Quantitative screening of protein biomarkers of early glycation, advanced glycation, oxidation and nitrosation in cellular and extracellular proteins by tandem mass spectrometry multiple reaction monitoring
Abstract
Glycation of proteins forms fructosamines and AGEs (advanced glycation end products). Oxidative and nitrosative stress leads to the formation of oxidative and nitrosative modifications. The modified amino acid residues formed in these processes are biomarkers of protein damage: some are risk markers and some may be risk factors for disease development. We developed a method for the concurrent quantitative measurement of 16 biomarkers indicative of protein glycation, oxidation and nitrosation damage using LC-MS/MS (LC with tandem MS detection). Underivatized analytes were detected free in physiological fluids and in enzymatic hydrolysates of cellular and extracellular proteins. Hydroimidazolones were the most important glycation biomarkers, and methionine sulphoxide was the most important oxidative biomarker quantitatively; 3-nitrotyrosine was the biomarker of nitrosation. Quantitative screening showed high levels of AGEs in cellular protein and moderate levels in protein of blood plasma. Levels of 3-nitrotyrosine were typically 100-fold lower than this. The major glycation adducts in blood plasma had high renal clearances in normal healthy human subjects, whereas methionine sulphoxide and 3-nitrotyrosine had low renal clearances due to further metabolism. Physiological AGEs in blood plasma were eliminated from the circulation in the kidney and not in the liver. LC-MS/MS peptide mapping was also used to locate the protein biomarkers. These studies reveal that advanced glycatio…
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Methionine is reversibly oxidized to methionine sulfoxide and irreversibly oxidized to methionine sulfone; methionine sulfone is stable and not targeted by methionine sulfoxide reductases.
“In contrast to the non-enzymatic oxidation of methionine to methionine sulfoxide, the reduction is catalyzed by methionine sulfoxide reductases [20]. Further oxidation results in methionine sulfone formation, which is not targeted by methionine sulfoxide reductases and has to be considered as a stable modification [21].”
From Protein oxidation - Formation mechanisms, detection and relevance as biomarkers in human diseases (2021) · cites this paper as [21]
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Anderson, L., & Hunter, C. L. (2006) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m500331-mcp200 · Cited by 1,230 · see citing works
Uribarri, J., Cai, W., Peppa, M., Goodman, S., Ferrucci, L., Striker, G., & Vlassara, H. (2007) · The Journals of Gerontology Series A: Biological Sciences and Medical Sciences · doi:10.1093/gerona/62.4.427 · Cited by 570 · see citing works
Tomlinson, D. R., & Gardiner, N. J. (2007) · Nature reviews. Neuroscience · doi:10.1038/nrn2294 · Cited by 566 · see citing works
The molecular basis for impaired hypoxia-induced VEGF expression in diabetic tissues
Thangarajah, H., Yao, D., Chang, E. I.-F., Shi, Y., Jazayeri, L., Vial, I. N., Galiano, R. D., Du, X.-L., Grogan, R. H., Galvez, M. G., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0906670106 · Cited by 469 · see citing works
Adams, J. B., Audhya, T., McDonough-Means, S., Rubin, R. A., Quig, D., Geis, E., Gehn, E., Loresto, M., Mitchell, J., Atwood, S., et al. (2011) · Nutrition & Metabolism · doi:10.1186/1743-7075-8-34 · Cited by 442 · see citing works
Wautier, J., & Schmidt, A. M. (2004) · Circulation Research · doi:10.1161/01.res.0000137876.28454.64 · Cited by 434 · see citing works
Mass Spectrometry Based Targeted Protein Quantification: Methods and Applications
Pan, S., Aebersold, R. H., Chen, R., Rush, A. J., Goodlett, D. R., McIntosh, M. W., Zhang, J., & Brentnall, T. A. (2008) · Journal of Proteome Research · doi:10.1021/pr800538n · Cited by 393 · 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
Advanced glycation end products and the kidney
Bohlender, J. M., Franke, S., Stein, G., & Wolf, G. (2005) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00398.2004 · Cited by 386 · see citing works
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Kehm, R., Baldensperger, T., Raupbach, J., & Höhn, A. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101901 · Cited by 348 · see citing works
