Advanced glycoxidation and lipoxidation end products (AGEs and ALEs): an overview of their mechanisms of formation

Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes

Esterbauer, H., Schaur, R. J., & Zollner, H. (1991) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(91)90192-6 · Cited by 6,672

A review of recent studies on malondialdehyde as toxic molecule and biological marker of oxidative stress

Rio, D. D., Stewart, A. J., & Pellegrini, N. (2005) · Nutrition Metabolism and Cardiovascular Diseases · doi:10.1016/j.numecd.2005.05.003 · Cited by 2,789

Advanced glycation end-products: A review

Singh, R., Barden, A., Mori, T., & Beilin, L. (2001) · Diabetologia · doi:10.1007/s001250051591 · Cited by 2,597

Isolation and characterization

Turksen, K. (2006) · Humana Press eBooks · Cited by 2,082

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 1,979

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

Lipid peroxidation: Physiological levels and dual biological effects

Niki, E. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.05.032 · Cited by 1,032

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

Advanced glycation end products and RAGE: a common thread in aging, diabetes, neurodegeneration, and inflammation

Ramasamy, R., Vannucci, S. J., Yan, S. S. D., Herold, K., Yan, S. F., & Schmidt, A. M. (2005) · Glycobiology · doi:10.1093/glycob/cwi053 · Cited by 834

The Advanced Glycation End Product, N∊-(Carboxymethyl)lysine, Is a Product of both Lipid Peroxidation and Glycoxidation Reactions

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

Large-scale fluid/fluid phase separation of proteins and lipids in giant plasma membrane vesicles

Baumgart, T., Hammond, A. T., Sengupta, P., Hess, S. T., Holowka, D. A., Baird, B. A., & Webb, W. W. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0611357104 · Cited by 816

Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase superfamily

Marchitti, S. A., Brocker, C. N., Stagos, D., & Vasiliou, V. (2008) · Expert Opinion on Drug Metabolism & Toxicology · doi:10.1517/17425255.4.6.697 · Cited by 806

Nonenzymatic Browning in Vivo: Possible Process for Aging of Long-Lived Proteins

Monnier, V. M., & Cerami, A. (1981) · Science · doi:10.1126/science.6779377 · Cited by 773

Acrolein: Sources, metabolism, and biomolecular interactions relevant to human health and disease

Stevens, J. F., & Maier, C. S. (2008) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.200700412 · Cited by 756

Global budgets of atmospheric glyoxal and methylglyoxal, and implications for formation of secondary organic aerosols

Fu, T., Jacob, D. J., Wittrock, F., Burrows, J. P., Vrekoussis, M., & Henze, D. K. (2008) · Journal of Geophysical Research Atmospheres · doi:10.1029/2007jd009505 · Cited by 746

Aldehyde Sources, Metabolism, Molecular Toxicity Mechanisms, and Possible Effects on Human Health

O'Brien, P. J., Siraki, A. G., & Shangari, N. (2005) · Critical Reviews in Toxicology · doi:10.1080/10408440591002183 · Cited by 738

Melanoidins produced by the Maillard reaction: Structure and biological activity

Wang, H.-Y., Qian, H., & Yao, W.-R. (2011) · Food Chemistry · doi:10.1016/j.foodchem.2011.03.075 · Cited by 719

Insights into the Interplay of Lewis and Brønsted Acid Catalysts in Glucose and Fructose Conversion to 5-(Hydroxymethyl)furfural and Levulinic Acid in Aqueous Media

Choudhary, V., Mushrif, S. H., Ho, C. R., Anderko, A., Nikolakis, V. A., Marinković, N., Frenkel, A. I., Sandler, S. I., & Vlachos, D. G. (2013) · Journal of the American Chemical Society · doi:10.1021/ja3122763 · Cited by 697

Binding and modification of proteins by methylglyoxal under physiological conditions. A kinetic and mechanistic study with N alpha-acetylarginine, N alpha-acetylcysteine, and N alpha-acetyllysine, and bovine serum albumin.

Lo, T. W. C., Westwood, M. E., McLellan, A. C., Selwood, T., & Thornalley, P. J. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)31635-1 · Cited by 695

Advanced lipid peroxidation end products in oxidative damage to proteins. Potential role in diseases and therapeutic prospects for the inhibitors

Negre‐Salvayre, A., Coatrieux, C., Ingueneau, C., & Salvayre, R. (2008) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0707395 · Cited by 641

Generation and Biological Activities of Oxidized Phospholipids

Bochkov, V. N., Oskolkova, O., Birukov, K. G., Levonen, A., Binder, C. J., & Stöckl, J. (2009) · Antioxidants and Redox Signaling · doi:10.1089/ars.2009.2597 · Cited by 625

N ε-(Carboxyethyl)lysine, a product of the chemical modification of proteins by methylglyoxal, increases with age in human lens proteins

Ahmed, M. U., Frye, E. B., Degenhardt, T. P., Thorpe, S. R., & Baynes, J. (1997) · Biochemical Journal · doi:10.1042/bj3240565 · Cited by 605

Reaction of Monosaccharides with Proteins: Possible Evolutionary Significance

Bunn, H. F., & Higgins, P. J. (1981) · Science · doi:10.1126/science.12192669 · Cited by 598

Identification of Glyoxal and Arabinose as Intermediates in the Autoxidative Modification of Proteins by Glucose

Wells‐Knecht, K. J., Zyzak, D. V., Litchfield, J., Thorpe, S. R., & Baynes, J. (1995) · Biochemistry · doi:10.1021/bi00011a027 · Cited by 594

Pharmacology of methylglyoxal: formation, modification of proteins and nucleic acids, and enzymatic detoxification-A role in pathogenesis and antiproliferative chemotherapy

Thornalley, P. J. (1996) · General Pharmacology: The Vascular System · doi:10.1016/0306-3623(95)02054-3 · Cited by 591

Action des acides amines sur les sucres : formation des melanoidines par voie methodique

Maillard, L. (1912) · Medical Entomology and Zoology · Cited by 574

Chemistry and biochemistry of lipid peroxidation products

Guéraud, F., Atalay, M., Bresgen, N., Gašparović, A. Č., Eckl, P., Laurence Therese, H. U. C., Jouanin, I., Siems, W., & Uchida, K. (2010) · Free Radical Research · doi:10.3109/10715762.2010.498477 · Cited by 570

Formation of pentosidine during nonenzymatic browning of proteins by glucose. Identification of glucose and other carbohydrates as possible precursors of pentosidine in vivo

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

Covalent attachment of 4-hydroxynonenal to glyceraldehyde-3-phosphate dehydrogenase. A possible involvement of intra- and intermolecular cross-linking reaction.

