메뉴 건너뛰기




Volumn 1804, Issue 4, 2010, Pages 789-798

Thermal aggregation of glycated bovine serum albumin

Author keywords

Albumin; FTIR spectroscopy; Glycation; Glycoxidation; Light scattering; Protein aggregation

Indexed keywords

ADVANCED GLYCATION END PRODUCT; BOVINE SERUM ALBUMIN; CYSTEINE; GLUCOSE; GLYCOSYLATED ALBUMIN;

EID: 77149162694     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2009.12.003     Document Type: Article
Times cited : (108)

References (66)
  • 2
    • 0036855661 scopus 로고    scopus 로고
    • Deciphering the genesis and fate of amyloid beta-protein yields novel therapies for Alzheimer disease
    • Selkoe D.J. Deciphering the genesis and fate of amyloid beta-protein yields novel therapies for Alzheimer disease. J. Clin. Invest. 110 (2002) 1375-1381
    • (2002) J. Clin. Invest. , vol.110 , pp. 1375-1381
    • Selkoe, D.J.1
  • 4
    • 0033827807 scopus 로고    scopus 로고
    • Influence of NaCl and CaCl2 on cold-set gelation of heat-denatured whey protein
    • Bryant C., and McClements D.J. Influence of NaCl and CaCl2 on cold-set gelation of heat-denatured whey protein. J. Food Sci. 65 (2000) 801-804
    • (2000) J. Food Sci. , vol.65 , pp. 801-804
    • Bryant, C.1    McClements, D.J.2
  • 5
    • 4143141192 scopus 로고    scopus 로고
    • Self-assembling peptides and proteins for nanotechnological applications
    • Rajagopal K., and Schneider J.P. Self-assembling peptides and proteins for nanotechnological applications. Curr. Opin. Struct. Biol. 14 (2004) 480-486
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 480-486
    • Rajagopal, K.1    Schneider, J.P.2
  • 6
    • 0043161935 scopus 로고    scopus 로고
    • Conformational changes involved in thermal aggregation processes of bovine serum albumin
    • Militello V., Vetri V., and Leone M. Conformational changes involved in thermal aggregation processes of bovine serum albumin. Biophys. Chem. 105 (2003) 133-141
    • (2003) Biophys. Chem. , vol.105 , pp. 133-141
    • Militello, V.1    Vetri, V.2    Leone, M.3
  • 8
    • 36048995611 scopus 로고    scopus 로고
    • Effects of succinylation on thermal induced amyloid formation in Concanavalin A
    • Vetri V., Librizzi F., Militello V., and Leone M. Effects of succinylation on thermal induced amyloid formation in Concanavalin A. Eur. Biophys. J. 36 (2007) 733-741
    • (2007) Eur. Biophys. J. , vol.36 , pp. 733-741
    • Vetri, V.1    Librizzi, F.2    Militello, V.3    Leone, M.4
  • 9
    • 1242271236 scopus 로고    scopus 로고
    • Aggregation kinetics of bovine serum albumin studied by FTIR spectroscopy and light scattering
    • Militello V., Casarino C., Emanuele A., Giostra A., Pullara F., and Leone M. Aggregation kinetics of bovine serum albumin studied by FTIR spectroscopy and light scattering. Biophys. Chem. 107 (2004) 175-187
    • (2004) Biophys. Chem. , vol.107 , pp. 175-187
    • Militello, V.1    Casarino, C.2    Emanuele, A.3    Giostra, A.4    Pullara, F.5    Leone, M.6
  • 10
    • 35748957119 scopus 로고    scopus 로고
    • Thermal aggregation of bovine serum albumin at different pH: comparison with human serum albumin
    • Vetri V., Librizzi F., Leone M., and Militello V. Thermal aggregation of bovine serum albumin at different pH: comparison with human serum albumin. Eur. Biophys. J. 36 (2007) 717-725
    • (2007) Eur. Biophys. J. , vol.36 , pp. 717-725
    • Vetri, V.1    Librizzi, F.2    Leone, M.3    Militello, V.4
  • 11
    • 2342569618 scopus 로고    scopus 로고
    • Conformational constraints for amyloid fibrillation: the importance of being unfolded