Multiple reaction monitoring for quantitative biomarker analysis in proteomics and metabolomics☆
Kitteringham, N. R., Jenkins, R. E., Lane, C. S., Elliott, V. L., & Park, B. K. (2008) · Journal of Chromatography B · doi:10.1016/j.jchromb.2008.11.013 · Cited by 343 · see citing works
Aging Hallmarks and Progression and Age-Related Diseases: A Landscape View of Research Advancement
Tenchov, R., Sasso, J. M., Wang, X., & Zhou, Q. A. (2024) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00531 · Cited by 276 · see citing works
Update on the pathogenesis and treatment of skeletal fragility in type 2 diabetes mellitus
Khosla, S., Samakkarnthai, P., Monroe, D. G., & Farr, J. N. (2021) · Nature Reviews Endocrinology · doi:10.1038/s41574-021-00555-5 · Cited by 260 · see citing works
Ceradini, D. J., Yao, D., Grogan, R. H., Callaghan, M. J., Edelstein, D., Brownlee, M., & Gurtner, G. C. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m707451200 · Cited by 245 · see citing works
Yao, D., Taguchi, T., Matsumura, T., Pestell, R. G., Edelstein, D., Giardino, I., Suske, G., Rabbani, N., Thornalley, P. J., Sarthy, V. P., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704703200 · Cited by 233 · see citing works
Self-citationAdvanced 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
Determinants of bone strength and quality in diabetes mellitus in humans
Farr, J. N., & Khosla, S. (2015) · Bone · doi:10.1016/j.bone.2015.07.027 · Cited by 192 · see citing works
Duran-Jimenez, B., Dobler, D., Moffatt, S., Rabbani, N., Streuli, C. H., Thornalley, P. J., Tomlinson, D. R., & Gardiner, N. J. (2009) · Diabetes · doi:10.2337/db09-0320 · Cited by 186 · see citing works
Self-citationThe AGE of the matrix: chemistry, consequence and cure
DeGroot, J. (2004) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2004.01.007 · Cited by 165 · see citing works
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
Kchaou, H., Benbettaïeb, N., Jridi, M., Abdelhedi, O., Karbowiak, T., Brachais, C., Léonard, M.-L., Debeaufort, F., & Nasri, M. (2018) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2018.05.011 · Cited by 151 · see citing works
Genuth, S., Sun, W., Cleary, P., Gao, X., Sell, D. R., Lachin, J., The DCCT/EDIC Research Group, & Monnier, V. M. (2015) · Diabetes · doi:10.2337/db14-0215 · Cited by 146 · see citing works
Candiano, G., Musante, L., Bruschi, M., Petretto, A., Santucci, L., Boccio, P. D., Pavone, B., Perfumo, F., Urbani, A., Scolari, F., et al. (2006) · Journal of the American Society of Nephrology · doi:10.1681/asn.2006050486 · Cited by 139 · see citing works
Kim, C., Park, S., & Kim, J. (2017) · Physical Activity and Nutrition · doi:10.20463/jenb.2017.0027 · Cited by 123 · see citing works
Danielson, S. R., Held, J. M., Schilling, B., Oo, M. L., Gibson, B. W., & Andersen, J. K. (2009) · Analytical Chemistry · doi:10.1021/ac901176t · Cited by 123 · see citing works
Verrastro, I., Pasha, S., Jensen, K., Pitt, A., & Spickett, C. (2015) · Biomolecules · doi:10.3390/biom5020378 · Cited by 114 · see citing works
Rubino, F. M., Pitton, M., Fabio, D. D., & Colombi, A. (2009) · Mass Spectrometry Reviews · doi:10.1002/mas.20207 · Cited by 113 · 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
Frolov, A., Hoffmann, P., & Hoffmann, R. (2006) · Journal of Mass Spectrometry · doi:10.1002/jms.1117 · Cited by 105 · see citing works
Tantalaki, E., Piperi, C., Livadas, S., Κόλλιας, Α., Adamopoulos, C., Koulouri, A., Christakou, C. D., & Diamanti‐Kandarakis, E. (2014) · HORMONES · doi:10.1007/bf03401321 · Cited by 101 · see citing works
The RAGE Axis and Endothelial Dysfunction: Maladaptive Roles in the Diabetic Vasculature and Beyond
Ramasamy, R., Yan, S. F., & Schmidt, A. M. (2005) · Trends in Cardiovascular Medicine · doi:10.1016/j.tcm.2005.08.003 · Cited by 91 · see citing works
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
Scheijen, J. L. J. M., van de Waarenburg, M. P. H., Stehouwer, C. D. A., & Schalkwijk, C. G. (2009) · Journal of Chromatography B · doi:10.1016/j.jchromb.2009.01.022 · Cited by 78 · see citing works
Lu, L., Pu, L. J., Zhang, Q., Wang, L. J., Kang, S., Zhang, R., Chen, Q., Wang, J. G., Caterina, R. D., & Shen, W. F. (2009) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2008.12.045 · Cited by 77 · see citing works
Glycation of Plant Proteins: Regulatory Roles and Interplay with Sugar Signalling?
