1 |
Baynes, J. W., Role of oxidative stress in development of complications in diabetes. Diabetes, 40, 405-412 (1991)
DOI
ScienceOn
|
2 |
Brownlee, M., Biochemistry and molecular biology of diabetic complications. Nature, 414, 813-820 (2000)
DOI
ScienceOn
|
3 |
Duhaiman, A. S., Rabbani, N., and Cotlier, E., Camel lens crystallins glycosylation and high molecular weight aggregate formation in the presence of ferrous ions and glucose. Biochem. Biophys. Res. Commun., 173, 823-832 (1990)
DOI
ScienceOn
|
4 |
Jiang, Z. Y., Hunt, J. V., and Wolff, S. P., Ferrous ion oxidation in the presence of xylenol orange for detection of lipid hydroperoxide in low density lipoprotein. Anal. Biochem., 202, 384-389 (1992)
DOI
|
5 |
Myint, T., Hoshi, S., Ookawara, T., Miyazawa, N., Suzuki, K., and Taniguchi, N., Immunological detection of glycated proteins in normal and streptozotocin-induced diabetic rats using anti hexitol-lysine IgG. Biochim. Biophys. Acta, 1272, 73-79 (1995)
DOI
ScienceOn
|
6 |
Sundaresan, M., Yu, Z. Y., Ferrans, C. J., Irani, K., and Finkel, T., Requirement for generation of H2O2 for platelet-derived growth factor signal transduction. Science, 270, 296-299 (1995)
DOI
ScienceOn
|
7 |
Varma, S. D. and Kinoshita, J. H., Sorbitol pathway in diabetic and galactosemic rat lens. Biochim. Biophys. Acta, 328, 632- 640 (1974)
|
8 |
Chance, B., Sies, H., and Boveris, A., Hydroperoxide metabolism in mammalian organs. Physiol. Rev., 59, 527-605 (1979)
DOI
|
9 |
Brownlee, M., Vlassara, H., and Cerami, A., Nonenzymatic glycosylation and the pathogenesis of diabetic complications. Ann. Int. Med., 101, 527-537 (1984)
DOI
ScienceOn
|
10 |
Kil, I. S., Lee, J. H., Shin, A. H., and Park, J.-W., Glycationinduced inactivation of -dependent isocitrate dehydrogenase: Imp;ications for diabetes and aging. Free Radic. Biol. Med., 37, 1765-1778 (2004)
DOI
ScienceOn
|
11 |
Meister, A. and Anderson, M. E., Glutathione. Ann. Rev. Biochem., 52, 711-760 (1983)
DOI
ScienceOn
|
12 |
Tauskela, J. S., Hewitt, K., Kang, L. P., Comas, T., Gendron, T., Hakim, A., Hogan, M., Durkin, J., and Morley, P., Evaluation of glutathione-sensitive fluorescent dyes in cortical culture. Glia, 30, 329-341 (2001)
DOI
ScienceOn
|
13 |
Lee, S. M., Koh, H. J., Park, D. C., Song, B. J., Huh, T. L., and Park, J. W., Cytosolic -dependent isocitrate dehydrogenase status modulates oxidative damage to cells. Free Radic. Biol. Med., 32, 1185-1196 (2002)
DOI
ScienceOn
|
14 |
Okimoto, Y., Watanabe, A., Niki, E., Yamashita, T., and Noguchi, N., A novel fluorescent probe diphenyl-1-pyrenylphosphine to follow lipid peroxidation in cell membranes. FEBS Lett., 474, 137-140 (2000)
DOI
ScienceOn
|
15 |
Nishikawa, T., Edelstein, D., Du, X. L., Yamagishi, S., Matsumura, T., Kaneda, Y., Yorek, M. A., Beebe, D., Oates, P. J., Hammes, H. P., Giardino, I., and Brownlee, M., Normalizing mitochondrial superoxide production blocks three pathways of hyperglycaemic damage. Nature, 404, 787-790 (2001)
DOI
ScienceOn
|
16 |
Tabatabaie, T. and Floyd, R. A., Susceptibility of glutathione peroxidase and glutathione reductase to oxidative damage and the protective effect of spin trapping agents. Arch. Biochem. Biophys., 314, 112-119 (1994)
DOI
ScienceOn
|
17 |
Shibutani, S., Takeshita, M., and Grollman, A. P., Insertion of specific base during DNA synthesis past the oxidationdamaged base 8-oxodG. Nature, 349, 431-434 (1991)
DOI
ScienceOn
|
18 |
Struthers, L., Patel, R., Clark, J., and Thomas, S., Direct detection of 8-oxodeoxyguanosine and 8-oxoguanine by avidin and its analogues. Anal. Biochem., 255, 20-31 (1998)
DOI
ScienceOn
|
19 |
Park, J. W. and Floyd, R. A., Lipid peroxidation products mediate the formation of 8-hydroxydeoxyguanosine in DNA. Free Radic. Biol. Med., 12, 245-250 (1992)
DOI
ScienceOn
|
20 |
McCord, J. M. and Fridovich, I., Superoxide dismutase: An enzymic function for erythrocuprein (hemocuprein). J. Biol. Chem., 224, 6049-6055 (1969)
|
21 |
Vincent, M. A., Brownlee, M., and Russell, J. W., Oxidative stress and programmed cell death in diabetic neuropathy. Ann. New York Acad. Sci., 959, 368-383 (2002)
DOI
|
22 |
Biemel, K. M., Friedl, D. A., and Lederer, M. O., Identification and quantification of major maillard cross-links in human serum albumin and lens protein. Evidence for glucosepane as the dominant compound. J. Biol. Chem., 277, 24907- 24915 (2002)
DOI
ScienceOn
|