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Volumn 442, Issue 1, 2012, Pages 221-230

Ellagic acid, a new antiglycating agent: Its inhibition of N ε-(carboxymethyl)lysine

Author keywords

Advanced glycation end product (AGE); Ellagic acid; Haemoglobin (Hb); Lens protein; Lens transparency; Lysozyme; N (carboxymethyl)lysine

Indexed keywords

ADVANCED GLYCATION END PRODUCT; ASCORBIC ACID; BOVINE SERUM ALBUMIN; CARBONYL DERIVATIVE; ELLAGIC ACID; FRUCTOSE; GLYCOSYLATED HEMOGLOBIN; LYSINE DERIVATIVE; LYSOZYME; METHYLGLYOXAL; N EPSILON(CARBOXYMETHYL)LYSINE; PROTEIN; RIBOSE; UNCLASSIFIED DRUG;

EID: 84856282540     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20110846     Document Type: Article
Times cited : (77)

References (55)
  • 1
    • 2342466734 scopus 로고    scopus 로고
    • Global Prevalence of Diabetes: Estimates for the year 2000 and projections for 2030
    • DOI 10.2337/diacare.27.5.1047
    • Wild, S., Roglic, G., Green, A., Sicree, R. and King, H. (2004) Global prevalence of diabetes: estimates for the year 2000 and projections for 2030. Diabetes Care 27, 1047-1053 (Pubitemid 38579764)
    • (2004) Diabetes Care , vol.27 , Issue.5 , pp. 1047-1053
    • Wild, S.1    Roglic, G.2    Green, A.3    Sicree, R.4    King, H.5
  • 3
    • 0035856980 scopus 로고    scopus 로고
    • Biochemistry and molecular cell biology of diabetic complications
    • Brownlee, M. (2001) Biochemistry and molecular cell biology of diabetic complications. Nature 414, 813-820
    • (2001) Nature , vol.414 , pp. 813-820
    • Brownlee, M.1
  • 4
    • 0035135246 scopus 로고    scopus 로고
    • Advanced glycation end-products: A review
    • DOI 10.1007/s001250051591
    • Singh, R., Barden, A., Mori, T. and Beilin, L. (2001) Advanced glycation end-products: a review. Diabetologia 44, 129-146 (Pubitemid 32156196)
    • (2001) Diabetologia , vol.44 , Issue.2 , pp. 129-146
    • Singh, R.1    Barden, A.2    Mori, T.3    Beilin, L.4
  • 5
    • 0032913309 scopus 로고    scopus 로고
    • Role of oxidative stress in diabetic complications: A new perspective on an old paradigm
    • DOI 10.2337/diabetes.48.1.1
    • Baynes, J. W. and Thorpe, S. R. (1999) Role of oxidative stress in diabetic complications: a new perspective on an old paradigm. Diabetes 48, 1-9 (Pubitemid 29019345)
    • (1999) Diabetes , vol.48 , Issue.1 , pp. 1-9
    • Baynes, J.W.1    Thorpe, S.R.2
  • 6
    • 11144324314 scopus 로고    scopus 로고
    • Advanced glycation endproducts - Role in pathology of diabetic complications
    • Ahmed, N. (2005) Advanced glycation endproducts - role in pathology of diabetic complications. Diabetes Res. Clin. Pract. 67, 3-21
    • (2005) Diabetes Res. Clin. Pract. , vol.67 , pp. 3-21
    • Ahmed, N.1
  • 7
    • 0028908348 scopus 로고
    • Advanced protein glycosylation in diabetes and aging
    • Brownlee, M. (1995) Advanced protein glycosylation in diabetes and aging. Annu. Rev. Med. 46, 223-234
    • (1995) Annu. Rev. Med. , vol.46 , pp. 223-234
    • Brownlee, M.1
  • 8
    • 0029998967 scopus 로고    scopus 로고
    • The presence of a glucose-derived Maillard reaction product in the human lens
    • DOI 10.1016/0014-5793(96)00142-1
    • Nagaraj, R. H. and Sady, C. (1996) The presence of a glucose-derived Maillard reaction product in the human lens. FEBS Lett. 382, 234-238 (Pubitemid 26092198)