    • Uversky V.N., and Fink A.L. Conformational constraints for amyloid fibrillation: the importance of being unfolded. Biochim. Biophys. Acta 1698 (2004) 131-153
    • (2004) Biochim. Biophys. Acta , vol.1698 , pp. 131-153
    • Uversky, V.N.1    Fink, A.L.2
  • 12
    • 33947723675 scopus 로고    scopus 로고
    • Assessment of temperature effects on beta-aggregation of native and glycated albumin by FTIR spectroscopy and PAGE: relations between structural changes and antioxidant properties
    • Rondeau P., Armenta S., Caillens H., Chesne S., and Bourdon E. Assessment of temperature effects on beta-aggregation of native and glycated albumin by FTIR spectroscopy and PAGE: relations between structural changes and antioxidant properties. Arch. Biochem. Biophys. 460 (2007) 141-150
    • (2007) Arch. Biochem. Biophys. , vol.460 , pp. 141-150
    • Rondeau, P.1    Armenta, S.2    Caillens, H.3    Chesne, S.4    Bourdon, E.5
  • 13
    • 0028227096 scopus 로고
    • Structure of serum albumin
    • Carter D.C., and Ho J.X. Structure of serum albumin. Adv. Protein Chem. 45 (1994) 153-203
    • (1994) Adv. Protein Chem. , vol.45 , pp. 153-203
    • Carter, D.C.1    Ho, J.X.2
  • 14
    • 0024286990 scopus 로고
    • Albumin: an important extracellular antioxidant?
    • Halliwell B. Albumin: an important extracellular antioxidant?. Biochem. Pharmacol. 37 (1988) 569-571
    • (1988) Biochem. Pharmacol. , vol.37 , pp. 569-571
    • Halliwell, B.1
  • 18
    • 38949158548 scopus 로고    scopus 로고
    • Impairment of the antioxidant properties of serum albumin in patients with diabetes: protective effects of metformin
    • Faure P., Wiernsperger N., Polge C., Favier A., and Halimi S. Impairment of the antioxidant properties of serum albumin in patients with diabetes: protective effects of metformin. Clin. Sci. (London) 114 (2008) 251-256
    • (2008) Clin. Sci. (London) , vol.114 , pp. 251-256
    • Faure, P.1    Wiernsperger, N.2    Polge, C.3    Favier, A.4    Halimi, S.5
  • 19
    • 55049111770 scopus 로고    scopus 로고
    • Oxidative stresses induced by glycated human or bovine serum albumins on human monocytes
    • Rondeau P., Singh N., Caillens H., and Bourdon E. Oxidative stresses induced by glycated human or bovine serum albumins on human monocytes. Free Radic. Biol. Med. 45 (2008) 799-812
    • (2008) Free Radic. Biol. Med. , vol.45 , pp. 799-812
    • Rondeau, P.1    Singh, N.2    Caillens, H.3    Bourdon, E.4
  • 20
    • 34748925901 scopus 로고    scopus 로고
    • Identification of preferential protein targets for carbonylation in human mature adipocytes treated with native or glycated albumin
    • Singh N.R., Rondeau P., Hoareau L., and Bourdon E. Identification of preferential protein targets for carbonylation in human mature adipocytes treated with native or glycated albumin. Free Radic. Res. 41 (2007) 1078-1088
    • (2007) Free Radic. Res. , vol.41 , pp. 1078-1088
    • Singh, N.R.1    Rondeau, P.2    Hoareau, L.3    Bourdon, E.4
  • 21
    • 0019475899 scopus 로고
    • Nonenzymatic browning in vivo: possible process for aging of long-lived proteins
    • Monnier V.M., and Cerami A. Nonenzymatic browning in vivo: possible process for aging of long-lived proteins. Science 211 (1981) 491-493
    • (1981) Science , vol.211 , pp. 491-493
    • Monnier, V.M.1    Cerami, A.2
  • 22
    • 33749608762 scopus 로고    scopus 로고
    • Beta-lactoglobulin-dextran Maillard conjugates: their effect on interfacial thickness and emulsion stability
    • Wooster T.J., and Augustin M.A. Beta-lactoglobulin-dextran Maillard conjugates: their effect on interfacial thickness and emulsion stability. J. Colloid Interface Sci. 303 (2006) 564-572
    • (2006) J. Colloid Interface Sci. , vol.303 , pp. 564-572