Shumilina, J., Kusnetsova, A., Tsarev, A. A., van Rensburg, H. C. J., Medvedev, S. S., Demidchik, V. V., den Ende, W. V., & Frolov, A. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20092366 · Cited by 75 · see citing works
Mass spectrometry and 3‐nitrotyrosine: Strategies, controversies, and our current perspective
Tsikas, D., & Duncan, M. W. (2014) · Mass Spectrometry Reviews · doi:10.1002/mas.21396 · Cited by 76 · see citing works
Boulanger, É., Wautier, M.-P., Gane, P., Mariette, C., Devuyst, O., & Wautier, J. (2004) · Nephrology Dialysis Transplantation · doi:10.1093/ndt/gfh277 · Cited by 76 · see citing works
RETRACTED: Methylglyoxal Modification of mSin3A Links Glycolysis to Angiopoietin-2 Transcription
Yao, D., Taguchi, T., Matsumura, T., Pestell, R. G., Edelstein, D., Giardino, I., Suske, G., Ahmed, N., Thornalley, P. J., Sarthy, V. P., et al. (2006) · Cell · doi:10.1016/j.cell.2005.11.024 · Cited by 73 · see citing works
Self-citationRetractedMethylglyoxal Induces Tau Hyperphosphorylation via Promoting AGEs Formation
Li, X., Xie, J., Jiang, X., Lv, B.-L., Cheng, X., Du, L., Zhang, J. Y., Wang, J., & Zhou, X. (2012) · NeuroMolecular Medicine · doi:10.1007/s12017-012-8191-0 · Cited by 72 · see citing works
Pathological Significance of Mitochondrial Glycation
Pun, P. B. L., & Murphy, M. P. (2012) · International Journal of Cell Biology · doi:10.1155/2012/843505 · Cited by 72 · see citing works
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 · see citing works
Jenkins, R. E., Kitteringham, N. R., Hunter, C. L., Webb, S., Hunt, T., Elsby, R., Watson, R. B., Williams, D. P., Pennington, S. R., & Park, B. K. (2006) · PROTEOMICS · doi:10.1002/pmic.200500432 · Cited by 70 · see citing works
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
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
Bansal, S., Burman, A., & Tripathi, A. K. (2023) · World Journal of Diabetes · doi:10.4239/wjd.v14.i8.1146 · Cited by 66 · see citing works
What is the Future of Diabetic Wound Care?
Sweitzer, S. M., Fann, S. A., Borg, T. K., Baynes, J., & Yost, M. J. (2006) · The Science of Diabetes Self-Management and Care · doi:10.1177/0145721706286897 · Cited by 60 · see citing works
Hambsch, B., Chen, B., Brenndörfer, J., Meyer, M., Avrabos, C., Maccarrone, G., Liu, R. H., Eder, M., Turck, C. W., & Landgraf, R. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.06693.x · Cited by 59 · see citing works
A novel advanced glycation index and its association with diabetes and microangiopathy
Rangasamy, S., Balasubramanyam, M., Rema, M., Premanand, C., & Mohan, V. (2005) · Metabolism · doi:10.1016/j.metabol.2005.02.017 · Cited by 59 · see citing works
Advances in Proteomic Technologies and Its Contribution to the Field of Cancer
Mesri, M. (2014) · Advances in Medicine · doi:10.1155/2014/238045 · Cited by 58 · see citing works
Advanced Glycation End Products Induce Obesity and Hepatosteatosis in CD-1 Wild-Type Mice
Sayej, W. N., Knight, P. R., Guo, W. A., Mullan, B., Ohtake, P. J., Davidson, B. A., Khan, A. R., Baker, R. D., & Baker, S. S. (2016) · BioMed Research International · doi:10.1155/2016/7867852 · Cited by 57 · see citing works
Chemical Reactivity and Respiratory Toxicity of the α-Diketone Flavoring Agents
Morgan, D. L., Jokinen, M. P., Johnson, C. L., Price, H. C., Gwinn, W. M., Bousquet, R. W., & Flake, G. P. (2016) · Toxicologic Pathology · doi:10.1177/0192623316638962 · Cited by 56 · see citing works
Advanced-Glycation End-Products Induce Podocyte Injury and Contribute to Proteinuria