    • (1996) FEBS Letters , vol.382 , Issue.3 , pp. 234-238
    • Nagaraj, R.H.1    Sady, C.2
  • 9
    • 0029793997 scopus 로고    scopus 로고
    • Advanced glycation end-products and atherosclerosis
    • Vlassara, H. (1996) Advanced glycation end-products and atherosclerosis. Ann. Med. 28, 419-426
    • (1996) Ann. Med. , vol.28 , pp. 419-426
    • Vlassara, H.1
  • 10
    • 0024852380 scopus 로고
    • Structure elucidation of a senescence cross-link from human extracellular matrix. Implication of pentoses in the aging process
    • Sell, D. R. and Monnier, V. M. (1989) Structure elucidation of a senescence cross-link from human extracellular matrix. Implication of pentoses in the aging process. J. Biol. Chem. 264, 21597-21602 (Pubitemid 20028722)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.36 , pp. 21597-21602
    • Sell, D.R.1    Monnir, V.M.2
  • 12
    • 0025892834 scopus 로고
    • Role of glycation in modification of lens crystallins in diabetic and nondiabetic senile cataracts
    • Lyons, T. J., Silvestri, G., Dunn, J. A., Dyer, D. G. and Baynes, J. W. (1991) Role of glycation in modification of lens crystallins in diabetic and nondiabetic senile cataracts. Diabetes 40, 1010-1015
    • (1991) Diabetes , vol.40 , pp. 1010-1015
    • Lyons, T.J.1    Silvestri, G.2    Dunn, J.A.3    Dyer, D.G.4    Baynes, J.W.5
  • 13
    • 84862553056 scopus 로고    scopus 로고
    • Advanced glycation end-products, a pathophysiological pathway in the cardiorenal syndrome
    • doi:10.1007/s10741-010-9225-z
    • Willemsen, S., Hartog, J. W., Heiner-Fokkema, M. R., van Veldhuisen, D. J. and Voors, A. A. (2011) Advanced glycation end-products, a pathophysiological pathway in the cardiorenal syndrome. Heart Fail. Rev. doi:10.1007/s10741-010- 9225-z
    • (2011) Heart Fail. Rev.
    • Willemsen, S.1    Hartog, J.W.2    Heiner-Fokkema, M.R.3    Van Veldhuisen, D.J.4    Voors, A.A.5
  • 14
    • 0025824383 scopus 로고
    • Post-translational modification of lens proteins in cataract
    • Harding, J. J. (1991) Post-translational modification of lens proteins in cataract. Lens Eye Toxic Res. 8, 245-250
    • (1991) Lens Eye Toxic Res. , vol.8 , pp. 245-250
    • Harding, J.J.1
  • 15
    • 84862643485 scopus 로고    scopus 로고
    • Lipid glycation and protein glycation in diabetes and atherosclerosis
    • doi:10.1007/s00726-010-0772-3
    • Miyazawa, T., Nakagawa, K., Shimasaki, S. and Nagai, R., Lipid glycation and protein glycation in diabetes and atherosclerosis. (2010) Amino Acids doi:10.1007/s00726-010-0772-3
    • (2010) Amino Acids
    • Miyazawa, T.1    Nakagawa, K.2    Shimasaki, S.3    Nagai, R.4
  • 16
    • 0027317391 scopus 로고
    • Nonenzymatic glycation alters protein structure and stability. A study of two eye lens crystallins
    • Luthra, M. and Balasubramanian, D. (1993) Nonenzymatic glycation alters protein structure and stability. A study of two eye lens crystallins. J. Biol. Chem. 268, 18119-18127 (Pubitemid 23260332)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.24 , pp. 18119-18127
    • Luthra, M.1    Balasubramanian, D.2
  • 17
    • 2342463583 scopus 로고    scopus 로고
    • Effect of dicarbonyl-induced browning on alpha-crystallin chaperone-like activity: Physiological significance and caveats of in vitro aggregation assays