    • Wooster, T.J.1    Augustin, M.A.2
  • 23
    • 22444432021 scopus 로고    scopus 로고
    • Historical perspective of the Maillard reaction in food science
    • Finot P.A. Historical perspective of the Maillard reaction in food science. Ann. N.Y. Acad. Sci. 1043 (2005) 1-8
    • (2005) Ann. N.Y. Acad. Sci. , vol.1043 , pp. 1-8
    • Finot, P.A.1
  • 24
    • 33749366840 scopus 로고    scopus 로고
    • Impact of Maillard type glycation on properties of beta-lactoglobulin
    • Chobert J.M., Gaudin J.C., Dalgalarrondo M., and Haertle T. Impact of Maillard type glycation on properties of beta-lactoglobulin. Biotechnol. Adv. 24 (2006) 629-632
    • (2006) Biotechnol. Adv. , vol.24 , pp. 629-632
    • Chobert, J.M.1    Gaudin, J.C.2    Dalgalarrondo, M.3    Haertle, T.4
  • 26
    • 0035135246 scopus 로고    scopus 로고
    • Advanced glycation end products: a review
    • Singh R., Barden A., Mori T., and Beilin L. Advanced glycation end products: a review. Diabetologia 44 (2001) 129-146
    • (2001) Diabetologia , vol.44 , pp. 129-146
    • Singh, R.1    Barden, A.2    Mori, T.3    Beilin, L.4
  • 27
    • 33746920337 scopus 로고    scopus 로고
    • Advanced glycation end products: sparking the development of diabetic vascular injury
    • Goldin A., Beckman J.A., Schimdt A.M., and Creager M.A. Advanced glycation end products: sparking the development of diabetic vascular injury. Circulation 114 (2006) 597-605
    • (2006) Circulation , vol.114 , pp. 597-605
    • Goldin, A.1    Beckman, J.A.2    Schimdt, A.M.3    Creager, M.A.4
  • 28
    • 60749136757 scopus 로고    scopus 로고
    • The interaction of metal ions with Maillard reaction products in a lactose-glycine model system
    • Ramonaityté D.T., Karšiené M., Adams A., Tehrani K.A., and De Kimpe N. The interaction of metal ions with Maillard reaction products in a lactose-glycine model system. Foos Res. Int. 42 (2009) 331-336
    • (2009) Foos Res. Int. , vol.42 , pp. 331-336
    • Ramonaityté, D.T.1    Karšiené, M.2    Adams, A.3    Tehrani, K.A.4    De Kimpe, N.5
  • 29
    • 40949155274 scopus 로고    scopus 로고
    • Propagation of protein glycation damage involves modification of tryptophan residues via reactive oxygen species: inhibition by pyridoxamine
    • Chetyrkin S.V., Mathis M.E., Ham A.L., Hachey D.L., Hudson B.G., and Voziyan P.A. Propagation of protein glycation damage involves modification of tryptophan residues via reactive oxygen species: inhibition by pyridoxamine. Free Radic. Biol. Med. 44 (2008) 1276-1285
    • (2008) Free Radic. Biol. Med. , vol.44 , pp. 1276-1285
    • Chetyrkin, S.V.1    Mathis, M.E.2    Ham, A.L.3    Hachey, D.L.4    Hudson, B.G.5    Voziyan, P.A.6
  • 30
    • 33750614168 scopus 로고    scopus 로고
    • Effects of oxidative modifications induced by the glycation of bovine serum albumin on its structure and on cultured adipose cells
    • Chesne S., Rondeau P., Armenta S., and Bourdon E. Effects of oxidative modifications induced by the glycation of bovine serum albumin on its structure and on cultured adipose cells. Biochimie 88 10 (2006) 1467-1477
    • (2006) Biochimie , vol.88 , Issue.10 , pp. 1467-1477
    • Chesne, S.1    Rondeau, P.2    Armenta, S.3    Bourdon, E.4
  • 31
    • 11144317965 scopus 로고    scopus 로고
    • Thermal induced conformational changes involved in the aggregation pathways of beta-lactoglobulin
    • Vetri V., and Militello V. Thermal induced conformational changes involved in the aggregation pathways of beta-lactoglobulin. Biophys. Chem. 113 (2005) 83-91
    • (2005) Biophys. Chem. , vol.113 , pp. 83-91
    • Vetri, V.1    Militello, V.2
  • 32