Nishad, R., Tahaseen, V., Kavvuri, R., Motrapu, M., Singh, A., Peddi, K., & Pasupulati, A. K. (2021) · Frontiers in Medicine · doi:10.3389/fmed.2021.685447 · Cited by 50 · see citing works
Price, C. L., Sharp, P. S., North, M. E., Rainbow, S. J., & Knight, S. C. (2004) · Diabetes · doi:10.2337/diabetes.53.6.1452 · Cited by 49 · 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
Takátsy, A., Böddi, K., Nagy, L., Nagy, G., Szabó, S. S., Markó, L., Wittmann, I., Ohmacht, R., Ringer, T., Bonn, G. K., et al. (2009) · Analytical Biochemistry · doi:10.1016/j.ab.2009.06.007 · Cited by 47 · see citing works
Gly-PseAAC: Identifying protein lysine glycation through sequences
Xu, Y., Li, L., Ding, J., Wu, L., Mai, G., & Zhou, F. (2016) · Gene · doi:10.1016/j.gene.2016.11.021 · Cited by 47 · see citing works
Soboleva, A., Mavropolo-Stolyarenko, G., Каронова, Т. Л., Thieme, D., Hoehenwarter, W., Ihling, C. H., Стефанов, В. Е., Grishina, T., & Frolov, A. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20092329 · Cited by 47 · see citing works
Magalhães, P. M., Appell, H.-J., & Duarte, J. A. (2008) · European Review of Aging and Physical Activity · doi:10.1007/s11556-008-0032-7 · Cited by 46 · see citing works
Targeted proteomics for validation of biomarkers in clinical samples
Ye, X., Blonder, J., & Veenstra, T. D. (2008) · Briefings in Functional Genomics and Proteomics · doi:10.1093/bfgp/eln050 · Cited by 46 · see citing works
Pageon, H., Zucchi, H., Dai, Z., Sell, D. R., Strauch, C., Monnier, V. M., & Asselineau, D. (2015) · BioResearch open access · doi:10.1089/biores.2014.0053 · Cited by 45 · see citing works
Yang, S., Kim, S.-W., Kim, Y., Lee, S.-H., Jeon, H., & Lee, K. (2014) · Food Chemistry · doi:10.1016/j.foodchem.2014.12.090 · Cited by 41 · see citing works
Greifenhagen, U., Nguyen, V. D., Moschner, J., Giannis, A., Frolov, A., & Hoffmann, R. (2014) · Journal of Proteome Research · doi:10.1021/pr500799m · Cited by 41 · see citing works
Proteomic approaches in biological and medical sciences: principles and applications.
Conrotto, P., & Souchelnytskyi, S. (2008) · PubMed · Cited by 41 · see citing works
Fan, X., Liu, X., Hao, S., Wang, B., Robinson, M. L., & Monnier, V. M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0050832 · Cited by 40 · see citing works
Non‐enzymatic glycation of chondrocyte‐seeded collagen gels for cartilage tissue engineering
Roy, R., Boskey, A. L., & Bonassar, L. J. (2008) · Journal of Orthopaedic Research® · doi:10.1002/jor.20662 · Cited by 39 · see citing works
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
Markiewicz, E., Jerome, J., Mammone, T., & Idowu, O. C. (2022) · Clinical Cosmetic and Investigational Dermatology · doi:10.2147/ccid.s364538 · Cited by 38 · see citing works
A review on food processing and preparation methods for altering fish allergenicity
Dasanayaka, B. P., Li, Z., Pramod, S. N., Chen, Y., Khan, M. U., & Lin, H. (2020) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2020.1848791 · Cited by 38 · see citing works
Hashimoto, C., Iwaihara, Y., Chen, S. J., Tanaka, M., Watanabe, T., & Matsui, T. (2013) · Analytical Chemistry · doi:10.1021/ac400294q · Cited by 37 · see citing works
Walsh, G. M., Lin, S., Evans, D. M., Khosrovi-Eghbal, A., Beavis, R. C., & Kast, J. (2008) · Journal of Proteomics · doi:10.1016/j.jprot.2008.11.015 · Cited by 37 · see citing works
Mouls, L., Silajdžić, E., Haroune, N., Spickett, C. M., & Pitt, A. R. (2009) · PROTEOMICS · doi:10.1002/pmic.200800391 · Cited by 35 · see citing works