    • DOI 10.1042/BJ20031633
    • Kumar, M. S., Reddy, P. Y., Kumar, P. A., Surolia, I. and Reddy, G. B. (2004) Effect of dicarbonyl-induced browning on alpha-crystallin chaperone-like activity: physiological significance and caveats of in vitro aggregation assays. Biochem. J. 379, 273-282 (Pubitemid 38570099)
    • (2004) Biochemical Journal , vol.379 , Issue.2 , pp. 273-282
    • Kumar, M.S.1    Reddy, P.Y.2    Kumar, P.A.3    Surolia, I.4    Reddy, G.B.5
  • 18
    • 0028304625 scopus 로고
    • Enhanced cellular oxidant stress by the interaction of advanced glycation end products with their receptors/binding proteins
    • Yan, S. D., Schmidt, A. M., Anderson, G. M., Zhang, J., Brett, J., Zou, Y. S., Pinsky, D. and Stern, D. (1994) Enhanced cellular oxidant stress by the interaction of advanced glycation end products with their receptors/binding proteins. J. Biol. Chem. 269, 9889-9897 (Pubitemid 24196599)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.13 , pp. 9889-9897
    • Yan, S.D.1    Schmidt, A.M.2    Anderson, G.M.3    Zhang, J.4    Brett, J.5    Zou, Y.S.6    Pinsky, D.7    Stern, D.8
  • 19
    • 36749055907 scopus 로고    scopus 로고
    • Effect of glycation on alpha-crystallin structure and chaperone-like function
    • DOI 10.1042/BJ20070989
    • Kumar, P. A., Kumar, M. S. and Reddy, G. B. (2007) Effect of glycation on alpha-crystallin structure and chaperone-like function. Biochem. J. 408, 251-258 (Pubitemid 350206348)
    • (2007) Biochemical Journal , vol.408 , Issue.2 , pp. 251-258
    • Kumar, P.A.1    Kumar, M.S.2    Reddy, G.B.3
  • 20
    • 0034992635 scopus 로고    scopus 로고
    • Increased protein glycation in cerebrospinal fluid of Alzheimer's disease
    • DOI 10.1016/S0197-4580(00)00253-0, PII S0197458000002530
    • Shuvaev, V. V., Laffont, I., Serot, J. M., Fujii, J., Taniguchi, N. and Siest, G. (2001) Increased protein glycation in cerebrospinal fluid of Alzheimer's disease. Neurobiol. Aging 22, 397-402 (Pubitemid 32510910)
    • (2001) Neurobiology of Aging , vol.22 , Issue.3 , pp. 397-402
    • Shuvaev, V.V.1    Laffont, I.2    Serot, J.-M.3    Fujii, J.4    Taniguchi, N.5    Siest, G.6
  • 22
    • 0029687013 scopus 로고    scopus 로고
    • Advanced glycosylation in nephropathy of diabetes and aging
    • Vlassara, H. (1996) Advanced glycosylation in nephropathy of diabetes and aging. Adv. Nephrol. Necker. Hosp. 25, 303-315
    • (1996) Adv. Nephrol. Necker. Hosp. , vol.25 , pp. 303-315
    • Vlassara, H.1
  • 25
    • 0142029114 scopus 로고    scopus 로고
    • Novel inhibitors of advanced glycation endproducts
    • DOI 10.1016/j.abb.2003.08.009
    • Rahbar, S. and Figarola, J. L. (2003) Novel inhibitors of advanced glycation endproducts. Arch. Biochem. Biophys. 419, 63-79 (Pubitemid 37287559)
    • (2003) Archives of Biochemistry and Biophysics , vol.419 , Issue.1 , pp. 63-79
    • Rahbar, S.1    Figarola, J.L.2
  • 26
    • 0032857820 scopus 로고    scopus 로고
    • Design and baseline characteristics for the aminoguanidine clinical trial in overt type 2 diabetic nephropathy (ACTION II)
    • DOI 10.1016/S0197-2456(99)00024-0, PII S0197245699000240
    • Freedman, B. I., Wuerth, J. P., Cartwright, K., Bain, R. P., Dippe, S., Hershon, K., Mooradian, A. D. and Spinowitz, B. S. (1999) Design and baseline characteristics for the Aminoguanidine Clinical Trial in Overt Type 2 Diabetic Nephropathy (ACTION II). Control Clin. Trials 20, 493-510 (Pubitemid 29460926)