Uchida, K., & Stadtman, E. R. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53264-6 · Cited by 513

Methylglyoxal in living organisms

Kalapos, M. P. (1999) · Toxicology Letters · doi:10.1016/s0378-4274(99)00160-5 · Cited by 507

The Chemistry and Technology of Furfural and its Many By-products

Li, J. Q. (2001) · Chemical Engineering Journal · doi:10.1016/s1385-8947(00)00182-0 · Cited by 499

The use of ozone and associated oxidation processes in drinking water treatment

Camel, V., & Bermond, A. (1998) · Water Research · doi:10.1016/s0043-1354(98)00130-4 · Cited by 465

Mechanism of formation of the Maillard protein cross-link pentosidine. Glucose, fructose, and ascorbate as pentosidine precursors

Grandhee, S. K., & Monnier, V. M. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)99006-x · Cited by 459

Membrane phospholipids, lipoxidative damage and molecular integrity: A causal role in aging and longevity

Pamplona, R. (2008) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.07.003 · Cited by 406

4-Hydroxynonenal as a bioactive marker of pathophysiological processes

Žarković, N. (2003) · Molecular Aspects of Medicine · doi:10.1016/s0098-2997(03)00023-2 · Cited by 398

Dietary Advanced Glycation End Products and Aging

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

Cell activation by glycated proteins. AGE receptors, receptor recognition factors and functional classification of AGEs.

Thornalley, P. J. (1998) · PubMed · Cited by 387

15-Deoxy-Δ12,14-prostaglandin J2

Shibata, T., Kondo, M., Osawa, T., Shibata, N., Kobayashi, M., & Uchida, K. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110314200 · Cited by 387

Methylglyoxal Modification of Protein

Oya, T., Hattori, N., Mizuno, Y., Miyata, S., Maeda, S., Osawa, T., & Uchida, K. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.26.18492 · Cited by 374

New Hemoglobin in Normal Adult Blood

Kunkel, H. G., & Wallenius, G. (1955) · Science · doi:10.1126/science.122.3163.288 · Cited by 371

Protein Adducts Generated from Products of Lipid Oxidation: Focus on HNE and ONE

Sayre, L. M., Lin, D., Yuan, Q., Zhu, X., & Tang, X. (2006) · Drug Metabolism Reviews · doi:10.1080/03602530600959508 · Cited by 364

1,2-Dicarbonyl Compounds in Commonly Consumed Foods

Degen, J., Hellwig, M., & Henle, T. (2012) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf301306g · Cited by 360

the chemistry and technology of furfural and its many by-products

(2000) · Sugar series · doi:10.1016/s0167-7675(00)x8001-3 · Cited by 351

Toxicology and risk assessment of 5‐Hydroxymethylfurfural in food

Abraham, K., Gürtler, R., Berg, K., Heinemeyer, G., Lampen, A., & Appel, K. E. (2011) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201000564 · Cited by 340

Application of the Hard and Soft, Acids and Bases (HSAB) Theory to Toxicant–Target Interactions

LoPachin, R. M., Gavin, T., DeCaprio, A. P., & Barber, D. S. (2011) · Chemical Research in Toxicology · doi:10.1021/tx2003257 · Cited by 327

Advanced glycation end products and neurodegenerative diseases: Mechanisms and perspective

Li, J., Liu, D., Sun, L., Lu, Y., & Zhang, Z. (2012) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2012.02.018 · Cited by 326

The importance of lipid-derived malondialdehyde in diabetes mellitus

Slatter, D. A., Bolton, C., & Bailey, A. J. (2000) · Diabetologia · doi:10.1007/s001250051342 · Cited by 318

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 308

Role of advanced glycation end products (AGEs) and oxidative stress in vascular complications in diabetes

Yamagishi, S., Maeda, S., Matsui, T., Ueda, S., Fukami, K., & Okuda, S. (2011) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2011.03.014 · Cited by 301

Current Status of Acrolein as a Lipid Peroxidation Product

Uchida, K. (1999) · Trends in Cardiovascular Medicine · doi:10.1016/s1050-1738(99)00016-x · Cited by 299

Molecular Basis of Arterial Stiffening: Role of Glycation – A Mini-Review

Sell, D. R., & Monnier, V. M. (2012) · Gerontology · doi:10.1159/000334668 · Cited by 298

Oxidized Membrane Vesicles and Blebs From Apoptotic Cells Contain Biologically Active Oxidized Phospholipids That Induce Monocyte-Endothelial Interactions

Huber, J., Vales, A., Mitulović, G., Blumer, M. J. F., Schmid, R., Witztum, J. L., Binder, B. R., & Leitinger, N. (2002) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/hq0102.101525 · Cited by 296

Intervention strategies to inhibit protein carbonylation by lipoxidation‐derived reactive carbonyls

Aldini, G., Dalle‐Donne, I., Facino, R. M., Milzani, A., & Carini, M. (2006) · Medicinal Research Reviews · doi:10.1002/med.20073 · Cited by 292

Maillard Reaction

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

Kinetic study on the Maillard reaction. Consideration of sugar reactivity

Laroque, D., Inisan, C., Berger, C., Vouland, É., Dufossé, L., & Guérard, F. (2008) · Food Chemistry · doi:10.1016/j.foodchem.2008.05.033 · Cited by 283

Protein Modification by Methylglyoxal: Chemical Nature and Synthetic Mechanism of a Major Fluorescent Adduct

Shipanova, I. N., Glomb, M. A., & Nagaraj, R. H. (1997) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1997.0195 · Cited by 277

Routes to 4-Hydroxynonenal: Fundamental Issues in the Mechanisms of Lipid Peroxidation

Schneider, C. G., Porter, N. A., & BRASH, A. R. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.r800001200 · Cited by 275

Mechanism for the formation of methylglyoxal from triosephosphates

Richard, J. P. (1993) · Biochemical Society Transactions · doi:10.1042/bst0210549 · Cited by 272

Molecular Mechanisms of 4-Hydroxy-2-nonenal and Acrolein Toxicity: Nucleophilic Targets and Adduct Formation

LoPachin, R. M., Gavin, T., Petersen, D. R., & Barber, D. S. (2009) · Chemical Research in Toxicology · doi:10.1021/tx900147g · Cited by 266

Forty years of furosine – Forty years of using Maillard reaction products as indicators of the nutritional quality of foods

Erbersdobler, H. F., & Somoza, V. (2007) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.200600154 · Cited by 261

The metabolism of acetone in rat.