Advanced-glycation end products in insulin-resistant states
Soldatos, G., Cooper, M. E., & Jandeleit-Dahm, K. A. M. (2005) · Current Hypertension Reports · doi:10.1007/s11906-005-0081-5 · Cited by 35 · see citing works
Analytical strategies to depict the fate of the Maillard reaction in foods
Troise, A. D. (2017) · Current Opinion in Food Science · doi:10.1016/j.cofs.2017.12.005 · Cited by 34 · see citing works
Handbook of Medical Sociology, Sixth Edition
Conrad, P., Bird, C., Fremont, A., & Timmermans, S. (2010) · Vanderbilt University Press eBooks · doi:10.2307/j.ctv16h2n9s · Cited by 35 · see citing works
Kaňková, K. (2008) · Proceedings of The Nutrition Society · doi:10.1017/s0029665108006034 · Cited by 30 · see citing works
Aldossari, S. M., Rehman, L. U., Ahmad, I., Aslam, M., Fozia, F., Mohany, M., Milošević, M. D., Al-Rejaie, S. S., & Aboul‐Soud, M. A. M. (2023) · ACS Omega · doi:10.1021/acsomega.3c04484 · Cited by 28 · see citing works
Adepoyibi, T., Weigl, B. H., Greb, H., Neogi, T., & McGuire, H. (2013) · Public Health Action · doi:10.5588/pha.13.0036 · Cited by 26 · see citing works
Challenges in Developing DNA and RNA Biomarkers of Inflammation
Dedon, P. C., DeMott, M. S., Elmquist, C. E., Prestwich, E. G., McFaline‐Figueroa, J. L., & Pang, B. (2007) · Biomarkers in Medicine · doi:10.2217/17520363.1.2.293 · Cited by 25 · see citing works
Chen, S. J., Aikawa, C., Yoshida, R., & Matsui, T. (2015) · Physiological Reports · doi:10.14814/phy2.12477 · Cited by 23 · see citing works
Sveen, K. A., Dahl‐Jørgensen, K., Stensæth, K. H., Angel, K., Seljeflot, I., Sell, D. R., Monnier, V. M., & Hanssen, K. F. (2014) · Journal of Diabetes and its Complications · doi:10.1016/j.jdiacomp.2014.12.011 · Cited by 23 · see citing works
Saraiva, M. A., Borges, C., & Florêncio, M. H. (2006) · Journal of Mass Spectrometry · doi:10.1002/jms.1031 · Cited by 23 · see citing works
Ahmed, K. A., Muniandy, S., & Ismail, I. S. (2009) · Journal of Clinical Biochemistry and Nutrition · doi:10.3164/jcbn.08-190 · Cited by 22 · see citing works
Koomen, J. M., & Smalley, K. S. M. (2011) · Oncotarget · doi:10.18632/oncotarget.263 · Cited by 21 · see citing works
Altered glyoxalase 1 expression in psychiatric disorders: Cause or consequence?
Hambsch, B. (2011) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2011.02.005 · Cited by 21 · see citing works
Surveying the damage: the challenges of developing nucleic acidbiomarkers of inflammation
Son, J., Pang, B., McFaline‐Figueroa, J. L., Taghizadeh, K., & Dedon, P. C. (2008) · Molecular BioSystems · doi:10.1039/b719411k · Cited by 21 · see citing works
Methods of the site-selective solid phase synthesis of peptide-derived Amadori products
Stefanowicz, P., Kijewska, M., Kapczyńska, K., & Szewczuk, Z. (2009) · Amino Acids · doi:10.1007/s00726-009-0294-z · Cited by 21 · see citing works
Yu, H., Wong, M., Zhao, S. S., Love, J. A., Ansley, D. M., & Chen, D. D. Y. (2012) · Electrophoresis · doi:10.1002/elps.201100368 · Cited by 20 · see citing works
The Clinical Chemome: A Tool for the Diagnosis and Management of Chronic Disease
Baynes, J. (2004) · Clinical Chemistry · doi:10.1373/clinchem.2004.034645 · Cited by 20 · see citing works
Lee, S. H., Miyamoto, K., Goto, T., & Oe, T. (2011) · Journal of Proteomics · doi:10.1016/j.jprot.2011.08.010 · Cited by 19 · see citing works
Lissner, L. J., Rodrigues, L., Wartchow, K. M., Borba, E., Bobermin, L. D., Fontella, F. U., Hansen, F., Quincozes‐Santos, A., Souza, D. O., & Gonçalves, C. (2020) · Neurochemical Research · doi:10.1007/s11064-020-03154-4 · Cited by 19 · see citing works