    • 0022691315 scopus 로고
    • Examination of the secondary structure of proteins by deconvolved FTIR spectra
    • Byler D.M., and Susi H. Examination of the secondary structure of proteins by deconvolved FTIR spectra. Biopolymers 25 (1986) 469-487
    • (1986) Biopolymers , vol.25 , pp. 469-487
    • Byler, D.M.1    Susi, H.2
  • 33
    • 0033584169 scopus 로고    scopus 로고
    • Identification of beta-turn and random coil amide III infrared bands for secondary structure estimation of proteins
    • Cai S., and Singh B.R. Identification of beta-turn and random coil amide III infrared bands for secondary structure estimation of proteins. Biophys. Chem. 80 (1999) 7-20
    • (1999) Biophys. Chem. , vol.80 , pp. 7-20
    • Cai, S.1    Singh, B.R.2
  • 34
    • 0025357111 scopus 로고
    • Protein secondary structures in water from second-derivative amide I infrared spectra
    • Dong A., Huang P., and Caughey W.S. Protein secondary structures in water from second-derivative amide I infrared spectra. Biochemistry 29 (1990) 3303-3308
    • (1990) Biochemistry , vol.29 , pp. 3303-3308
    • Dong, A.1    Huang, P.2    Caughey, W.S.3
  • 35
    • 0034650323 scopus 로고    scopus 로고
    • Spectroscopic methods for analysis of protein secondary structure
    • Pelton J.T., and McLean L.R. Spectroscopic methods for analysis of protein secondary structure. Anal. Biochem. 277 (2000) 167-176
    • (2000) Anal. Biochem. , vol.277 , pp. 167-176
    • Pelton, J.T.1    McLean, L.R.2
  • 36
    • 0031574012 scopus 로고    scopus 로고
    • Conformation of beta-lactoglobulin studied by FTIR: effect of pH, temperature, and adsorption to the oil-water interface
    • Fang Y., and Dalgleish D.G. Conformation of beta-lactoglobulin studied by FTIR: effect of pH, temperature, and adsorption to the oil-water interface. J. Colloid Interface Sci. 196 (1997) 292-298
    • (1997) J. Colloid Interface Sci. , vol.196 , pp. 292-298
    • Fang, Y.1    Dalgleish, D.G.2
  • 37
    • 0038172338 scopus 로고    scopus 로고
    • Formation of intermolecular beta-sheet structures: a phenomenon relevant to protein film structure at oil-water interfaces of emulsions
    • Lefevre T., and Subirade M. Formation of intermolecular beta-sheet structures: a phenomenon relevant to protein film structure at oil-water interfaces of emulsions. J. Colloid Interface Sci. 263 (2003) 59-67
    • (2003) J. Colloid Interface Sci. , vol.263 , pp. 59-67
    • Lefevre, T.1    Subirade, M.2
  • 38
    • 0030993642 scopus 로고    scopus 로고
    • Effect of temperature on the secondary structure of beta-lactoglobulin at pH 6.7, as determined by CD and IR spectroscopy: a test of the molten globule hypothesis
    • Qi X.L., Holt C., McNulty D., Clarke D.T., Brownlow S., and Jones G.R. Effect of temperature on the secondary structure of beta-lactoglobulin at pH 6.7, as determined by CD and IR spectroscopy: a test of the molten globule hypothesis. Biochem. J. 324-Pt 1 (1997) 341-346
    • (1997) Biochem. J. , vol.324 -PART 1 , pp. 341-346
    • Qi, X.L.1    Holt, C.2    McNulty, D.3    Clarke, D.T.4    Brownlow, S.5    Jones, G.R.6
  • 39
    • 35748948052 scopus 로고    scopus 로고
    • Thermal aggregation of beta-lactoglobulin in presence of metal ions
    • Navarra G., Leone M., and Militello V. Thermal aggregation of beta-lactoglobulin in presence of metal ions. Biophys. Chem. 131 (2007) 52-61
    • (2007) Biophys. Chem. , vol.131 , pp. 52-61
    • Navarra, G.1    Leone, M.2    Militello, V.3
  • 42
    • 77149166345 scopus 로고
    • Patent Application No. 5,135,850 () Washington DC, USA
    • M. Prost Patent Application No. 5,135,850 (1992) Washington DC, USA.
