanchez, J. (2009) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m900439-mcp200 · Cited by 77 · see citing works

Gelatin-bacterial cellulose composite sponges thermally cross-linked with glucose for tissue engineering applications

Kirdponpattara, S., Phisalaphong, M. K. M., & Kongruang, S. (2017) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2017.08.094 · Cited by 74 · see citing works

Diabetic Cardiomyopathy: An Immunometabolic Perspective

Mishra, P. K., Ying, W., Nandi, S. S., Bandyopadhyay, G. K., Patel, K. P., & Mahata, S. K. (2017) · Frontiers in Endocrinology · doi:10.3389/fendo.2017.00072 · Cited by 73 · see citing works

Free amino acids, acrylamide and biogenic amines in gamma-aminobutyric acid enriched sourdough and commercial breads

Diana, M., Rafecas, M., & Quı́lez, J. (2014) · Journal of Cereal Science · doi:10.1016/j.jcs.2014.06.009 · Cited by 73 · see citing works

Quantitative analysis of glycation patterns in human serum albumin using 16O/18O-labeling and MALDI–TOF MS

Barnaby, O. S., Cerny, R. L., Clarke, W., & Hage, D. S. (2011) · Clinica Chimica Acta · doi:10.1016/j.cca.2011.05.012 · Cited by 72 · see citing works

Glycated Serum Albumin and AGE Receptors

Vetter, S. W. (2015) · Advances in clinical chemistry · doi:10.1016/bs.acc.2015.07.005 · Cited by 71 · see citing works

Maillard Reaction, mitochondria and oxidative stress: Potential role of antioxidants

Edeas, M. A., Attaf, D., Mailfert, A.-S., Nasu, M., & Joubet, R. (2009) · Pathologie Biologie · doi:10.1016/j.patbio.2009.09.011 · Cited by 72 · see citing works

Mass spectrometry in food proteomics: a tutorial

Cunsolo, V., Muccilli, V., Saletti, R., & Foti, S. (2014) · Journal of Mass Spectrometry · doi:10.1002/jms.3374 · Cited by 69 · see citing works

The status of glycation in protein aggregation

Taghavi, F., Habibi-Rezaei, M., Amani, M., Moosavi‐Movahedi, A. A., & Moosavi‐Movahedi, A. A. (2016) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2015.12.085 · Cited by 68 · see citing works

Food contaminants: Impact of food processing, challenges and mitigation strategies for food security

Vignesh, A., Amal, T. C., & Vasanth, K. (2024) · Food Research International · doi:10.1016/j.foodres.2024.114739 · Cited by 72 · see citing works

Probing Protein Glycation by Chromatography and Mass Spectrometry: Analysis of Glycation Adducts

Soboleva, A., Vikhnina, M., Grishina, T., & Frolov, A. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18122557 · Cited by 68 · see citing works

Analysis of protein glycation using phenylboronate acrylamide gel electrophoresis

Morais, M. P. P., Mackay, J. D., Bhamra, S. K., BUCHANAN, J. G., James, T. D., Fossey, J., & van den Elsen, J. M. H. (2009) · PROTEOMICS · doi:10.1002/pmic.200900269 · Cited by 65 · see citing works

Diabetes-induced morphological, biomechanical, and compositional changes in ocular basement membranes

To, M. Q., Goz, A., Camenzind, L. C., Oertle, P., Candiello, J., Sullivan, M., Henrich, P. B., Loparić, M., Safi, F., Eller, A. W., et al. (2013) · Experimental Eye Research · doi:10.1016/j.exer.2013.09.011 · Cited by 63 · see citing works

Excess free fructose, high-fructose corn syrup and adult asthma: the Framingham Offspring Cohort

DeChristopher, L. R., & Tucker, K. L. (2018) · British Journal Of Nutrition · doi:10.1017/s0007114518000417 · Cited by 59 · see citing works

Dietary Advanced Glycation End-products (AGE) and Risk of Breast Cancer in the Prostate, Lung, Colorectal and Ovarian Cancer Screening Trial (PLCO)

Omofuma, O. O., Turner, D. P., Peterson, L. L., Merchant, A. T., Zhang, J., & Steck, S. E. (2020) · Cancer Prevention Research · doi:10.1158/1940-6207.capr-19-0457 · Cited by 57 · see citing works

