{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,17]],"date-time":"2026-01-17T23:46:41Z","timestamp":1768693601397,"version":"3.49.0"},"reference-count":64,"publisher":"Springer Science and Business Media LLC","issue":"4","license":[{"start":{"date-parts":[[2019,9,18]],"date-time":"2019-09-18T00:00:00Z","timestamp":1568764800000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"},{"start":{"date-parts":[[2019,9,18]],"date-time":"2019-09-18T00:00:00Z","timestamp":1568764800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"funder":[{"DOI":"10.13039\/http:\/\/dx.doi.org\/10.13039\/501100003968","name":"Iran National Science Foundation","doi-asserted-by":"publisher","award":["96008461"],"award-info":[{"award-number":["96008461"]}],"id":[{"id":"10.13039\/http:\/\/dx.doi.org\/10.13039\/501100003968","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Cell Biochem Biophys"],"published-print":{"date-parts":[[2019,12]]},"DOI":"10.1007\/s12013-019-00884-3","type":"journal-article","created":{"date-parts":[[2019,9,18]],"date-time":"2019-09-18T06:02:50Z","timestamp":1568786570000},"page":"343-355","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":6,"title":["Carnosine Prevents Different Structural Damages Induced by Methylglyoxal in Lens Crystallins"],"prefix":"10.1007","volume":"77","author":[{"given":"Maryam","family":"Kianpour","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Reza","family":"Yousefi","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2019,9,18]]},"reference":[{"issue":"3","key":"884_CR1","doi-asserted-by":"publisher","first-page":"407","DOI":"10.1016\/j.pbiomolbio.2003.11.012","volume":"86","author":"H Bloemendal","year":"2004","unstructured":"Bloemendal, H., de Jong, W., Jaenicke, R., Lubsen, N. H., Slingsby, C., & Tardieu, A. (2004). Ageing and vision: structure, stability and function of lens crystallins. Progress in Biophysics and Molecular Biology, 86(3), 407\u2013485.","journal-title":"Progress in Biophysics and Molecular Biology"},{"issue":"5074","key":"884_CR2","doi-asserted-by":"publisher","first-page":"1220","DOI":"10.1126\/science.1355616","volume":"257","author":"ER Stadtman","year":"1992","unstructured":"Stadtman, E. R. (1992). Protein oxidation and aging. Science, 257(5074), 1220\u20131224.","journal-title":"Science"},{"issue":"6865","key":"884_CR3","doi-asserted-by":"publisher","first-page":"813","DOI":"10.1038\/414813a","volume":"414","author":"M Brownlee","year":"2001","unstructured":"Brownlee, M. (2001). Biochemistry and molecular cell biology of diabetic complications. Nature, 414(6865), 813.","journal-title":"Nature"},{"issue":"8","key":"884_CR4","doi-asserted-by":"publisher","first-page":"1010","DOI":"10.2337\/diab.40.8.1010","volume":"40","author":"TJ Lyons","year":"1991","unstructured":"Lyons, T. J., Silvestri, G., Dunn, J. A., Dyer, D. G., & Baynes, J. W. (1991). Role of glycation in modification of lens crystallins in diabetic and nondiabetic senile cataracts. Diabetes, 40(8), 1010\u20131015.","journal-title":"Diabetes"},{"issue":"1483","key":"884_CR5","doi-asserted-by":"publisher","first-page":"1195","DOI":"10.1098\/rstb.2007.2044","volume":"362","author":"G Yim","year":"2007","unstructured":"Yim, G., & Wang, H. H. (2007). Antibiotics as signalling molecules. Philosophical Transactions of the Royal Society B: Biological Sciences, 362(1483), 1195\u20131200.","journal-title":"Philosophical Transactions of the Royal Society B: Biological Sciences"},{"key":"884_CR6","doi-asserted-by":"publisher","first-page":"3164734","DOI":"10.1155\/2016\/3164734","volume":"2016","author":"M Nita","year":"2016","unstructured":"Nita, M., & Grzybowski, A. (2016). The role of the reactive oxygen species and oxidative stress in the pathomechanism of the age-related ocular diseases and other pathologies of the anterior and posterior eye segments in