    • (1999) Controlled Clinical Trials , vol.20 , Issue.5 , pp. 493-510
    • Freedman, B.I.1    Wuerth, J.-P.2    Cartwright, K.3    Bain, R.P.4    Dippe, S.5    Hershon, K.6    Mooradian, A.D.7    Spinowitz, B.S.8
  • 27
    • 0032524963 scopus 로고    scopus 로고
    • In vivo formation of a Schiff base of aminoguanidine with pyridoxal phosphate
    • DOI 10.1016/S0006-2952(98)00010-0, PII S0006295298000100
    • Taguchi, T., Sugiura, M., Hamada, Y. and Miwa, I. (1998) In vivo formation of a Schiff base of aminoguanidine with pyridoxal phosphate. Biochem. Pharmacol. 55, 1667-1671 (Pubitemid 28223459)
    • (1998) Biochemical Pharmacology , vol.55 , Issue.10 , pp. 1667-1671
    • Taguchi, T.1    Sugiura, M.2    Hamada, Y.3    Miwa, I.4
  • 28
    • 0142074864 scopus 로고    scopus 로고
    • Use of aminoguanidine (Pimagedine) to prevent the formation of advanced glycation endproducts
    • Thornalley, P. J. (2003) Use of aminoguanidine (Pimagedine) to prevent the formation of advanced glycation endproducts. Arch. Biochem. Biophys. 419, 31-40
    • (2003) Arch. Biochem. Biophys. , vol.419 , pp. 31-40
    • Thornalley, P.J.1
  • 29
    • 47549111139 scopus 로고    scopus 로고
    • Therapeutic applications of pomegranate (Punica granatum L.): A review
    • Jurenka, J. S. (2008) Therapeutic applications of pomegranate (Punica granatum L.): a review. Altern. Med. Rev. 13, 128-144
    • (2008) Altern. Med. Rev. , vol.13 , pp. 128-144
    • Jurenka, J.S.1
  • 31
    • 51349096457 scopus 로고    scopus 로고
    • Multitargeted therapy of cancer by ellagitannins
    • Heber, D. (2008) Multitargeted therapy of cancer by ellagitannins. Cancer Lett. 269, 262-268
    • (2008) Cancer Lett. , vol.269 , pp. 262-268
    • Heber, D.1
  • 32
    • 79952111529 scopus 로고    scopus 로고
    • Ellagic acid inhibits oxidized LDL-mediated LOX-1 expression, ROS generation, and inflammation in human endothelial cells
    • Lee, W. J., Ou, H. C., Hsu, W. C., Chou, M. M., Tseng, J. J., Hsu, S. L., Tsai, K. L. and Sheu, W. H. Ellagic acid inhibits oxidized LDL-mediated LOX-1 expression, ROS generation, and inflammation in human endothelial cells. J. Vasc. Surg. 52, 1290-1300
    • J. Vasc. Surg. , vol.52 , pp. 1290-1300
    • Lee, W.J.1    Ou, H.C.2    Hsu, W.C.3    Chou, M.M.4    Tseng, J.J.5    Hsu, S.L.6    Tsai, K.L.7    Sheu, W.H.8
  • 33
    • 67649429389 scopus 로고    scopus 로고
    • Prevention of non-enzymic glycation of proteins by dietary agents: Prospects for alleviating diabetic complications
    • Saraswat, M., Reddy, P. Y., Muthenna, P. and Reddy, G. B. (2009) Prevention of non-enzymic glycation of proteins by dietary agents: prospects for alleviating diabetic complications. Br. J. Nutr. 101, 1714-1721
    • (2009) Br. J. Nutr. , vol.101 , pp. 1714-1721
    • Saraswat, M.1    Reddy, P.Y.2    Muthenna, P.3    Reddy, G.B.4
  • 34
    • 34547505136 scopus 로고    scopus 로고
    • Effect of curcumin on hyperglycemia-induced vascular endothelial growth factor expression in streptozotocin-induced diabetic rat retina
    • DOI 10.1016/j.bbrc.2007.07.059, PII S0006291X0701546X