Protective effect of selenium supplementation following oxidative stress mediated by glucose on retinal pigment epithelium

de Vega, R. G., García, M., Fernández‐Sánchez, M. L., González‐Iglesias, H., & Sanz‐Medel, A. (2017) · Metallomics · doi:10.1039/c7mt00209b · Cited by 55 · see citing works

Advanced glycation end products (AGEs) in oral pathology

Ilea, A., Băbțan, A.-M., Boşca, A. B., Crişan, M., Petrescu, N. B., Collino, M., Sainz, R. M., Gerlach, J. Q., & Câmpian, R. S. (2018) · Archives of Oral Biology · doi:10.1016/j.archoralbio.2018.05.013 · Cited by 55 · see citing works

Temporal Signal Pattern Recognition in Mass Spectrometry: A Method for Rapid Identification and Accurate Quantification of Biomarkers for Inborn Errors of Metabolism with Quality Assurance

DiBattista, A., McIntosh, N., Lamoureux, M., Al-Dirbashi, O. Y., Chakraborty, P. K., & Britz‐McKibbin, P. (2017) · Analytical Chemistry · doi:10.1021/acs.analchem.7b01727 · Cited by 54 · see citing works

Applications of reversible covalent chemistry in analytical sample preparation

Siegel, D. J. (2012) · The Analyst · doi:10.1039/c2an35697j · Cited by 51 · see citing works

Rosmarinic acid restrains protein glycation and aggregation in human serum albumin: Multi spectroscopic and microscopic insight - Possible Therapeutics Targeting Diseases

Shamsi, A., Ahmed, A., Khan, M. S., Husain, F. M., & Bano, B. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.06.048 · Cited by 51 · see citing works

B-Type Natriuretic Peptide Signal Peptide Circulates in Human Blood

Siriwardena, M., Kleffmann, T., Ruygrok, P., Cameron, V. A., Yandle, T. G., Nicholls, M. G., Richards, M., & Pemberton, C. J. (2010) · Circulation · doi:10.1161/circulationaha.109.909937 · Cited by 51 · see citing works

Influence and effect of osmolytes in biopharmaceutical formulations

Wlodarczyk, S. R., Custodio, D. F., Pessoa, A., & Monteiro, G. (2018) · European Journal of Pharmaceutics and Biopharmaceutics · doi:10.1016/j.ejpb.2018.07.019 · Cited by 50 · see citing works

Glycation modulates alpha-synuclein fibrillization kinetics: A sweet spot for inhibition

Farzadfard, A., König, A., Petersen, S. V., Nielsen, J., Vasili, E., Dominguez‐Meijide, A., Buell, A. K., Outeiro, T. F., & Otzen, D. E. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.101848 · Cited by 48 · see citing works

Effect of dietary advanced glycation end products on inflammation and cardiovascular risks in healthy overweight adults: a randomised crossover trial

Baye, E., de Courten, M. P., Walker, K., Ranasinha, S., Earnest, A., Forbes, J. M., & de Courten, B. (2017) · Scientific Reports · doi:10.1038/s41598-017-04214-6 · Cited by 50 · see citing works

Maillard Proteomics: Opening New Pages

Soboleva, A., Schmidt, R., Vikhnina, M., Grishina, T., & Frolov, A. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18122677 · Cited by 47 · see citing works

Perspective: The Paradox in Dietary Advanced Glycation End Products Research—The Source of the Serum and Urinary Advanced Glycation End Products Is the Intestines, Not the Food

DeChristopher, L. R. (2017) · Advances in Nutrition · doi:10.3945/an.117.016154 · Cited by 47 · see citing works

Application of Proteomics in Food Technology and Food Biotechnology: Process Development, Quality Control and Product Safety

Gašo-Sokač, D., Kovač, S., & Josić, D. (2010) · University of Zagreb University Computing Centre (SRCE) · Cited by 46 · see citing works

Isotope dilution ESI-LC-MS/MS for quantification of free and total Nε-(1-Carboxymethyl)-l-Lysine and free Nε-(1-Carboxyethyl)-l-Lysine: Comparison of total Nε-(1-Carboxymethyl)-l-Lysine levels measured with new method to ELISA assay in gruel samples