adults. Oxidative Medicine and Cellular Longevity, 2016, 3164734.","journal-title":"Oxidative Medicine and Cellular Longevity"},{"issue":"8","key":"884_CR7","doi-asserted-by":"publisher","first-page":"1099","DOI":"10.1001\/archopht.1988.01060140255036","volume":"106","author":"P Kador","year":"1988","unstructured":"Kador, P., Akagi, Y., Terubayashi, H., Wyman, M., & Kinoshita, J. (1988). Prevention of pericyte ghost formation in retinal capillaries of galactose-fed dogs by aldose reductase inhibitors. Archives of Ophthalmology, 106(8), 1099\u20131102.","journal-title":"Archives of Ophthalmology"},{"issue":"2","key":"884_CR8","doi-asserted-by":"publisher","first-page":"632","DOI":"10.1016\/0304-4165(74)90326-2","volume":"338","author":"S Varma","year":"1974","unstructured":"Varma, S., & Kinoshita, J. (1974). Sorbitol pathway in diabetic and galactosemic rat lens. Biochimica et Biophysica Acta (BBA)-General Subjects, 338(2), 632\u2013640.","journal-title":"Biochimica et Biophysica Acta (BBA)-General Subjects"},{"issue":"10","key":"884_CR9","first-page":"713","volume":"13","author":"JH Kinoshita","year":"1974","unstructured":"Kinoshita, J. H. (1974). Mechanisms initiating cataract formation proctor lecture. Investigative Ophthalmology & Visual Science, 13(10), 713\u2013724.","journal-title":"Investigative Ophthalmology & Visual Science"},{"issue":"2","key":"884_CR10","doi-asserted-by":"publisher","first-page":"258","DOI":"10.1016\/j.cell.2006.01.002","volume":"124","author":"R Ramasamy","year":"2006","unstructured":"Ramasamy, R., Yan, S. F., & Schmidt, A. M. (2006). Methylglyoxal comes of AGE. Cell, 124(2), 258\u2013260.","journal-title":"Cell"},{"key":"884_CR11","unstructured":"Seidler, N. W. (2012). GAPDH: biological properties and diversity. Springer, Dordrecht, 985, 1\u201336."},{"issue":"12","key":"884_CR12","doi-asserted-by":"publisher","first-page":"5287","DOI":"10.1167\/iovs.03-0573","volume":"44","author":"N Ahmed","year":"2003","unstructured":"Ahmed, N., Thornalley, P. J., Dawczynski, J., Franke, S., Strobel, J., Stein, Gn, & Haik, G. M. (2003). Methylglyoxal-derived hydroimidazolone advanced glycation end-products of human lens proteins. Investigative Ophthalmology & Visual Science, 44(12), 5287\u20135292.","journal-title":"Investigative Ophthalmology & Visual Science"},{"issue":"5","key":"884_CR13","doi-asserted-by":"publisher","first-page":"355","DOI":"10.1016\/j.trsl.2011.12.004","volume":"159","author":"M Jack","year":"2012","unstructured":"Jack, M., & Wright, D. (2012). Role of advanced glycation endproducts and glyoxalase I in diabetic peripheral sensory neuropathy. Translational Research, 159(5), 355\u2013365.","journal-title":"Translational Research"},{"issue":"6","key":"884_CR14","doi-asserted-by":"publisher","first-page":"782","DOI":"10.1002\/mds.26566","volume":"31","author":"H Vicente Miranda","year":"2016","unstructured":"Vicente Miranda, H., El\u2010Agnaf, O., & Outeiro, T. F. (2016). Glycation in Parkinson\u2019s disease and Alzheimer\u2019s disease. Movement Disorders, 31(6), 782\u2013790.","journal-title":"Movement Disorders"},{"issue":"1-2","key":"884_CR15","doi-asserted-by":"publisher","first-page":"125","DOI":"10.1515\/DMDI.2008.23.1-2.125","volume":"23","author":"PJ Thornalley","year":"2008","unstructured":"Thornalley, P. J. (2008). Protein and nucleotide damage by glyoxal and methylglyoxal in physiological systems-role in ageing and disease. Drug Metabolism and Drug Interactions, 23(1-2), 125\u2013150.","journal-title":"Drug Metabolism and Drug Interactions"},{"key":"884_CR16","doi-asserted-by":"publisher","first-page":"3","DOI":"10.3109\/10715762.2013.815348","volume":"47","author":"G Vistoli","year":"2013","unstructured":"Vistoli, G., De Maddis, D., Cipak, A., Zarkovic, N., Carini, M., & Aldini, G. (2013). Advanced glycoxidation and lipoxidation end products (AGEs and ALEs): an overview of their mechanisms of formation. Free Radical Research, 47, 3\u201327.","journal-title":"Free Radical Research"},{"issue":"8","key":"884_CR17","doi-asserted-by":"publisher","first-page":"1101","DOI":"10.1016\/0020-711X(93)90587-5","volume":"25","author":"A Boldyrev","year":"1993","unstructured":"Boldyrev, A. (1993). Does carnosine possess direct antioxidant activity? The International Journal of Biochemistry, 25(8), 1101\u20131107.","journal-title":"The International Journal of Biochemistry"},{"issue":"10","key":"884_CR18","doi-asserted-by":"publisher","first-page":"1564","DOI":"10.1016\/S0891-5849(00)00270-7","volume":"28","author":"C Brownson","year":"2000","unstructured":"Brownson, C., & Hipkiss, A. R. (2000). Carnosine reacts with a glycated protein. Free Radical Biology and Medicine, 28(10), 1564\u20131570.","journal-title":"Free Radical Biology and Medicine"},{"issue":"11","key":"884_CR19","doi-asserted-by":"publisher","first-page":"1379","DOI":"10.1016\/j.lfs.2004.05.002","volume":"75","author":"LJ Hobart","year":"2004","unstructured":"Hobart, L. J., Seibel, I., Yeargans, G. S., & Seidler, N. W. (2004). Anti-crosslinking properties of carnosine: significance of histidine. Life Sciences, 75(11), 1379\u20131389.","journal-title":"Life Sciences"},{"key":"884_CR20","first-page":"1","volume":"13","author":"A Boldyrev","year":"1994","unstructured":"Boldyrev, A., Formazyuk, V., & Sergienko, V. D. (1994). Biological significance of histidine-containing dipeptides with special reference to carnosine: chemistry, distribution, metabolism and medical applications. Physicochem Biol, 13, 1\u201360.","journal-title":"Physicochem Biol"},{"issue":"5","key":"884_CR21","doi-asserted-by":"publisher","first-page":"379","DOI":"10.1016\/0098-2997(92)90006-L","volume":"13","author":"PJ Quinn","year":"1992","unstructured":"Quinn, P. J., Boldyrev, A. A., & Formazuyk, V. E. (1992). Carnosine: its properties, functions and potential therapeutic applications. Molecular Aspects of Medicine, 13(5), 379\u2013444.","journal-title":"Molecular Aspects of Medicine"},{"issue":"1","key":"884_CR22","doi-asserted-by":"publisher","first-page":"81","DOI":"10.1016\/0014-5793(95)00849-5","volume":"371","author":"AR Hipkiss","year":"1995","unstructured":"Hipkiss, A. R., Michaelis, J., & Syrris, P. (1995). Non-enzymatic glycosylation of the dipeptide L-carnosine, a potential anti-protein-cross-linking agent. FEBS Letters, 371(1), 81\u201385.","journal-title":"FEBS Letters"},{"issue":"4","key":"884_CR23","doi-asserted-by":"publisher","first-page":"450","DOI":"10.2174\/092986612799789396","volume":"19","author":"H Khalili-Hezarjaribi","year":"2012","unstructured":"Khalili-Hezarjaribi, H., Yousefi, R., & Moosavi-Movahedi, A. A. (2012). Effect of temperature and ionic strength on structure and chaperone activity of glycated and non-glycated alpha-crystallins. Protein and Peptide Letters, 19(4), 450\u2013457.","journal-title":"Protein and Peptide Letters"},{"issue":"2","key":"884_CR24","doi-asserted-by":"publisher","first-page":"251","DOI":"10.1042\/BJ20070989","volume":"408","author":"PA Kumar","year":"2007","unstructured":"Kumar, P. A., Kumar, M. S., & Reddy, G. B. (2007). Effect of glycation on \u03b1-crystallin structure and chaperone-like function. Biochemical Journal, 408(2), 251\u2013258.","journal-title":"Biochemical Journal"},{"issue":"8","key":"884_CR25","doi-asserted-by":"publisher","first-page":"1518","DOI":"10.1002\/1522-2683(200105)22:8<1518::AID-ELPS1518>3.0.CO;2-U","volume":"22","author":"SE Fayle","year":"2001","unstructured":"Fayle, S. E., Healy, J. P., Brown, P. A., Reid, E. A., Gerrard, J. A., & Ames, J. M. (2001). Novel approaches to the analysis of the Maillard reaction of proteins. Electrophoresis, 22(8), 