    • (1992)
    • Prost, M.1
  • 43
    • 0030858674 scopus 로고    scopus 로고
    • Effect of a two-year supplementation with low doses of antioxidant vitamins and/or minerals in elderly subjects on levels of nutrients and antioxidant defense parameters
    • Girodon F., Blache D., Monget A.L., Lombart M., Brunet-Lecompte P., Arnaud J., Richard M.J., and Galan P. Effect of a two-year supplementation with low doses of antioxidant vitamins and/or minerals in elderly subjects on levels of nutrients and antioxidant defense parameters. J. Am. Coll. Nutr. 16 (1997) 357-365
    • (1997) J. Am. Coll. Nutr. , vol.16 , pp. 357-365
    • Girodon, F.1    Blache, D.2    Monget, A.L.3    Lombart, M.4    Brunet-Lecompte, P.5    Arnaud, J.6    Richard, M.J.7    Galan, P.8
  • 44
    • 0029928812 scopus 로고    scopus 로고
    • The pyridoindole antioxidant stobadine inhibited glycation-induced absorbance and fluorescence changes in albumin
    • Stefek M., Drozdikova I., and Vajdova K. The pyridoindole antioxidant stobadine inhibited glycation-induced absorbance and fluorescence changes in albumin. Acta Diabetol. 33 (1996) 35-40
    • (1996) Acta Diabetol. , vol.33 , pp. 35-40
    • Stefek, M.1    Drozdikova, I.2    Vajdova, K.3
  • 46
    • 0032966525 scopus 로고    scopus 로고
    • Glucose and free radicals impair the antioxidant properties of serum albumin
    • Bourdon E., Loreau N., and Blache D. Glucose and free radicals impair the antioxidant properties of serum albumin. FASEB J. 13 (1999) 233-244
    • (1999) FASEB J. , vol.13 , pp. 233-244
    • Bourdon, E.1    Loreau, N.2    Blache, D.3
  • 48
    • 63249093042 scopus 로고    scopus 로고
    • Rapid glycation with D-ribose induces globular amyloid-like aggregations of BSA with high cytotoxicity to SH-SY5Y cells
    • Wei Y., Chen L., Chen J., Ge L., and He R. Rapid glycation with D-ribose induces globular amyloid-like aggregations of BSA with high cytotoxicity to SH-SY5Y cells. BMC Cell Biol. 10 (2009) 10
    • (2009) BMC Cell Biol. , vol.10 , pp. 10
    • Wei, Y.1    Chen, L.2    Chen, J.3    Ge, L.4    He, R.5
  • 49
    • 0029924912 scopus 로고    scopus 로고
    • Fluorescence behaviour of tryptophan residues of bovine and human serum albumins in ionic surfactant solutions: a comparative study of the two and one tryptophan(s) of bovine and human albumins
    • Moriyama Y., Ohta D., Hachiya K., Mitsui Y., and Takeda K. Fluorescence behaviour of tryptophan residues of bovine and human serum albumins in ionic surfactant solutions: a comparative study of the two and one tryptophan(s) of bovine and human albumins. J. Protein Chem. 15 (1996) 265-272
    • (1996) J. Protein Chem. , vol.15 , pp. 265-272
    • Moriyama, Y.1    Ohta, D.2    Hachiya, K.3    Mitsui, Y.4    Takeda, K.5
  • 50
    • 0025929570 scopus 로고
    • Fluorescence techniques for studying protein structure
    • Eftink M.R. Fluorescence techniques for studying protein structure. Methods Biochem. Anal. 35 (1991) 127-205
    • (1991) Methods Biochem. Anal. , vol.35 , pp. 127-205
    • Eftink, M.R.1
  • 51
    • 0034518920 scopus 로고    scopus 로고
    • Native fluorescence and mag-indo-1-protein interaction as tools for probing unfolding and refolding sequences of the bovine serum albumin subdomain in the presence of guanidine hydrochloride