Tareke, E., Forslund, A. H., Lindh, C. H., Fahlgren, C., & Östman, E. M. (2013) · Food Chemistry · doi:10.1016/j.foodchem.2013.07.003 · Cited by 46 · see citing works

Inhalation Dosage Forms: A Focus on Dry Powder Inhalers and Their Advancements

Magramane, S., Vlahović, K., Gordon, P., Kállai‐Szabó, N., Zelkó, R., Antal, I., & Farkas, D. (2023) · Pharmaceuticals · doi:10.3390/ph16121658 · Cited by 45 · see citing works

Identification and characterization of glycation adducts on osteocalcin

Thomas, C. J., Cleland, T. P., Zhang, S., Gundberg, C. M., & Vashishth, D. (2017) · Analytical Biochemistry · doi:10.1016/j.ab.2017.02.011 · Cited by 45 · see citing works

Aptasensor based optical detection of glycated albumin for diabetes mellitus diagnosis

Ghosh, S., Datta, D., Cheema, M., Dutta, M. B., & Stroscio, M. A. (2017) · Nanotechnology · doi:10.1088/1361-6528/aa893a · Cited by 45 · see citing works

Combining hydrophilic chemotherapy and hydrophobic phytotherapy via tumor-targeted albumin–QDs nano-hybrids: covalent coupling and phospholipid complexation approaches

Zayed, D. G., Ebrahim, S. M., Helmy, M. W., Khattab, S. N., Bahey-El-Din, M., Fang, J., Elkhodairy, K. A., & Elzoghby, A. O. (2019) · Journal of Nanobiotechnology · doi:10.1186/s12951-019-0445-7 · Cited by 45 · see citing works

New insights into deleterious impacts of in vivo glycation on albumin antioxidant activities

Baraka-Vidot, J., Guérin-Dubourg, A., Dubois, F., Payet, B., Bourdon, E., & Rondeau, P. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.01.019 · Cited by 44 · see citing works

Oxidative stress induced carbonylation in human plasma

Madian, A. G., Diaz-Maldonado, N., Gao, Q., & Regnier, F. E. (2011) · Journal of Proteomics · doi:10.1016/j.jprot.2011.07.014 · Cited by 43 · see citing works

Glucose Slows Down the Heat-Induced Aggregation of β-Lactoglobulin at Neutral pH

Pinto, M. D. S., Bouhallab, S., de Carvalho, A. F., Henry, G., Putaux, J., & Léonil, J. (2011) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf2037664 · Cited by 43 · see citing works

Food-Derived Uremic Toxins in Chronic Kidney Disease

Lauriola, M., Farré, R., Evenepoel, P., Overbeek, S. A., & Meijers, B. K. I. (2023) · Toxins · doi:10.3390/toxins15020116 · Cited by 43 · see citing works

Analytical Comparability Assessments of 5 Recombinant CRM 197 Proteins From Different Manufacturers and Expression Systems

Hickey, J. M., Toprani, V. M., Kaur, K., Mishra, R. P. N., Goel, A., Oganesyan, N., Lees, A., Sitrin, R. D., Joshi, S. B., & Volkin, D. B. (2018) · Journal of Pharmaceutical Sciences · doi:10.1016/j.xphs.2018.03.002 · Cited by 42 · see citing works

Protocatechuic and 3,4-Dihydroxyphenylacetic Acids Inhibit Protein Glycation by Binding Lysine through a Metal-Catalyzed Oxidative Mechanism

Tagliazucchi, D., Martini, S., & Conte, A. (2019) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.9b02357 · Cited by 42 · see citing works

Applications and pitfalls of hemoglobin A1C and alternative methods of glycemic monitoring

Lundholm, M. D., Emanuele, M. A., Ashraf, A., & Nadeem, S. (2020) · Journal of Diabetes and its Complications · doi:10.1016/j.jdiacomp.2020.107585 · Cited by 42 · see citing works

Analysis of Hemoglobin Glycation Using Microfluidic CE-MS: A Rapid, Mass Spectrometry Compatible Method for Assessing Diabetes Management

Redman, E. A., Ramos‐Payán, M., Mellors, J. S., & Ramsey, J. M. (2016) · Analytical Chemistry · doi:10.1021/acs.analchem.6b00622 · Cited by 41 · see citing works

Glycation, glycolysis, and neurodegenerative diseases: Is there any connection?