1518\u20131525.","journal-title":"Electrophoresis"},{"issue":"8","key":"884_CR26","doi-asserted-by":"publisher","first-page":"717","DOI":"10.1007\/s10930-012-9451-4","volume":"31","author":"S Khazaei","year":"2012","unstructured":"Khazaei, S., Yousefi, R., & Alavian-Mehr, M. M. (2012). Aggregation and fibrillation of eye lens crystallins by homocysteinylation; implication in the eye pathological disorders. The Protein Journal, 31(8), 717\u2013727.","journal-title":"The Protein Journal"},{"issue":"2","key":"884_CR27","doi-asserted-by":"publisher","first-page":"368","DOI":"10.1016\/0003-2697(87)90587-2","volume":"166","author":"H Sch\u00e4gger","year":"1987","unstructured":"Sch\u00e4gger, H., & Von Jagow, G. (1987). Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Analytical Biochemistry, 166(2), 368\u2013379.","journal-title":"Analytical Biochemistry"},{"issue":"7","key":"884_CR28","doi-asserted-by":"publisher","first-page":"553","DOI":"10.1016\/j.jnutbio.2008.05.015","volume":"20","author":"PA Kumar","year":"2009","unstructured":"Kumar, P. A., Reddy, P. Y., Srinivas, P., & Reddy, G. B. (2009). Delay of diabetic cataract in rats by the antiglycating potential of cumin through modulation of \u03b1-crystallin chaperone activity. The Journal of Nutritional Biochemistry, 20(7), 553\u2013562.","journal-title":"The Journal of Nutritional Biochemistry"},{"issue":"8","key":"884_CR29","doi-asserted-by":"publisher","first-page":"785","DOI":"10.1134\/S0006297914080069","volume":"79","author":"A Qadeer","year":"2014","unstructured":"Qadeer, A., Zaman, M., & Khan, R. (2014). Inhibitory effect of post-micellar SDS concentration on thermal aggregation and activity of papain. Biochemistry (Moscow), 79(8), 785\u2013796.","journal-title":"Biochemistry (Moscow)"},{"issue":"15","key":"884_CR30","doi-asserted-by":"publisher","first-page":"3852","DOI":"10.1021\/bi00336a006","volume":"24","author":"G Musci","year":"1985","unstructured":"Musci, G., & Berliner, L. J. (1985). Probing different conformational states of bovine \u03b1-Lactalbumin: fluorescence studies with 4,4\u2019-Bis[1-(phenylamino)-8-naphthalenesulfonate]. Biochemistry, 24(15), 3852\u20133856.","journal-title":"Biochemistry"},{"issue":"11","key":"884_CR31","doi-asserted-by":"publisher","first-page":"4945","DOI":"10.1167\/iovs.08-1813","volume":"49","author":"X Fan","year":"2008","unstructured":"Fan, X., & Monnier, V. M. (2008). Nucleophilic compounds decrease advanced glycation end products (AGEs) from ascorbic acid in the hSVCT2 transgenic mouse model of lenticular aging. Investigative Ophthalmology & Visual Science, 49(11), 4945.","journal-title":"Investigative Ophthalmology & Visual Science"},{"issue":"5","key":"884_CR32","doi-asserted-by":"publisher","first-page":"549","DOI":"10.1562\/0031-8655(2002)076<0549:TRASSF>2.0.CO;2","volume":"76","author":"L Kessel","year":"2002","unstructured":"Kessel, L., Kalinin, S., Nagaraj, R. H., Larsen, M., & Johansson, L. B. A. (2002). Time\u2010resolved and steady\u2010state fluorescence spectroscopic studies of the human lens with comparison to Argpyrimidine, Pentosidine and 3\u2010OH\u2010kynurenine. Photochemistry and Photobiology, 76(5), 549\u2013554.","journal-title":"Photochemistry and Photobiology"},{"issue":"2","key":"884_CR33","doi-asserted-by":"publisher","first-page":"119","DOI":"10.1016\/j.bbapap.2005.06.005","volume":"1751","author":"SM Kelly","year":"2005","unstructured":"Kelly, S. M., Jess, T. J., & Price, N. C. (2005). How to study proteins by circular dichroism. Biochimica et Biophysica Acta (BBA)-Proteins and Proteomics, 1751(2), 119\u2013139.","journal-title":"Biochimica et Biophysica Acta (BBA)-Proteins and Proteomics"},{"issue":"10","key":"884_CR34","doi-asserted-by":"publisher","first-page":"1960","DOI":"10.1110\/ps.9.10.1960","volume":"9","author":"M Bouchard","year":"2000","unstructured":"Bouchard, M., Zurdo, J., Nettleton, E. J., Dobson, C. M., & Robinson, C. V. (2000). Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy. Protein Science, 9(10), 1960\u20131967.","journal-title":"Protein Science"},{"issue":"8","key":"884_CR35","doi-asserted-by":"publisher","first-page":"3331","DOI":"10.1016\/j.bpj.2008.12.3957","volume":"96","author":"T Zako","year":"2009","unstructured":"Zako, T., Sakono, M., Hashimoto, N., Ihara, M., & Maeda, M. (2009). Bovine insulin filaments induced by reducing disulfide bonds show a different morphology, secondary structure, and cell toxicity from intact insulin amyloid fibrils. Biophysical Journal, 96(8), 3331\u20133340.","journal-title":"Biophysical Journal"},{"issue":"12","key":"884_CR36","doi-asserted-by":"publisher","first-page":"1687","DOI":"10.1001\/archophthalmol.2008.507","volume":"126","author":"MB Datiles","year":"2008","unstructured":"Datiles, M. B., Ansari, R. R., Suh, K. I., Vitale, S., Reed, G. F., Zigler, J. S., & Ferris, F. L. (2008). Clinical detection of precataractous lens protein changes using dynamic light scattering. Archives of Ophthalmology, 126(12), 1687\u20131693.","journal-title":"Archives of Ophthalmology"},{"key":"884_CR37","doi-asserted-by":"publisher","first-page":"7","DOI":"10.1016\/j.ab.2014.11.016","volume":"472","author":"C Zhou","year":"2015","unstructured":"Zhou, C., Qi, W., Lewis, E. N., & Carpenter, J. F. (2015). Concomitant raman spectroscopy and dynamic light scattering for characterization of therapeutic proteins at high concentrations. Analytical Biochemistry, 472, 7\u201320.","journal-title":"Analytical Biochemistry"},{"key":"884_CR38","doi-asserted-by":"publisher","first-page":"170","DOI":"10.1016\/j.colsurfb.2014.11.002","volume":"125","author":"M Ghahramani","year":"2015","unstructured":"Ghahramani, M., Yousefi, R., Khoshaman, K., & Alavianmehr, M. M. (2015). The impact of calcium ion on structure and aggregation propensity of peroxynitrite-modified lens crystallins: new insights into the pathogenesis of cataract disorders. Colloids and Surfaces B: Biointerfaces, 125, 170\u2013180.","journal-title":"Colloids and Surfaces B: Biointerfaces"},{"key":"884_CR39","doi-asserted-by":"publisher","first-page":"208","DOI":"10.1016\/j.ijbiomac.2016.02.040","volume":"87","author":"M Ghahramani","year":"2016","unstructured":"Ghahramani, M., Yousefi, R., Khoshaman, K., Moghadam, S. S., & Kurganov, B. I. (2016). Evaluation of structure, chaperone-like activity and protective ability of peroxynitrite modified human \u03b1-crystallin subunits against copper-mediated ascorbic acid oxidation. International Journal of Biological Macromolecules, 87, 208\u2013221.","journal-title":"International Journal of Biological Macromolecules"},{"issue":"46","key":"884_CR40","doi-asserted-by":"publisher","first-page":"7269","DOI":"10.1021\/bi501004y","volume":"53","author":"MA DiMauro","year":"2014","unstructured":"DiMauro, M. A., Nandi, S. K., Raghavan, C. T., Kar, R. K., Wang, B., Bhunia, A., Nagaraj, R. H., & Biswas, A. (2014). Acetylation of Gly1 and Lys2 promotes aggregation of human \u03b3D-crystallin. Biochemistry, 53(46), 7269\u20137282.","journal-title":"Biochemistry"},{"issue":"2","key":"884_CR41","doi-asserted-by":"publisher","first-page":"120","DOI":"10.1016\/j.bbadis.2011.11.011","volume":"1822","author":"RH Nagaraj","year":"2012","unstructured":"Nagaraj, R. H., Nahomi, R. B., Shanthakumar, S., Linetsky, M., Padmanabha, S., Pasupuleti, N., Wang, B., Santhoshkumar, P., Panda, A. K., & Biswas, A. (2012). Acetylation of \u03b1A-crystallin in the human lens: Effects on structure and chaperone function. Biochimica et Biophysica Acta (BBA)-Molecular Basis of Disease, 1822(2), 120\u2013129.","journal-title":"Biochimica et Biophysica Acta (BBA)-Molecular Basis of Disease"},{"issue":"34","key":"884_CR42","doi-asserted-by":"publisher","first-page":"19888","DOI":"10.1074\/jbc.270.34.19888","volume":"270","author":"B