Casazza, J. P., Felver, M., & Veech, R. L. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)43646-5 · Cited by 260

Methylglyoxal metabolism and diabetic complications: roles of aldose reductase, glyoxalase-I, betaine aldehyde dehydrogenase and 2-oxoaldehyde dehydrogenase

Jagt, D. L. V., & Hunsaker, L. A. (2003) · Chemico-Biological Interactions · doi:10.1016/s0009-2797(02)00212-0 · Cited by 256

Physiological relevance of dietary melanoidins

Morales, F. J., Somoza, V., & Fogliano, V. (2010) · Amino Acids · doi:10.1007/s00726-010-0774-1 · Cited by 256

The tandem of free radicals and methylglyoxal

Kalapos, M. P. (2007) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2007.11.009 · Cited by 252

METABOLISM OF METHYLGLYOXAL IN MICROORGANISMS

Cooper, R. A. (1984) · Annual Review of Microbiology · doi:10.1146/annurev.mi.38.100184.000405 · Cited by 252

Nonenzymatic Glycation of Bovine Serum Albumin by Fructose (Fructation)

Suárez, G., Rajaram, R., Oronsky, A. L., & Gawinowicz, M. A. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)84904-9 · Cited by 244

Characterization of 4-Oxo-2-nonenal as a Novel Product of Lipid Peroxidation

Lee, S. H., & Blair, I. A. (2000) · Chemical Research in Toxicology · doi:10.1021/tx000101a · Cited by 244

Chemical modification of proteins by methylglyoxal.

Degenhardt, T. P., Thorpe, S. R., & Baynes, J. (1998) · PubMed · Cited by 243

Mutarotation, Hydrolysis, and Rearrangement Reactions of Glycosylamines1

Isbell, H. S., & Frush, H. L. (1958) · The Journal of Organic Chemistry · doi:10.1021/jo01103a019 · Cited by 237

Catabolism of polyamines

Seiler, N. (2004) · Amino Acids · doi:10.1007/s00726-004-0070-z · Cited by 236

Structural Definition of Early Lysine and Histidine Adduction Chemistry of 4-Hydroxynonenal

Nadkarni, D. V., & Sayre, L. M. (1995) · Chemical Research in Toxicology · doi:10.1021/tx00044a014 · Cited by 235

Flavour chemistry of methylglyoxal and glyoxal

Wang, Y., & Ho, C. (2012) · Chemical Society Reviews · doi:10.1039/c2cs35025d · Cited by 230

Insights into Oxidative Stress: The Isoprostanes

Montuschi, P., Barnes, P. J., & Roberts, L. J. (2007) · Current Medicinal Chemistry · doi:10.2174/092986707780059607 · Cited by 230

Mammalian plasma and tissue-bound semicarba ide-sensitive amine oxidases: Biochemical, pharmacological and toxicological aspects

Lyles, G. A. (1996) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/1357-2725(95)00130-1 · Cited by 228

Molecular characteristics of methylglyoxal-modified bovine and human serum albumins. Comparison with glucose-derived advanced glycation endproduct-modified serum albumins

Westwood, M. E., & Thornalley, P. J. (1995) · Journal of Protein Chemistry · doi:10.1007/bf01886793 · Cited by 225

The Maillard reaction in the human body. The main discoveries and factors that affect glycation

Tessier, F. J. (2009) · Pathologie Biologie · doi:10.1016/j.patbio.2009.09.014 · Cited by 222

Acrolein – a pulmonary hazard

Bein, K., & Leikauf, G. D. (2011) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201100279 · Cited by 214

The road to advanced glycation end products: a mechanistic perspective

Cho, S.-J., Roman, G., Yeboah, F., & Konishi, Y. (2007) · Current Medicinal Chemistry · doi:10.2174/092986707780830989 · Cited by 213

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

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

A Comparative Review of Petroleum‐Based and Bio‐Based Acrolein Production

Liu, L., Ye, X. P., & Bozell, J. J. (2012) · ChemSusChem · doi:10.1002/cssc.201100447 · Cited by 210

Fructose-mediated non-enzymatic glycation: sweet coupling or bad modification

Schalkwijk, C. G., Stehouwer, C. D. A., & van Hinsbergh, V. W. M. (2004) · Diabetes/Metabolism Research and Reviews · doi:10.1002/dmrr.488 · Cited by 206

Sucrose, High-Fructose Corn Syrup, and Fructose, Their Metabolism and Potential Health Effects: What Do We Really Know?

Rippe, J. M., & Angelopoulos, T. J. (2013) · Advances in Nutrition · doi:10.3945/an.112.002824 · Cited by 203

Sugars as tobacco ingredient: Effects on mainstream smoke composition

Talhout, R., Opperhuizen, A., & van Amsterdam, J. (2006) · Food and Chemical Toxicology · doi:10.1016/j.fct.2006.06.016 · Cited by 202

Aldehydic lipid peroxidation products derived from linoleic acid

Spiteller, P. (2001) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/s1388-1981(01)00100-7 · Cited by 201

Advanced lipoxidation end-products

Pamplona, R. (2011) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2011.01.007 · Cited by 200

Determination of toxic carbonyl compounds in cigarette smoke

Fujioka, K., & Shibamoto, T. (2006) · Environmental Toxicology · doi:10.1002/tox.20153 · Cited by 197

Oxidatively modified autoantigens in autoimmune diseases

Kurien, B. T., Hensley, K., Bachmann, M. P., & Scofield, R. H. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.05.020 · Cited by 189

Structure and Mechanism of Formation of Human Lens Fluorophore LM-1

Tessier, F. J., Obrenovich, M. E., & Monnier, V. M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.30.20796 · Cited by 188

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

Trans-4-hydroxy-2-hexenal, a product of n-3 fatty acid peroxidation: Make some room HNE…

Long, E. K., & Picklo, M. J. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.03.015 · Cited by 178

New Insights Regarding the Autoxidation of Polyunsaturated Fatty Acids

Yin, H., & Porter, N. A. (2004) · Antioxidants and Redox Signaling · doi:10.1089/ars.2005.7.170 · Cited by 177

Degradation of Glucose: Reinvestigation of Reactive α-Dicarbonyl Compounds †

Gobert, J., & Glomb, M. A. (2009) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf9019085 · Cited by 175