    • Viallet P.M., Vo-Dinh T., Ribou A.C., Vigo J., and Salmon J.M. Native fluorescence and mag-indo-1-protein interaction as tools for probing unfolding and refolding sequences of the bovine serum albumin subdomain in the presence of guanidine hydrochloride. J. Protein Chem. 19 (2000) 431-439
    • (2000) J. Protein Chem. , vol.19 , pp. 431-439
    • Viallet, P.M.1    Vo-Dinh, T.2    Ribou, A.C.3    Vigo, J.4    Salmon, J.M.5
  • 52
    • 24644500617 scopus 로고    scopus 로고
    • Main-chain dominated amyloid structures demonstrated by the effect of high pressure
    • Chatani E., Kato M., Kawai T., Naiki H., and Goto Y. Main-chain dominated amyloid structures demonstrated by the effect of high pressure. J. Mol. Biol. 352 (2005) 941-951
    • (2005) J. Mol. Biol. , vol.352 , pp. 941-951
    • Chatani, E.1    Kato, M.2    Kawai, T.3    Naiki, H.4    Goto, Y.5
  • 53
    • 0035922871 scopus 로고    scopus 로고
    • Mechanism of bovine serum albumin aggregation during ultrafiltration
    • Maruyama T., Katoh S., Nakajima M., and Nabetani H. Mechanism of bovine serum albumin aggregation during ultrafiltration. Biotechnol. Bioeng. 75 (2001) 233-238
    • (2001) Biotechnol. Bioeng. , vol.75 , pp. 233-238
    • Maruyama, T.1    Katoh, S.2    Nakajima, M.3    Nabetani, H.4
  • 54
    • 0032528558 scopus 로고    scopus 로고
    • Intermolecular beta-sheet results from trifluoroethanol-induced nonnative alpha-helical structure in beta-sheet predominant proteins: infrared and circular dichroism spectroscopic study
    • Dong A., Matsuura J., Manning M.C., and Carpenter J.F. Intermolecular beta-sheet results from trifluoroethanol-induced nonnative alpha-helical structure in beta-sheet predominant proteins: infrared and circular dichroism spectroscopic study. Arch. Biochem. Biophys. 355 (1998) 275-281
    • (1998) Arch. Biochem. Biophys. , vol.355 , pp. 275-281
    • Dong, A.1    Matsuura, J.2    Manning, M.C.3    Carpenter, J.F.4
  • 55
    • 70350571211 scopus 로고    scopus 로고
    • Influence of metal ions on thermal aggregation of bovine serum albumin: aggregation kinetics and structural changes
    • Navarra G., Tinti A., Leone M., Militello V., and Torreggiani A. Influence of metal ions on thermal aggregation of bovine serum albumin: aggregation kinetics and structural changes. J. Inorg. Biochem. 103 (2009) 1729-1738
    • (2009) J. Inorg. Biochem. , vol.103 , pp. 1729-1738
    • Navarra, G.1    Tinti, A.2    Leone, M.3    Militello, V.4    Torreggiani, A.5
  • 56
    • 0037093336 scopus 로고    scopus 로고
    • Assay of advanced glycation endproducts (AGEs): surveying AGEs by chromatographic assay with derivatization by 6-aminoquinolyl-N-hydroxysuccinimidyl-carbamate and application to Nepsilon-carboxymethyl-lysine- and Nepsilon-(1-carboxyethyl)lysine-modified albumin
    • Ahmed N., Argirov O.K., Minhas H.S., Cordeiro C.A., and Thornalley P.J. Assay of advanced glycation endproducts (AGEs): surveying AGEs by chromatographic assay with derivatization by 6-aminoquinolyl-N-hydroxysuccinimidyl-carbamate and application to Nepsilon-carboxymethyl-lysine- and Nepsilon-(1-carboxyethyl)lysine-modified albumin. Biochem. J. 364 (2002) 1-14