Raman","year":"1995","unstructured":"Raman, B., Ramakrishna, T., & Rao, C.M. (1995). Rapid refolding studies on the chaperone-like \u03b1-crystallin effect of \u03b1-crystallin on refolding of \u03b2-and \u03b3-crystallins. Journal of Biological Chemistry, 270(34), 19888\u201319892.","journal-title":"Journal of Biological Chemistry"},{"key":"884_CR43","doi-asserted-by":"publisher","first-page":"819","DOI":"10.1016\/j.freeradbiomed.2015.09.013","volume":"89","author":"K Khoshaman","year":"2015","unstructured":"Khoshaman, K., Yousefi, R., Tamaddon, A. M., Saso, L., & Moosavi-Movahedi, A. A. (2015). The impact of hydrogen peroxide on structure, stability and functional properties of human R12C mutant \u03b1A-crystallin: the imperative insights into pathomechanism of the associated congenital cataract incidence. Free Radical Biology and Medicine, 89, 819\u2013830.","journal-title":"Free Radical Biology and Medicine"},{"issue":"1","key":"884_CR44","doi-asserted-by":"publisher","first-page":"22","DOI":"10.1016\/j.bbadis.2007.10.003","volume":"1782","author":"M Linetsky","year":"2008","unstructured":"Linetsky, M., Shipova, E., Cheng, R., & Ortwerth, B. J. (2008). Glycation by ascorbic acid oxidation products leads to the aggregation of lens proteins. Biochimica et Biophysica Acta (BBA)-Molecular Basis of Disease, 1782(1), 22\u201334.","journal-title":"Biochimica et Biophysica Acta (BBA)-Molecular Basis of Disease"},{"issue":"2","key":"884_CR45","doi-asserted-by":"publisher","first-page":"269","DOI":"10.1016\/S0014-4835(87)80011-8","volume":"44","author":"RE Perry","year":"1987","unstructured":"Perry, R. E., Swamy, M., & Abraham, E. (1987). Progressive changes in lens crystallin glycation and high-molecular-weight aggregate formation leading to cataract development in streptozotocin-diabetic rats. Experimental Eye Research, 44(2), 269\u2013282.","journal-title":"Experimental Eye Research"},{"key":"884_CR46","doi-asserted-by":"crossref","unstructured":"Schmid, F. X. (2001). Biological macromolecules: UV\u2010visible spectrophotometry. Encyclopedia of Life Sciences; Macmillan Publisher Ltd, New York, 1\u20134.","DOI":"10.1038\/npg.els.0003142"},{"issue":"7","key":"884_CR47","doi-asserted-by":"publisher","first-page":"1217","DOI":"10.1016\/S0891-5849(96)00557-6","volume":"22","author":"PJ Coussons","year":"1997","unstructured":"Coussons, P. J., Jacoby, J., McKay, A., Kelly, S. M., Price, N. C., & Hunt, J. V. (1997). Glucose modification of human serum albumin: a structural study. Free Radical Biology and Medicine, 22(7), 1217\u20131227.","journal-title":"Free Radical Biology and Medicine"},{"issue":"9","key":"884_CR48","doi-asserted-by":"publisher","first-page":"669","DOI":"10.1515\/cclm.1997.35.9.669","volume":"35","author":"G M\u00fcnch","year":"1997","unstructured":"M\u00fcnch, G., Keis, R., We\u00dfels, A., Riederer, P., Bahner, U., Heidland, A., Niwa, T., Lemke, H. D., & Schinzel, R. (1997). Determination of advanced glycation end products in serum by fluorescence spectroscopy and competitive ELISA. Clinical Chemistry and Laboratory Medicine, 35(9), 669\u2013678.","journal-title":"Clinical Chemistry and Laboratory Medicine"},{"issue":"1","key":"884_CR49","doi-asserted-by":"publisher","first-page":"184","DOI":"10.1196\/annals.1333.023","volume":"1043","author":"R Cheng","year":"2005","unstructured":"Cheng, R., Feng, Q., Argirov, O. K., & Ortwerth, B. J. (2005). K2P\u2014A novel cross\u2010link from human lens protein. Annals of the New York Academy of Sciences, 1043(1), 184\u2013194.","journal-title":"Annals of the New York Academy of Sciences"},{"issue":"1","key":"884_CR50","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0191014","volume":"13","author":"MA Khan","year":"2018","unstructured":"Khan, M. A., Arif, Z., Khan, M. A., & Alam, K. (2018). Methylglyoxal