The cytotoxic mechanism of glyoxal involves oxidative stress

Shangari, N., & O’Brien, P. J. (2004) · Biochemical Pharmacology · doi:10.1016/j.bcp.2004.06.013 · Cited by 174

Effects of Smoking Cessation on Eight Urinary Tobacco Carcinogen and Toxicant Biomarkers

Carmella, S. G., Chen, M., Han, S., Briggs, A., Jensen, J., Hatsukami, D. K., & Hecht, S. S. (2009) · Chemical Research in Toxicology · doi:10.1021/tx800479s · Cited by 174

Protein fructosylation: fructose and the Maillard reaction

Dills, W. (1993) · The American Journal of Clinical Nutrition · doi:10.1093/ajcn/58.5.779s · Cited by 171

Toxicology and risk assessment of acrolein in food

Abraham, K., Andres, S., Palavinskas, R., Berg, K., Appel, K. E., & Lampen, A. (2011) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201100481 · Cited by 170

Rapid Formation of Advanced Glycation End Products by Intermediate Metabolites of Glycolytic Pathway and Polyol Pathway

Hamada, Y., Araki, N., Koh, N., Nakamura, J., Horiuchi, S., & Hotta, N. (1996) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1996.1695 · Cited by 169

4-Oxo-2-nonenal Is Both More Neurotoxic and More Protein Reactive than 4-Hydroxy-2-nonenal

Lin, D., Lee, H., Liu, Q., Perry, G. L., Smith, M. A., & Sayre, L. M. (2005) · Chemical Research in Toxicology · doi:10.1021/tx050080q · Cited by 164

An update on advanced glycation endproducts and atherosclerosis

Turco, S. D., & Basta, G. (2012) · BioFactors · doi:10.1002/biof.1018 · Cited by 157

Evidence for the Formation of Adducts andS-(Carboxymethyl)cysteine on Reaction of α-Dicarbonyl Compounds with Thiol Groups on Amino Acids, Peptides, and Proteins

Zeng, J., & Davies, M. J. (2005) · Chemical Research in Toxicology · doi:10.1021/tx050074u · Cited by 153

The pathogenic role of Maillard reaction in the aging eye

Nagaraj, R. H., Linetsky, M. D., & Stitt, A. W. (2010) · Amino Acids · doi:10.1007/s00726-010-0778-x · Cited by 151

Accumulation of fructosyl-lysine and advanced glycation end products in the kidney, retina and peripheral nerve of streptozotocin-induced diabetic rats

Karachalias, N., Babaei‐Jadidi, R., Ahmed, N., & Thornalley, P. J. (2003) · Biochemical Society Transactions · doi:10.1042/bst0311423 · Cited by 150

Advanced Glycation End Products and Diabetic Cardiovascular Disease

Prasad, A., Bekker, P., & Tsimikas, S. (2012) · Cardiology in Review · doi:10.1097/crd.0b013e318244e57c · Cited by 150

Dietary advanced glycation endproducts (AGEs) and their health effects – PRO

Šebeková, K., & Somoza, V. (2007) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.200700035 · Cited by 148

Covalent adduction of nucleophilic amino acids by 4-hydroxynonenal and 4-oxononenal

Doorn, J. A., & Petersen, D. R. (2003) · Chemico-Biological Interactions · doi:10.1016/s0009-2797(02)00178-3 · Cited by 147

Cross-linking of proteins by maillard processes: characterization and detection of lysine–arginine cross-links derived from glyoxal and methylglyoxal

Lederer, M. O., & Klaiber, R. (1999) · Bioorganic & Medicinal Chemistry · doi:10.1016/s0968-0896(99)00212-6 · Cited by 146

Glycation research in amino acids: a place to call home

Rabbani, N., & Thornalley, P. J. (2010) · Amino Acids · doi:10.1007/s00726-010-0782-1 · Cited by 145

3-Deoxyglucosone: metabolism, analysis, biological activity, and clinical implication

Niwa, T. (1999) · Journal of Chromatography B Biomedical Sciences and Applications · doi:10.1016/s0378-4347(99)00113-9 · Cited by 144

Amides Are Novel Protein Modifications Formed by Physiological Sugars

Glomb, M. A., & Pfahler, C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103557200 · Cited by 144

Fate of 4-hydroxynonenal in vivo: disposition and metabolic pathways

Alary, J., Guéraud, F., & Cravedi, J. (2003) · Molecular Aspects of Medicine · doi:10.1016/s0098-2997(03)00012-8 · Cited by 143

3,4-Dideoxyglucosone-3-ene (3,4-DGE): A cytotoxic glucose degradation product in fluids for peritoneal dialysis

Lindén, T., Cohen, A. S., Deppisch, R. M., Kjellstrand, P. T. T., & Wieslander, A. P. (2002) · Kidney International · doi:10.1046/j.1523-1755.2002.00490.x · Cited by 143

Formation Pathways for Lysine-Arginine Cross-links Derived from Hexoses and Pentoses by Maillard Processes

Biemel, K. M., Reihl, O., Conrad, J., & Lederer, M. O. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102035200 · Cited by 141

Formation of Crossline as a Fluorescent Advanced Glycation End Productin Vitroandin Vivo

Obayashi, H., Nakano, K., Shigeta, H., Yamaguchi, M., Yoshimori, K., Fukui, M., Fujii, M., Kitagawa, Y., Nakamura, N., Nakamura, K., et al. (1996) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1996.1308 · Cited by 137

The naturally occurring furanones: formation and function from pheromone to food

Slaughter, J. C. (1999) · Biological reviews/Biological reviews of the Cambridge Philosophical Society · doi:10.1017/s0006323199005332 · Cited by 135

Diabetic Kidney Stone Formers Excrete More Oxalate and Have Lower Urine pH Than Nondiabetic Stone Formers

Eisner, B. H., Porten, S. P., Bechis, S. K., & Stoller, M. L. (2010) · The Journal of Urology · doi:10.1016/j.juro.2010.02.007 · Cited by 129

2-Aminoadipic acid is a marker of protein carbonyl oxidation in the aging human skin: effects of diabetes, renal failure and sepsis

Sell, D. R., Strauch, C., Shen, W., & Monnier, V. M. (2007) · Biochemical Journal · doi:10.1042/bj20061645 · Cited by 126

Roles of 3-nitrotyrosine- and 4-hydroxynonenal-modified brain proteins in the progression and pathogenesis of Alzheimer's disease