Muronetz, V. I., Melnikova, A. K., Seferbekova, Z., Barinova, K. V., & Schmalhausen, E. V. (2017) · Biochemistry (Moscow) · doi:10.1134/s0006297917080028 · Cited by 41 · see citing works

Review of pentosidine and pyrraline in food and chemical models: formation, potential risks and determination

Li, H., & Yu, S. (2017) · Journal of the Science of Food and Agriculture · doi:10.1002/jsfa.8853 · Cited by 41 · see citing works

Metabolic Signatures of Cystic Fibrosis Identified in Dried Blood Spots For Newborn Screening Without Carrier Identification

DiBattista, A., McIntosh, N., Lamoureux, M., Al-Dirbashi, O. Y., Chakraborty, P. K., & Britz‐McKibbin, P. (2018) · Journal of Proteome Research · doi:10.1021/acs.jproteome.8b00351 · Cited by 41 · see citing works

A New Strategy for Early Diagnosis of Type 2 Diabetes by Standard-Free, Label-Free LC-MS/MS Quantification of Glycated Peptides

Zhang, M., Xu, W. L., & Deng, Y. (2013) · Diabetes · doi:10.2337/db13-0347 · Cited by 40 · see citing works

Dietary Maillard Reaction Products: Implications for Human Health and Disease

Ames, J. M. (2009) · Czech Journal of Food Sciences · doi:10.17221/624-cjfs · Cited by 40 · see citing works

Antioxidant and UV-blocking glucose-crosslinked sericin films with enhanced structural integrity

Oh, S., Park, J., Nam, J., Hyun, Y., Jin, H., & Kwak, H. W. (2021) · Reactive and Functional Polymers · doi:10.1016/j.reactfunctpolym.2021.104942 · Cited by 40 · see citing works

Maillard induced aggregation of individual milk proteins and interactions involved

Cardoso, H. B., Wierenga, P. A., Gruppen, H., & Schols, H. A. (2018) · Food Chemistry · doi:10.1016/j.foodchem.2018.10.061 · Cited by 38 · see citing works

GlyStruct: glycation prediction using structural properties of amino acid residues

Reddy, H. M., Sharma, A. K., Dehzangi, A., Shigemizu, D., Chandra, A. A., & Tsunoda, T. (2019) · BMC Bioinformatics · doi:10.1186/s12859-018-2547-x · Cited by 38 · see citing works

Plant-Derived Agents with Anti-Glycation Activity

Odjakova, M., Popova, E., Al, M., & Mironov, R. (2012) · InTech eBooks · doi:10.5772/48186 · Cited by 39 · see citing works

Transformation of waste cooking oil into C-18 fatty acids using a novel lipase produced by Penicillium chrysogenum through solid state fermentation

Kumar, S., & Negi, S. (2014) · 3 Biotech · doi:10.1007/s13205-014-0268-z · Cited by 37 · see citing works

Non‐enzymatic glycation and glycoxidation protein products in foods and diseases: An interconnected, complex scenario fully open to innovative proteomic studies

Arena, S., Salzano, A. M., Renzone, G., DˈAmbrosio, C., & Scaloni, A. (2013) · Mass Spectrometry Reviews · doi:10.1002/mas.21378 · Cited by 84 · see citing works

Maillard Proteomics: Opening New Pages

Soboleva, A., Schmidt, R., Vikhnina, M., Grishina, T., & Frolov, A. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18122677 · Cited by 47 · see citing works

A perspective on the maillard reaction and the analysis of protein glycation by mass spectrometry

Zhang, Q., Ames, J. M., Smith, R. D., Baynes, J., & Metz, T. (2009) · Journal of Proteome Research · doi:10.1021/pr80085bh · Cited by 2 · see citing works

Protein Glycation in Diabetes as Determined by Mass Spectrometry

Lapolla, A., Molin, L., & Traldi, P. (2013) · International Journal of Endocrinology · doi:10.1155/2013/412103 · Cited by 38 · see citing works

Review Article Protein Glycation in Diabetes as Determined by Mass Spectrometry

Lapolla, A., Molin, L., & Traldi, P. (2013)