produces more changes in biochemical and biophysical properties of human IgG under high glucose compared to normal glucose level. PLoS ONE, 13(1), e0191014.","journal-title":"PLoS ONE"},{"issue":"7","key":"884_CR51","doi-asserted-by":"publisher","first-page":"1487","DOI":"10.1007\/s11095-007-9516-9","volume":"25","author":"A Hawe","year":"2008","unstructured":"Hawe, A., Sutter, M., & Jiskoot, W. (2008). Extrinsic fluorescent dyes as tools for protein characterization. Pharmaceutical Research, 25(7), 1487\u20131499.","journal-title":"Pharmaceutical Research"},{"issue":"37","key":"884_CR52","doi-asserted-by":"publisher","first-page":"11177","DOI":"10.1021\/bi000200n","volume":"39","author":"KW Plaxco","year":"2000","unstructured":"Plaxco, K. W., Simons, K. T., Ruczinski, I., & Baker, D. (2000). Topology, stability, sequence, and length: defining the determinants of two-state protein folding kinetics. Biochemistry, 39(37), 11177\u201311183.","journal-title":"Biochemistry"},{"issue":"6","key":"884_CR53","first-page":"1460","volume":"41","author":"Y Nakamura","year":"2000","unstructured":"Nakamura, Y., Fukiage, C., Shih, M., Ma, H., David, L. L., Azuma, M., & Shearer, T. R. (2000). Contribution of calpain Lp82\u2013induced proteolysis to experimental cataractogenesis in mice. Investigative Ophthalmology & Visual Science, 41(6), 1460\u20131466.","journal-title":"Investigative Ophthalmology & Visual Science"},{"issue":"9","key":"884_CR54","first-page":"301","volume":"11","author":"S Biswas","year":"2005","unstructured":"Biswas, S., Harris, F., Dennison, S., Singh, J. P., & Phoenix, D. (2005). Calpains: enzymes of vision? Medical Science Monitor, 11(9), 301\u2013310.","journal-title":"Medical Science Monitor"},{"issue":"2","key":"884_CR55","doi-asserted-by":"publisher","first-page":"300","DOI":"10.1006\/bbrc.2000.3298","volume":"275","author":"Y Tamada","year":"2000","unstructured":"Tamada, Y., Fukiage, C., Nakamura, Y., Azuma, M., Kim, Y., & Shearer, T. (2000). Evidence for apoptosis in the selenite rat model of cataract. Biochemical and Biophysical Research Communications, 275(2), 300\u2013306.","journal-title":"Biochemical and Biophysical Research Communications"},{"issue":"3","key":"884_CR56","doi-asserted-by":"publisher","first-page":"1016","DOI":"10.1167\/iovs.07-0792","volume":"49","author":"LJ Robertson","year":"2008","unstructured":"Robertson, L. J., David, L. L., Riviere, M. A., Wilmarth, P. A., Muir, M. S., & Morton, J. D. (2008). Susceptibility of ovine lens crystallins to proteolytic cleavage during formation of hereditary cataract. Investigative Ophthalmology & Visual Science, 49(3), 1016\u20131022.","journal-title":"Investigative Ophthalmology & Visual Science"},{"key":"884_CR57","doi-asserted-by":"publisher","first-page":"200","DOI":"10.1016\/j.diabres.2019.01.002","volume":"148","author":"J Bellier","year":"2019","unstructured":"Bellier, J., Nokin, M. J., Lard\u00e9, E., Karoyan, P., Peulen, O., Castronovo, V., & Bellahc\u00e8ne, A. (2019). Methylglyoxal, a potent inducer of AGEs, connects between diabetes and cancer. Diabetes Research and Clinical Practice, 148, 200\u2013211.","journal-title":"Diabetes Research and Clinical Practice"},{"issue":"1","key":"884_CR58","doi-asserted-by":"publisher","first-page":"10","DOI":"10.2174\/1871530317666170703123519","volume":"11","author":"F Aydin","year":"2018","unstructured":"Aydin, F., Kalaz, E. B., Kucukgergin, C., Coban, J., Dogru-Abbasoglu, S., & Uysal, M. (2018). Carnosine treatment diminished oxidative stress and glycation products in serum and tissues of D-galactose-treated rats. Current Aging Science, 11(1), 10\u201315.","journal-title":"Current Aging Science"},{"key":"884_CR59","doi-asserted-by":"publisher","unstructured":"Sahin, S., Uyla\u015f, U., Sahinturk, V., & Alatas, O. (2018). Protective effect of carnosine on hepatic