Butterfield, D. A., Reed, T. T., & Rukhsana Sultana, A. (2010) · Free Radical Research · doi:10.3109/10715762.2010.520014 · Cited by 125

Acid-Stable Fluorescent Advanced Glycation End Products: Vesperlysines A, B, and C Are Formed as Crosslinked Products in the Maillard Reaction between Lysine or Proteins with Glucose

Nakamura, K., Nakazawa, Y., & Ienaga, K. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.6262 · Cited by 122

α-Oxoaldehyde metabolism and diabetic complications

Beisswenger, P. J., Howell, S. K., Nelson, R. G., Mauer, M. S., & Szwergold, B. S. (2003) · Biochemical Society Transactions · doi:10.1042/bst0311358 · Cited by 121

Formation of α-dicarbonyl fragments from mono- and disaccharides under caramelization and Maillard reaction conditions

Hollnagel, A., & Kroh, L. W. (1998) · Zeitschrift für Lebensmittel-Untersuchung und -Forschung. B, Referate und Lebensmittelrecht · doi:10.1007/s002170050294 · Cited by 120

A synopsis of the process of lipid peroxidation since the discovery of the essential fatty acids

Catalá, Á. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.07.087 · Cited by 118

A New Mechanism of the Maillard Reaction Involving Sugar Fragmentation and Free Radical Formation

Namiki, M., & Hayashi, T. (1983) · ACS symposium series · doi:10.1021/bk-1983-0215.ch002 · Cited by 117

Fructosamine 3-kinase is involved in an intracellular deglycation pathway in human erythrocytes

Delpierre, G., Collard, F., Fortpied, J., & SCHAFTINGEN, E. V. (2002) · Biochemical Journal · doi:10.1042/bj20020325 · Cited by 115

Sugar Fragmentation in the Maillard Reaction Cascade: Formation of Short-Chain Carboxylic Acids by a New Oxidative α-Dicarbonyl Cleavage Pathway

Davídek, T., Robert, F., Devaud, S., Vera, F. A., & Blank, I. (2006) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf060668i · Cited by 113

Nϵ-(3-Methylpyridinium)lysine, a Major Antigenic Adduct Generated in Acrolein-modified Protein

Furuhata, A., Ishii, T., Kumazawa, S., Yamada, T., Nakayama, T., & Uchida, K. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m309401200 · Cited by 112

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

Detection and identification of a protein-bound imidazolone resulting from the reaction of arginine residues and methylglyoxal

Henle, T., Walter, A. W., Hae�ner, R., & Klostermeyer, H. (1994) · European Food Research and Technology · doi:10.1007/bf01192954 · Cited by 107

Model Studies on Protein Side Chain Modification by 4-Oxo-2-nonenal

Zhang, W., Liu, J., Xu, G., Yuan, Q., & Sayre, L. M. (2003) · Chemical Research in Toxicology · doi:10.1021/tx020105a · Cited by 107

Interactions of glutathione transferases with 4-hydroxynonenal

Balogh, L. M., & Atkins, W. M. (2011) · Drug Metabolism Reviews · doi:10.3109/03602532.2011.558092 · Cited by 105

Advances in glyoxalase research. Glyoxalase expression in malignancy, anti-proliferative effects of methylglyoxal, glyoxalase I inhibitor diesters and S-d-lactoylglutathione, and methylglyoxal-modified protein binding and endocytosis by the advanced glycation endproduct receptor

Thornalley, P. J. (1995) · Critical Reviews in Oncology/Hematology · doi:10.1016/1040-8428(94)00149-n · Cited by 105

Chemical Modifications of Peptides and Their Impact on Food Properties

Lancker, F. V., Adams, A., & KIMPE, N. D. (2011) · Chemical Reviews · doi:10.1021/cr200032j · Cited by 104

Detection and quantification of pentosidine in foods

Henle, T., Schwarzenbolz, U., & Klostermeyer, H. (1997) · Zeitschrift für Lebensmittel-Untersuchung und -Forschung. B, Referate und Lebensmittelrecht · doi:10.1007/s002170050043 · Cited by 104

METHYLGLYOXAL, DIABETES MELLITUS AND DIABETIC COMPLICATIONS

Jagt, D. L. V. (2008) · Drug metabolism and drug interactions · doi:10.1515/dmdi.2008.23.1-2.93 · Cited by 104

Mass Spectroscopic Characterization of Protein Modification by 4-Hydroxy-2-(E)-nonenal and 4-Oxo-2-(E)-nonenal

Liu, Z., Minkler, P. E., & Sayre, L. M. (2003) · Chemical Research in Toxicology · doi:10.1021/tx0300030 · Cited by 102

Glyoxal Formation and Its Role in Endogenous Oxalate Synthesis

Lange, J. N., Wood, K. D., Knight, J. L., Assimos, D. G., & Holmes, R. P. (2012) · Advances in Urology · doi:10.1155/2012/819202 · Cited by 97

Involvement of the Toxic AGEs (TAGE)-RAGE System in the Pathogenesis of Diabetic Vascular Complications: A Novel Therapeutic Strategy

Takeuchi, M., Takino, J.-I., & Yamagishi, S. (2010) · Current Drug Targets · doi:10.2174/1389450111009011468 · Cited by 96

Formation of a dihydropyridine derivative as a potential cross‐link derived from malondialdehyde in physiological systems

Slatter, D. A., Murray, M., & Bailey, A. J. (1998) · FEBS Letters · doi:10.1016/s0014-5793(97)01554-8 · Cited by 95

Toxicity of glyoxals – role of oxidative stress, metabolic detoxification and thiamine deficiency

Shangari, N., Bruce, W. R., Poon, R. W. M., & O'Brien, P. J. (2003) · Biochemical Society Transactions · doi:10.1042/bst0311390 · Cited by 94

Acetone catabolism by cytochrome P450 2E1: studies with CYP2E1-null mice

Bondoc, F. Y., Bao, Z., Hu, W., Gonzalez, F. J., Wang, Y., Yang, C. S., & Hong, J. (1999) · Biochemical Pharmacology · doi:10.1016/s0006-2952(99)00111-2 · Cited by 94

3‐Deoxy‐glucosone is an Intermediate in the Formation of Furfurals from D ‐Glucose.