Can grape polyphenols affect glycation markers? A systematic review
Coelho, O. G. L., Ribeiro, P. V. D. M., & Alfenas, R. D. C. G. (2021) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2021.1962796 · Cited by 18 · see citing works
Assessing the Components of the eIF3 Complex and their Phosphorylation Status
Farley, A. R., Powell, D. W., Weaver, C. M., Jennings, J. L., & Link, A. J. (2011) · Journal of Proteome Research · doi:10.1021/pr100877m · Cited by 18 · see citing works
Antiglycation Activity of Aucubin In Vitro and in Exogenous Methylglyoxal Injected Rats
Jung, E., Park, S., Jung, W. K., Kim, H. R., & Kim, J. (2019) · Molecules · doi:10.3390/molecules24203653 · Cited by 18 · see citing works
Čolak, E., & Majkić‐Singh, N. (2009) · Journal of Medical Biochemistry · doi:10.2478/v10011-009-0006-y · Cited by 16 · see citing works
Acute Methylglyoxal-Induced Damage in Blood–Brain Barrier and Hippocampal Tissue
Lissner, L. J., Wartchow, K. M., Rodrigues, L., Bobermin, L. D., Borba, E., Gayger-Dias, V., Hansen, F., Quincozes‐Santos, A., & Gonçalves, C. (2022) · Neurotoxicity Research · doi:10.1007/s12640-022-00571-x · Cited by 16 · see citing works
[Glycation and protein crosslinking in the diabetes and ageing pathogenesis].
Cárdenas‐León, M., Díaz‐Díaz, E., Argüelles-Medina, R., Sánchez-Canales, P., Díaz‐Sánchez, V., & Larrea, F. (2009) · PubMed · Cited by 16 · see citing works
CD proteome and beyond - technologies for targeting the immune cell surfaceome
Bock, T. (2011) · Frontiers in bioscience · doi:10.2741/4006 · Cited by 16 · see citing works
Glycation of Ribonuclease A affects its enzymatic activity and DNA binding ability
Dinda, A. K., Tripathy, D. R., & Dasgupta, S. (2015) · Biochimie · doi:10.1016/j.biochi.2015.09.014 · Cited by 15 · see citing works
Golegaonkar, S. B., Bhonsle, H. S., Boppana, R., & Kulkarni, M. J. (2010) · European Journal of Mass Spectrometry · doi:10.1255/ejms.1066 · Cited by 15 · see citing works
Identification and comparative quantitation of glycation by stable isotope labeling and LC–MS
Liu, H., Ponniah, G., Neill, A., Patel, R., & Andrien, B. A. (2014) · Journal of Chromatography B · doi:10.1016/j.jchromb.2014.03.021 · Cited by 14 · see citing works
- Authors
- Ahmed, N., & Thornalley, P. J.
- Affiliations
- University of Essex (GB)
- ORCID
- Thornalley, P.J.
- Venue
- Biochemical Society Transactions
- Publisher
- Portland Press Ltd.
- Published
- 2003-12-01
- Volume
- 31
- Issue
- 6
- Pages
- 1417-1422
- ISSN
- 0300-5127 (ISSN-L)
- 1470-8752
- OpenAlex
- W2136468934
- Cited by
- 152
- References
- 0
- Citations by year
- 2026: 4 · 2025: 4 · 2024: 2 · 2023: 4 · 2022: 3 · 2021: 8 · 2020: 3 · 2019: 7 · 2018: 2 · 2017: 6 · 2016: 7 · 2015: 7 · 2014: 7 · 2013: 6 · 2012: 7
- FWCI
- 4.17
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemical Society Transactions (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Keywords
- protein glycation, advanced glycation end products, oxidative stress, nitrosative stress, protein oxidation, nitrosation, protein biomarkers, hydroimidazolone, methionine sulfoxide, nitrotyrosine, fructosamine, blood plasma, renal clearance, peptide mapping, multiple reaction monitoring, proteasomal degradation, antioxidants
- MeSH terms
- Glucose, Nitroso Compounds, Oxidation-Reduction, Proteins, Mass Spectrometry, Biomarkers, Glycation End Products, Advanced
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