ischemia-reperfusion injury in rats. Osmangazi T\u0131p Dergisi,\n\nhttps:\/\/doi.org\/10.20515\/otd.481714\n\n.","DOI":"10.20515\/otd.481714"},{"issue":"8","key":"884_CR60","doi-asserted-by":"publisher","first-page":"1766","DOI":"10.1080\/07391102.2016.1194230","volume":"35","author":"S Javadi","year":"2017","unstructured":"Javadi, S., Yousefi, R., Hosseinkhani, S., Tamaddon, A. M., & Uversky, V.N. (2017). Protective effects of carnosine on dehydroascorbate-induced structural alteration and opacity of lens crystallins: Important implications of carnosine pleiotropic functions to combat cataractogenesis. Journal of Biomolecular Structure and Dynamics, 35(8), 1766\u20131784.","journal-title":"Journal of Biomolecular Structure and Dynamics"},{"issue":"3","key":"884_CR61","doi-asserted-by":"publisher","first-page":"513","DOI":"10.1021\/acs.chemrestox.8b00363","volume":"32","author":"L Carroll","year":"2019","unstructured":"Carroll, L., Karton, A., Radom, L., Davies, M. J., & Pattison, D. I. (2019). Carnosine and carcinine derivatives rapidly react with hypochlorous acid to form chloramines and dichloramines. Chemical Research in Toxicology, 32(3), 513\u2013525.","journal-title":"Chemical Research in Toxicology"},{"key":"884_CR62","doi-asserted-by":"publisher","first-page":"8","DOI":"10.31665\/JFB.2019.5174","volume":"5","author":"L Xing","year":"2019","unstructured":"Xing, L., Chee, M. E., Zhang, H., Zhang, W., & Mine, Y. (2019). Carnosine\u2014a natural bioactive dipeptide: bioaccessibility, bioavailability and health benefits. Journal of Food Bioactives, 5, 8\u201317.","journal-title":"Journal of Food Bioactives"},{"issue":"5","key":"884_CR63","doi-asserted-by":"publisher","first-page":"1367","DOI":"10.1111\/1541-4337.12376","volume":"17","author":"MA Freund","year":"2018","unstructured":"Freund, M. A., Chen, B., & Decker, E. A. (2018). The inhibition of advanced glycation end products by carnosine and other natural dipeptides to reduce diabetic and age\u2010related complications. Comprehensive Reviews in Food Science and Food Safety, 17(5), 1367\u20131378.","journal-title":"Comprehensive Reviews in Food Science and Food Safety"},{"key":"884_CR64","doi-asserted-by":"crossref","unstructured":"Preedy, V. R. (2015). Imidazole dipeptides: chemistry, analysis, function and effects. In Royal Society of Chemistry. RSC Publishing, Cambridge, 217\u2013237.","DOI":"10.1039\/9781782622611"}],"container-title":["Cell Biochemistry and Biophysics"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1007\/s12013-019-00884-3.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/link.springer.com\/article\/10.1007\/s12013-019-00884-3\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/link.springer.com\/content\/pdf\/10.1007\/s12013-019-00884-3.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2020,10,9]],"date-time":"2020-10-09T18:38:12Z","timestamp":1602268692000},"score":1,"resource":{"primary":{"URL":"http:\/\/link.springer.com\/10.1007\/s12013-019-00884-3"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,9,18]]},"references-count":64,"journal-issue":{"issue":"4","published-print":{"date-parts":[[2019,12]]}},"alternative-id":["884"],"URL":"https:\/\/doi.org\/10.1007\/s12013-019-00884-3","relation":{},"ISSN":["1085-9195","1559-0283"],"issn-type":[{"value":"1085-9195","type":"print"},{"value":"1559-0283","type":"electronic"}],"subject":[],"published":{"date-parts":[[2019,9,18]]},"assertion":[{"value":"12 March 2019","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"5 September 2019","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"18 September 2019","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Compliance with Ethical Standards"}},{"value":"The authors declare that they have no conflict of interest.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Conflict of Interest"}}]}}