Jadhav, H. S., Pedersen, C. M., Sølling, T. I., & Bols, M. (2011) · ChemSusChem · doi:10.1002/cssc.201100249 · Cited by 94

METHYLGLYOXAL AND GLUCOSE METABOLISM: A HISTORICAL PERSPECTIVE AND FUTURE AVENUES FOR RESEARCH

Kalapos, M. P. (2008) · Drug metabolism and drug interactions · doi:10.1515/dmdi.2008.23.1-2.69 · Cited by 92

Phospholipid Hydroxyalkenals

Hoff, H. F., O'NEIL, J. A., Wu, Z., Hoppe, G., & Salomon, R. G. (2003) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000051407.42536.73 · Cited by 85

Experimental studies on the role of fructose in the development of diabetic complications.

Sakai, M., Oimomi, M., & Kasuga, M. (2002) · PubMed · doi:10.24546/00318725 · Cited by 83

Methylglyoxal production in vascular smooth muscle cells from different metabolic precursors

Dhar, A., Desai, K. M., Kazachmov, M., Yu, P. H., & Wu, L. (2008) · Metabolism · doi:10.1016/j.metabol.2008.04.014 · Cited by 83

The role of dicarbonyl compounds in non-enzymatic crosslinking: a structure–activity study

Meade, S. J., Miller, A. G., & Gerrard, J. A. (2003) · Bioorganic & Medicinal Chemistry · doi:10.1016/s0968-0896(02)00564-3 · Cited by 79

Reactions of Lipid-derived Malondialdehyde with Collagen

Slatter, D. A., Paul, R. G., Murray, M., & Bailey, A. J. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.28.19661 · Cited by 78

Chemical Modification of Proteins by Lipids in Diabetes

Baynes, J. (2003) · Clinical Chemistry and Laboratory Medicine (CCLM) · doi:10.1515/cclm.2003.179 · Cited by 77

Advanced lipoxidation end‐products mediate lipid‐induced glomerular injury: role of receptor‐mediated mechanisms

Iacobini, C., Menini, S., Ricci, P. C., Scipioni, A., Sansoni, V., Mazzitelli, G., Cordone, S., Pesce, C. M., Pugliese, F. R., Pricci, F., et al. (2009) · The Journal of Pathology · doi:10.1002/path.2536 · Cited by 76

Identification and quantification of six major α-dicarbonyl process contaminants in high-fructose corn syrup

Gensberger‐Reigl, S., Mittelmaier, S., Glomb, M. A., & Pischetsrieder, M. (2012) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-012-5817-x · Cited by 75

MOLECULAR ENZYMOLOGY OF THE GLYOXALASE SYSTEM

Mannervik, B. (2008) · Drug metabolism and drug interactions · doi:10.1515/dmdi.2008.23.1-2.13 · Cited by 74

Structure of advanced Maillard reaction products and their pathological role

Monnier, V. M., Nagaraj, R. H., Portero‐Otín, M., Glomb, M. A., Elgawish, A.-H., Sell, D. R., & Friedlander, M. A. (1996) · Nephrology Dialysis Transplantation · doi:10.1093/ndt/11.supp5.20 · Cited by 74

Identification of Nω-carboxymethylarginine as a novel acid-labile advanced glycation end product in collagen

Iijima, K., Murata, M., Takahara, H., Irie, S., & Fujimoto, D. (2000) · Biochemical Journal · doi:10.1042/bj3470023 · Cited by 74

Identification of a New Cross-link and Unique Histidine Adduct from Bovine Serum Albumin Incubated with Malondialdehyde

Slatter, D. A., Avery, N. C., & Bailey, A. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m310608200 · Cited by 73

Minor Strecker degradation products of phenylalanine and phenylglycine

Adamiec, J., Rössner, J., Velı́šek, J., Cejpek, K., & ŠAVEL, J. (2001) · European Food Research and Technology · doi:10.1007/s002170000234 · Cited by 73

Formation of Arginine Modifications in a Model System of N α - tert -Butoxycarbonyl (Boc)-Arginine with Methylglyoxal

Klöpfer, A., Spanneberg, R., & Glomb, M. A. (2010) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf103116c · Cited by 73

Production of 1,2-Propanediol from Glycerol in Saccharomyces cerevisiae

Jung, J. Y. (2011) · Journal of Microbiology and Biotechnology · doi:10.4014/jmb.1103.03009 · Cited by 70

Anaerobic vs aerobic pathways of carbonyl and oxidant stress in human lens and skin during aging and in diabetes: A comparative analysis

Fan, X., Sell, D. R., Zhang, J., Nemet, I., Theves, M., Lu, J., Strauch, C., Halushka, M. K., & Monnier, V. M. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.06.003 · Cited by 70

Identification of N(omega)-carboxymethylarginine as a novel acid-labileadvanced glycation end product in collagen.

Iijima, K., Murata, M., Takahara, H., et al. (2000) · PubMed · Cited by 69

Catalysis and Specificity in Enzymes: A Study of Triosephosphate Isomerase and Comparison with Methyl Glyoxal Synthase

Cui, Q., & Karplus, M. (2003) · Advances in protein chemistry · doi:10.1016/s0065-3233(03)66008-0 · Cited by 68

Raman spectroscopy of glyoxal oligomers in aqueous solutions

Avzianova, E., & Brooks, S. D. (2012) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2012.09.050 · Cited by 68

Isoketals: highly reactive γ-ketoaldehydes formed from the H2-isoprostane pathway

Davies, S. S., Amarnath, V., & Roberts, L. J. (2003) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2003.10.007 · Cited by 67

Mass Spectroscopic Characterization of Protein Modification by Malondialdehyde

Ishii, T., Kumazawa, S., Sakurai, T., Nakayama, T., & Uchida, K. (2005) · Chemical Research in Toxicology · doi:10.1021/tx050231p · Cited by 66

Conversion of Arginine into Ornithine by Advanced Glycation in Senescent Human Collagen and Lens Crystallins

Sell, D. R., & Monnier, V. M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408946200 · Cited by 64

Increased erythrocyte 3-DG and AGEs in diabetic hemodialysis patients: Role of the polyol pathway

Tsukushi, S., Katsuzaki, T., Aoyama, I., Takayama, F., Miyazaki, T., Shimokata, K., & Niwa, T. (1999) · Kidney International · doi:10.1046/j.1523-1755.1999.00418.x · Cited by 63

Identification and Determination of α-Dicarbonyl Compounds Formed in the Degradation of Sugars

Usui, T., Yanagisawa, S., OHGUCHI, M., YOSHINO, M., Kawabata, R., KISHIMOTO, J., Arai, Y., Kaoru, A. I. D. A., Watanabe, H., & Hayase, F. (2007) · Bioscience Biotechnology and Biochemistry · doi:10.1271/bbb.70229 · Cited by 60