    • Mrudula, T., Suryanarayana, P., Srinivas, P. N. and Reddy, G. B. (2007) Effect of curcumin on hyperglycemia-induced vascular endothelial growth factor expression in streptozotocin-induced diabetic rat retina. Biochem. Biophys. Res. Commun. 361, 528-532 (Pubitemid 47187290)
    • (2007) Biochemical and Biophysical Research Communications , vol.361 , Issue.2 , pp. 528-532
    • Mrudula, T.1    Suryanarayana, P.2    Srinivas, P.N.B.S.3    Reddy, G.B.4
  • 35
    • 67651052702 scopus 로고    scopus 로고
    • Delay of diabetic cataract in rats by the antiglycating potential of cumin through modulation of alpha-crystallin chaperone activity
    • Kumar, P. A., Reddy, P. Y., Srinivas, P. N. and Reddy, G. B. (2009) Delay of diabetic cataract in rats by the antiglycating potential of cumin through modulation of alpha-crystallin chaperone activity. J. Nutr. Biochem. 20, 553-562
    • (2009) J. Nutr. Biochem. , vol.20 , pp. 553-562
    • Kumar, P.A.1    Reddy, P.Y.2    Srinivas, P.N.3    Reddy, G.B.4
  • 36
    • 77955704177 scopus 로고    scopus 로고
    • Antiglycating potential of Zingiber officinalis and delay of diabetic cataract in rats
    • Saraswat, M., Suryanarayana, P., Reddy, P. Y., Patil, M. A., Balakrishna, N. and Reddy, G. B. (2010) Antiglycating potential of Zingiber officinalis and delay of diabetic cataract in rats. Mol. Vis. 16, 1525-1537
    • (2010) Mol. Vis. , vol.16 , pp. 1525-1537
    • Saraswat, M.1    Suryanarayana, P.2    Reddy, P.Y.3    Patil, M.A.4    Balakrishna, N.5    Reddy, G.B.6
  • 37
    • 0033789887 scopus 로고    scopus 로고
    • Ellagic acid, vitamin C, and total phenolic contents and radical scavenging capacity affected by freezing and frozen storage in raspberry fruit
    • De Ancos, B., Gonzalez, E. M. and Cano, M. P. (2000) Ellagic acid, vitamin C, and total phenolic contents and radical scavenging capacity affected by freezing and frozen storage in raspberry fruit. J. Agric. Food Chem. 48, 4565-4570
    • (2000) J. Agric. Food Chem. , vol.48 , pp. 4565-4570
    • De Ancos, B.1    Gonzalez, E.M.2    Cano, M.P.3
  • 38
    • 79957598613 scopus 로고    scopus 로고
    • Ellagitannins, ellagic acid and their derived metabolites: A review about source, metabolism, functions and health
    • Landete, J. M. (2011) Ellagitannins, ellagic acid and their derived metabolites: a review about source, metabolism, functions and health. Food Res. Int. 44, 1150-1160
    • (2011) Food Res. Int. , vol.44 , pp. 1150-1160
    • Landete, J.M.1
  • 39
    • 11144346788 scopus 로고    scopus 로고
    • Effect of nonenzymatic glycation on functional and structural properties of hemoglobin
    • DOI 10.1016/j.bpc.2004.05.005, PII S0301462204001383
    • Sen, S., Kar, M., Roy, A. and Chakraborti, A. S. (2005) Effect of nonenzymatic glycation on functional and structural properties of hemoglobin. Biophys. Chem. 113, 289-298 (Pubitemid 40037809)
    • (2005) Biophysical Chemistry , vol.113 , Issue.3 , pp. 289-298
    • Sen, S.1    Kar, M.2    Roy, A.3    Chakraborti, A.S.4
  • 40
    • 33947219872 scopus 로고    scopus 로고
    • Aged garlic extract and S-allyl cysteine prevent formation of advanced glycation endproducts
    • DOI 10.1016/j.ejphar.2007.01.041, PII S0014299907000891
    • Ahmad, M. S., Pischetsrieder, M. and Ahmed, N. (2007) Aged garlic extract and S-allyl cysteine prevent formation of advanced glycation endproducts. Eur. J. Pharmacol. 561, 32-38 (Pubitemid 46435858)