    • (2002) Biochem. J. , vol.364 , pp. 1-14
    • Ahmed, N.1    Argirov, O.K.2    Minhas, H.S.3    Cordeiro, C.A.4    Thornalley, P.J.5
  • 57
    • 0037376556 scopus 로고    scopus 로고
    • AGE-breakers cleave model compounds, but do not break Maillard crosslinks in skin and tail collagen from diabetic rats
    • Yang S., Litchfield J.E., and Baynes J.W. AGE-breakers cleave model compounds, but do not break Maillard crosslinks in skin and tail collagen from diabetic rats. Arch. Biochem. Biophys. 412 (2003) 42-46
    • (2003) Arch. Biochem. Biophys. , vol.412 , pp. 42-46
    • Yang, S.1    Litchfield, J.E.2    Baynes, J.W.3
  • 58
    • 0032913309 scopus 로고    scopus 로고
    • Role of oxidative stress in diabetic complications: a new perspective on an old paradigm
    • Baynes J.W., and Thorpe S.R. Role of oxidative stress in diabetic complications: a new perspective on an old paradigm. Diabetes 48 (1999) 1-9
    • (1999) Diabetes , vol.48 , pp. 1-9
    • Baynes, J.W.1    Thorpe, S.R.2
  • 59
    • 61849159854 scopus 로고    scopus 로고
    • A perspective on the Maillard reaction and the analysis of protein glycation by mass spectrometry: probing the pathogenesis of chronic disease
    • Zhang Q., Ames J.M., Smith R.D., Baynes J.W., and Metz T.O. A perspective on the Maillard reaction and the analysis of protein glycation by mass spectrometry: probing the pathogenesis of chronic disease. J. Proteome Res. 8 (2009) 754-769
    • (2009) J. Proteome Res. , vol.8 , pp. 754-769
    • Zhang, Q.1    Ames, J.M.2    Smith, R.D.3    Baynes, J.W.4    Metz, T.O.5
  • 60
    • 31044442243 scopus 로고    scopus 로고
    • Methylglyoxal comes of AGE
    • Ramasamy R., Yan S.F., and Schmidt A.M. Methylglyoxal comes of AGE. Cell 124 (2006) 258-260
    • (2006) Cell , vol.124 , pp. 258-260
    • Ramasamy, R.1    Yan, S.F.2    Schmidt, A.M.3
  • 62
    • 0018395653 scopus 로고
    • Nonenzymatically glucosylated albumin. In vitro preparation and isolation from normal human serum
    • Day J.F., Thorpe S.R., and Baynes J.W. Nonenzymatically glucosylated albumin. In vitro preparation and isolation from normal human serum. J. Biol. Chem. 254 (1979) 595-597
    • (1979) J. Biol. Chem. , vol.254 , pp. 595-597
    • Day, J.F.1    Thorpe, S.R.2    Baynes, J.W.3
  • 64
    • 0346731073 scopus 로고    scopus 로고
    • Maillard reaction products in tissue proteins: new products and new perspectives
    • Thorpe S.R., and Baynes J.W. Maillard reaction products in tissue proteins: new products and new perspectives. Amino Acids 25 (2003) 275-281
    • (2003) Amino Acids , vol.25 , pp. 275-281
    • Thorpe, S.R.1    Baynes, J.W.2
  • 65
    • 23844502010 scopus 로고    scopus 로고
    • Evidence for the formation of adducts and S-(carboxymethyl)cysteine on reaction of alpha-dicarbonyl compounds with thiol groups on amino acids, peptides, and proteins
    • Zeng J., and Davies M.J. Evidence for the formation of adducts and S-(carboxymethyl)cysteine on reaction of alpha-dicarbonyl compounds with thiol groups on amino acids, peptides, and proteins. Chem. Res. Toxicol. 18 (2005) 1232-1241
    • (2005) Chem. Res. Toxicol. , vol.18 , pp. 1232-1241
    • Zeng, J.1    Davies, M.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.