Chemistry and biochemistry of lipid peroxidation products. Free Radic Res

Guéraud, F., Atalay, M., Bresgen, N., et al. (2010) · Cited by 60

On the reaction of glyoxal with proteins

Schwarzenbolz, U., Henle, T., Haeßner, R., & Klostermeyer, H. (1997) · Zeitschrift für Lebensmittel-Untersuchung und -Forschung. B, Referate und Lebensmittelrecht · doi:10.1007/s002170050137 · Cited by 59

Transport of the Advanced Glycation End Products Alanylpyrraline and Pyrralylalanine by the Human Proton-Coupled Peptide Transporter hPEPT1

Geißler, S., Hellwig, M., Zwarg, M., Markwárdt, F., Henle, T., & Brandsch, M. (2010) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf903791u · Cited by 59

Pyrraline Ether Crosslinks as a Basis for Protein Crosslinking by the Advanced Maillard Reaction in Aging and Diabetes

Nagaraj, R. H., Portero‐Otín, M., & Monnier, V. M. (1996) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1996.0019 · Cited by 58

α‐Dicarbonyl Compounds—Key Intermediates for the Formation of Carbohydrate‐based Melanoidins

Kroh, L. W., Fiedler, T., & Wagner, J. (2008) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1433.058 · Cited by 58

Mercapturic Acid Conjugates of 4-Hydroxy-2-nonenal and 4-Oxo-2-nonenal Metabolites Are in Vivo Markers of Oxidative Stress

Kuiper, H. C., Miranda, C. L., Sowell, J. D., & Stevens, J. F. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802797200 · Cited by 57

Nonenzymatic browning reactions of retro-aldol degradation products of carbohydrates

Cämmerer, B., Wedzicha, B. L., & Kroh, L. W. (1999) · European Food Research and Technology · doi:10.1007/s002170050490 · Cited by 57

The dual face of endogenous α-aminoketones: Pro-oxidizing metabolic weapons

Bechara, E. J. H., Dutra, F., Cardoso, V. E. S., Sartori, A., Olympio, K. P. K., Penatti, C. A. A., Adhikari, A., & Assunção, N. A. (2007) · Comparative Biochemistry and Physiology Part C: Toxicology & Pharmacology · doi:10.1016/j.cbpc.2006.07.004 · Cited by 57

Imidazolone, a novel advanced glycation end product, is present at high levels in kidneys of rats with streptozotocin‐induced diabetes

Niwa, T., Katsuzaki, T., Ishizaki, Y., Hayase, F., Miyazaki, T., Uematsu, T., Tatemichi, N., & Takei, Y. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00362-1 · Cited by 56

Accelerated Formation of Nϵ-(carboxymethyl) Lysine, an Advanced Glycation End Product, by Glyoxal and 3-Deoxyglucosone in Cultured Rat Sensory Neurons

Niwa, H., Takeda, A., Wakai, M., Miyata, T., Yasuda, Y., Mitsuma, T., Kurokawa, K., & Sobue, G. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.8899 · Cited by 56

3-Deoxyfructose Concentrations are Increased in Human Plasma and Urine in Diabetes

Wells‐Knecht, K. J., Lyons, T. J., McCance, D. R., Thorpe, S. R., Feather, M. S., & Baynes, J. (1994) · Diabetes · doi:10.2337/diab.43.9.1152 · Cited by 55

Formation of .EPSILON.-(2-formyl-5-hydroxymethyl-pyrrol-1-yl)-L-norleucine in the maillard reaction between D-glucose and L-lysine.

Nakayama, T., Hayase, F., & Kato, H. (1980) · Agricultural and Biological Chemistry · doi:10.1271/bbb1961.44.1201 · Cited by 54

Glyoxal formation by Fenton-induced degradation of carbohydrates and related compounds

Manini, P., Pietra, P. L., Panzella, L., Napolitano, A., & d’Ischia, M. (2006) · Carbohydrate Research · doi:10.1016/j.carres.2006.03.027 · Cited by 53

Proteomic Analysis of Arginine Adducts on Glyoxal-modified Ribonuclease

Cotham, W. E., Metz, T., Ferguson, P. L., Brock, J. W. C., Hinton, D. J. S., Thorpe, S. R., Baynes, J., & Ames, J. M. (2004) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m400002-mcp200 · Cited by 53

N -(Carboxymethyl)lysine and 3-DG-Imidazolone Are Major AGE Structures in Protein Modification by 3-Deoxyglucosone

Jono, T. (2004) · The Journal of Biochemistry · doi:10.1093/jb/mvh124 · Cited by 51

[104] Methylglyoxal synthase

Cooper, R. A. (1975) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(75)41106-5 · Cited by 50

Kinetic and structural features of betaine aldehyde dehydrogenases: Mechanistic and regulatory implications

Muñoz‐Clares, R. A., Díaz‐Sánchez, Á. G., González‐Segura, L., & Montiel, C. (2009) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2009.09.006 · Cited by 48

Formation of 2,5-Dimethyl-4-hydroxy-3(2H)-furanone through Methylglyoxal: A Maillard Reaction Intermediate

Wang, Y., & Ho, C. (2008) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf8012025 · Cited by 48

Differences in glyoxal and methylglyoxal metabolism determine cellular susceptibility to protein carbonylation and cytotoxicity

Yang, K., Dong, Q., Delaney, S., Mehta, R., Bruce, W. R., & O’Brien, P. J. (2011) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2011.02.012 · Cited by 48

Modulation of Insulin Action by Advanced Glycation Endproducts: A New Player in the Field

Schalkwijk, C. G., Brouwers, O., & Stehouwer, C. D. A. (2008) · Hormone and Metabolic Research · doi:10.1055/s-0028-1082085 · Cited by 47

Quantitative Analysis of Acrolein-Specific Adducts Generated during Lipid Peroxidation–Modification of Proteins in Vitro: Identification of Nτ-(3-Propanal)histidine as the Major Adduct

Maeshima, T., Honda, K., Chikazawa, M., Shibata, T., Kawai, Y., Akagawa, M., & Uchida, K. (2012) · Chemical Research in Toxicology · doi:10.1021/tx3000818 · Cited by 47

Exploring Post-translational Arginine Modification Using Chemically Synthesized Methylglyoxal Hydroimidazolones