    • (2007) European Journal of Pharmacology , vol.561 , Issue.1-3 , pp. 32-38
    • Ahmad, M.S.1    Pischetsrieder, M.2    Ahmed, N.3
  • 41
    • 4544361960 scopus 로고    scopus 로고
    • Tomato paste fraction inhibiting the formation of advanced glycation end-products
    • DOI 10.1271/bbb.68.200
    • Kiho, T., Usui, S., Hirano, K., Aizawa, K. and Inakuma, T. (2004) Tomato paste fraction inhibiting the formation of advanced glycation end-products. Biosci. Biotechnol. Biochem. 68, 200-205 (Pubitemid 39251584)
    • (2004) Bioscience, Biotechnology and Biochemistry , vol.68 , Issue.1 , pp. 200-205
    • Kiho, T.1    Usui, S.2    Hirano, K.3    Aizawa, K.4    Inakuma, T.5
  • 42
    • 0035966113 scopus 로고    scopus 로고
    • Chelating activity of advanced glycation end-product inhibitors
    • Price, D. L., Rhett, P. M., Thorpe, S. R. and Baynes, J. W. (2001) Chelating activity of advanced glycation end-product inhibitors. J. Biol. Chem. 276, 48967-48972
    • (2001) J. Biol. Chem. , vol.276 , pp. 48967-48972
    • Price, D.L.1    Rhett, P.M.2    Thorpe, S.R.3    Baynes, J.W.4
  • 43
    • 0031054249 scopus 로고    scopus 로고
    • In vitro kinetic studies of formation of antigenic advanced glycation end products (AGEs). Novel inhibition of post-Amadori glycation pathways
    • DOI 10.1074/jbc.272.9.5430
    • Booth, A. A., Khalifah, R. G., Todd, P. and Hudson, B. G. (1997) In vitro kinetic studies of formation of antigenic advanced glycation end products (AGEs). Novel inhibition of post-Amadori glycation pathways. J. Biol. Chem. 272, 5430-5437 (Pubitemid 27102361)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.9 , pp. 5430-5437
    • Booth, A.A.1    Khalifah, R.G.2    Todd, P.3    Hudson, B.G.4
  • 44
    • 0032878626 scopus 로고    scopus 로고
    • A new rapid method to detect inhibition of Amadori product generated by delta-gluconolactone
    • DOI 10.1016/S0009-8981(99)00125-4, PII S0009898199001254
    • Rahbar, S. and Nadler, J. L. (1999) A new rapid method to detect inhibition of Amadori product generated by delta-gluconolactone. Clin. Chim. Acta 287, 123-130 (Pubitemid 29413014)
    • (1999) Clinica Chimica Acta , vol.287 , Issue.1-2 , pp. 123-130
    • Rahbar, S.1    Nadler, J.L.2
  • 45
    • 84856265105 scopus 로고    scopus 로고
    • Inhibition of advanced glycation end-product formation on eye lens protein by rutin
    • Muthenna, P., Akileshwari, C., Saraswat, M. and Bhanuprakash Reddy, G. (2011) Inhibition of advanced glycation end-product formation on eye lens protein by rutin. Br. J. Nutr. 25, 1-9
    • (2011) Br. J. Nutr. , vol.25 , pp. 1-9
    • Muthenna, P.1    Akileshwari, C.2    Saraswat, M.3    Bhanuprakash Reddy, G.4
  • 46
    • 79952111529 scopus 로고    scopus 로고
    • Ellagic acid inhibits oxidized LDL-mediated LOX-1 expression, ROS generation, and inflammation in human endothelial cells
    • Lee, W. J., Ou, H. C., Hsu, W. C., Chou, M. M., Tseng, J. J., Hsu, S. L., Tsai, K. L. and Sheu, W. H. (2010) Ellagic acid inhibits oxidized LDL-mediated LOX-1 expression, ROS generation, and inflammation in human endothelial cells. J. Vasc. Surg. 52, 1290-1300
    • (2010) J. Vasc. Surg. , vol.52 , pp. 1290-1300
    • Lee, W.J.1    Ou, H.C.2    Hsu, W.C.3    Chou, M.M.4    Tseng, J.J.5    Hsu, S.L.6    Tsai, K.L.7    Sheu, W.H.8