Wang, T., Kartika, R., & Spiegel, D. A. (2012) · Journal of the American Chemical Society · doi:10.1021/ja301994d · Cited by 47

Elevated level of methylglyoxal during diabetic ketoacidosis and its recovery phase

Turk, Z., Nemet, I., Varga‐Defterdarovič, L., & Car, N. (2006) · Diabetes & Metabolism · doi:10.1016/s1262-3636(07)70266-5 · Cited by 47

Methylglyoxal determination from different carbohydrates during heat processing

Homoki-Farkas, P., Örsi, F., & Kroh, L. W. (1997) · Food Chemistry · doi:10.1016/s0308-8146(96)00273-7 · Cited by 46

Site-specific modification of positively-charged surfaces on human serum albumin by malondialdehyde

Ishii, T., Ito, S., Kumazawa, S., Sakurai, T., Yamaguchi, S., Mori, T., Nakayama, T., & Uchida, K. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.03.140 · Cited by 46

In vitro production of long chain pyrrole fatty esters from carbonyl-amine reactions.

Hidalgo, F. J., & Zamora, R. (1995) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)40058-6 · Cited by 46

Chapter 31 Some aspects of the pathophysiology of semicarbazide-sensitive amine oxidase enzymes

Callingham, B. A., Crosbie, A. E., & Rous, B. (1995) · Progress in brain research · doi:10.1016/s0079-6123(08)61227-3 · Cited by 45

Structure−Reactivity Relationships of Flavan-3-ols on Product Generation in Aqueous Glucose/Glycine Model Systems

Noda, Y., & Peterson, D. G. (2007) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf063423e · Cited by 45

Identification of the Modified Structure of Arginine Residues in Proteins with 3-Deoxyglucosone, a Maillard Reaction Intermediate

Hayase, F., Konishi, Y., & Kato, H. (1995) · Bioscience Biotechnology and Biochemistry · doi:10.1271/bbb.59.1407 · Cited by 45

Aldose Reductase, Oxidative Stress and Diabetic Cardiovascular Complications

Vedantham, S., Ananthakrishnan, R., Schmidt, A. M., & Ramasamy, R. (2012) · Cardiovascular & Hematological Agents in Medicinal Chemistry · doi:10.2174/187152512802651097 · Cited by 45

Reactivity of Thermally Treated α-Dicarbonyl Compounds

Pfeifer, Y. V., Haase, P. T., & Kroh, L. W. (2013) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf302959k · Cited by 45

Identification of 3-deoxyglucosone dehydrogenase as aldehyde dehydrogenase 1A1 (retinaldehyde dehydrogenase 1)

Collard, F., Vertommen, D., Fortpied, J., Duester, G., & SCHAFTINGEN, E. V. (2006) · Biochimie · doi:10.1016/j.biochi.2006.11.005 · Cited by 42

Acrolein and Methacrolein

Arntz, D., Fischer, A., Höpp, M., Jacobi, S., Sauer, J., Ohara, T., Sato, T., Shimizu, N., & Schwind, H. (2007) · Ullmann's Encyclopedia of Industrial Chemistry · doi:10.1002/14356007.a01_149.pub2 · Cited by 41

Accumulation of Pyrraline-modified Albumin in Phagocytes due to Reduced Degradation by Lysosomal Enzymes

Miyata, S., Liu, B.-F., Shoda, H., Ohara, T., Yamada, H., Suzuki, K., & Kasuga, M. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.7.4037 · Cited by 37

Measurement and Clinical Significance of Biomarkers of Oxidative Stress in Humans

Marrocco, I., Fabio Altieri, F., & Peluso, I. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/6501046 · Cited by 907

N-Acetylcysteine as an antioxidant and disulphide breaking agent: the reasons why

Aldini, G., Altomare, A., Baron, G., Vistoli, G., Carini, M., Borsani, L., & Sergio, F. (2018) · Free Radical Research · doi:10.1080/10715762.2018.1468564 · Cited by 837

Advanced Glycation End-Products (AGEs): Formation, Chemistry, Classification, Receptors, and Diseases Related to AGEs

Twarda‐Clapa, A., Olczak, A., Białkowska, A. M., & Koziołkiewicz, M. (2022) · Cells · doi:10.3390/cells11081312 · Cited by 829

Oxidative Stress and Antioxidants in Neurodegenerative Disorders

Olufunmilayo, E. O., Gerke-Duncan, M. B., & Holsinger, R. M. D. (2023) · Antioxidants · doi:10.3390/antiox12020517 · Cited by 752

Targeting Oxidative Stress and Mitochondrial Dysfunction in the Treatment of Impaired Wound Healing: A Systematic Review

Sanchez, M. C. C., Lancel, S., Boulanger, É., & Nevière, R. (2018) · Antioxidants · doi:10.3390/antiox7080098 · Cited by 584

Special issue on “AGEs and ALEs: chemistry, physiopathology and molecular strategies for their inhibition”

Aldini, G., Grune, T., & Bartosz, G. (2013) · Free Radical Research · doi:10.3109/10715762.2013.819427 · Cited by 1

Molecular strategies to prevent, inhibit, and degrade advanced glycoxidation and advanced lipoxidation end products

Aldini, G., Vistoli, G., Štefek, M., Chondrogianni, N., Grune, T., Sereikaitė, J., Sadowska‐Bartosz, I., & Bartosz, G. (2013) · Free Radical Research · doi:10.3109/10715762.2013.792926 · Cited by 154

DETERMINATION OF ADVANCED GLYCATION (AGEs) AND LIPOXIDATION (ALEs) END PRODUCTS IN FOODS AND BIOLOGICAL SYSTEMS: ADVANCES, CHALLENGES AND PERSPECTIVES

Barbosa, J. H. P., Souza, I. T., Santana, A. E. G., & Goulart, M. O. F. (2016) · Química Nova · doi:10.5935/0100-4042.20160048 · Cited by 22

Advanced Glycation End Products: Association with the Pathogenesis of Diseases and the Current Therapeutic Advances

Ajith, T. A., & Vinodkumar, P. (2016) · Current Clinical Pharmacology · doi:10.2174/1574884711666160511150028 · Cited by 59

ADVANCED GLYCATION END PRODUCTS

ნ., M. N. Მ., პ., T. P. Თ., გ., M. G. Მ., მ., P. M. Პ., & ე., E. E. Ე. (2016) · TSMU COLLECTION OF SCIENTIFIC WORKS · doi:10.52340/csw.2016.50.0.81-84 · Cited by 26