  • 47
    • 0031752685 scopus 로고    scopus 로고
    • Global burden of diabetes, 1995-2025: Prevalence, numerical estimates, and projections
    • King, H., Aubert, R. E. and Herman, W. H. (1998) Global burden of diabetes, 1995-2025: prevalence, numerical estimates, and projections. Diabetes Care 21, 1414-1431 (Pubitemid 28405191)
    • (1998) Diabetes Care , vol.21 , Issue.9 , pp. 1414-1431
    • King, H.1    Aubert, R.E.2    Herman, W.H.3
  • 49
    • 0029870323 scopus 로고    scopus 로고
    • Thiamine pyrophosphate and pyridoxamine inhibit the formation of antigenic advanced glycation end-products: Comparison with aminoguanidine
    • Booth, A. A., Khalifah, R. G. and Hudson, B. G. (1996) Thiamine pyrophosphate and pyridoxamine inhibit the formation of antigenic advanced glycation end-products: comparison with aminoguanidine. Biochem. Biophys. Res. Commun. 220, 113-119
    • (1996) Biochem. Biophys. Res. Commun. , vol.220 , pp. 113-119
    • Booth, A.A.1    Khalifah, R.G.2    Hudson, B.G.3
  • 50
    • 65349103941 scopus 로고    scopus 로고
    • Antioxidative activity, polyphenolic content and antiglycation effect of some Thai medicinal plants traditionally used in diabetic patients
    • Kusirisin, W., Srichairatanakool, S., Lerttrakarnnon, P., Lailerd, N., Suttajit, M., Jaikang, C. and Chaiyasut, C. (2009) Antioxidative activity, polyphenolic content and antiglycation effect of some Thai medicinal plants traditionally used in diabetic patients. Med. Chem. 5, 139-147
    • (2009) Med. Chem. , vol.5 , pp. 139-147
    • Kusirisin, W.1    Srichairatanakool, S.2    Lerttrakarnnon, P.3    Lailerd, N.4    Suttajit, M.5    Jaikang, C.6    Chaiyasut, C.7
  • 51
    • 0037051521 scopus 로고    scopus 로고
    • Protective activity of green tea against free radical- and glucose-mediated protein damage
    • DOI 10.1021/jf011339n
    • Nakagawa, T., Yokozawa, T., Terasawa, K., Shu, S. and Juneja, L. R. (2002) Protective activity of green tea against free radical- and glucose-mediated protein damage. J. Agric. Food Chem. 50, 2418-2422 (Pubitemid 34275319)
    • (2002) Journal of Agricultural and Food Chemistry , vol.50 , Issue.8 , pp. 2418-2422
    • Nakagawa, T.1    Yokozawa, T.2    Terasawa, K.3    Shu, S.4    Juneja, L.R.5
  • 53
    • 34249302408 scopus 로고    scopus 로고
    • Hypothesis: The 'metabolic memory', the new challenge of diabetes
    • DOI 10.1111/j.1464-5491.2007.02138.x
    • Ihnat, M. A., Thorpe, J. E. and Ceriello, A. (2007) Hypothesis: the 'metabolic memory', the new challenge of diabetes. Diabet. Med. 24, 582-586 (Pubitemid 46808866)
    • (2007) Diabetic Medicine , vol.24 , Issue.6 , pp. 582-586
    • Ihnat, M.A.1    Thorpe, J.E.2    Ceriello, A.3
  • 54
    • 18844369302 scopus 로고    scopus 로고
    • Role of aldose reductase and oxidative damage in diabetes and the consequent potential for therapeutic options
    • DOI 10.1210/er.2004-0028
    • Srivastava, S. K., Ramana, K. V. and Bhatnagar, A. (2005) Role of aldose reductase and oxidative damage in diabetes and the consequent potential for therapeutic options. Endocr. Rev. 26, 380-392 (Pubitemid 40691299)
    • (2005) Endocrine Reviews , vol.26 , Issue.3 , pp. 380-392
    • Srivastava, S.K.1    Ramana, K.V.2    Bhatnagar, A.3


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