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Volumn , Issue , 2011, Pages 91-113

Protein photo-oxidative damage - consequences, characterisation and control

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EID: 84892023760     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter
Times cited : (3)

References (134)
  • 1
    • 0001773162 scopus 로고    scopus 로고
    • Molecular and cellular effects of UV radiation relevant to chronic photodamage
    • In: Gilchrest, BA, editor.
    • Kochevar, IE. Molecular and cellular effects of UV radiation relevant to chronic photodamage. In: Gilchrest, BA, editor. Photodamage, 1999, 51-67.
    • (1999) Photodamage , pp. 51-67
    • Kochevar, I.E.1
  • 2
    • 0141628349 scopus 로고    scopus 로고
    • Chemical and photo-oxidative hair damage studied by dye diffusion and electrophoresis
    • Ruetsch, SB; Yang, B; Kamath, YK. Chemical and photo-oxidative hair damage studied by dye diffusion and electrophoresis. Journal of Cosmetic Science, 2003, 54, 379-94.
    • (2003) Journal of Cosmetic Science , vol.54 , pp. 379-394
    • Ruetsch, S.B.1    Yang, B.2    Kamath, Y.K.3
  • 3
    • 3142718195 scopus 로고    scopus 로고
    • 3-hydroxypyridine chromophores are endogenous sensitizers of photo-oxidative stress in human skin cells
    • Wondrak, GT; Roberts, MJ; Jacobson, MK, et al. 3-hydroxypyridine chromophores are endogenous sensitizers of photo-oxidative stress in human skin cells. Journal of Biological Chemistry, 2004, 279, 30009-20.
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 30009-30020
    • Wondrak, G.T.1    Roberts, M.J.2    Jacobson, M.K.3
  • 5
    • 12444296480 scopus 로고    scopus 로고
    • Proteins as biomarkers of oxidative/nitrosative stress in diseases: The contribution of redox proteomics
    • Dalle-Donne, I; Scaloni, A; Giustarini, D; et al. Proteins as biomarkers of oxidative/nitrosative stress in diseases: The contribution of redox proteomics. Mass Spectrometry Reviews, 2005, 24, 55-99.
    • (2005) Mass Spectrometry Reviews , vol.24 , pp. 55-99
    • Dalle-Donne, I.1    Scaloni, A.2    Giustarini, D.3
  • 6
    • 84903923436 scopus 로고    scopus 로고
    • Sensory and quality properties of packaged meat
    • In: JP; Kerry, D; Ledward, editors., Cambridge: Woodhead Publishing Limited
    • O'Sullivan, MG; Kerry, JP. Sensory and quality properties of packaged meat. In: JP; Kerry, D; Ledward, editors. Improving the Sensory and Nutritional Quality of Fresh Meat. Cambridge: Woodhead Publishing Limited; 2009, 595-7.
    • (2009) Improving the Sensory and Nutritional Quality of Fresh Meat. , pp. 595-597
    • O'Sullivan, M.G.1    Kerry, J.P.2
  • 7
    • 42449113793 scopus 로고    scopus 로고
    • Protection against photo-oxidation of milk by high urate content
    • Østdal, H; Weisbjerg, MR; Skibsted, LH; et al. Protection against photo-oxidation of milk by high urate content. Milchwissenschaft, 2008, 63, 119-22.
    • (2008) Milchwissenschaft , vol.63 , pp. 119-122
    • Østdal, H.1    Weisbjerg, M.R.2    Skibsted, L.H.3
  • 8
    • 0032985811 scopus 로고    scopus 로고
    • Protection against UVB inactivation (in vitro) of rat lens enzymes by natural antioxidants
    • Reddy, GB; Bhat, KS. Protection against UVB inactivation (in vitro) of rat lens enzymes by natural antioxidants. Molecular and Cellular Biochemistry, 1999, 194, 41-5.
    • (1999) Molecular and Cellular Biochemistry , vol.194 , pp. 41-45
    • Reddy, G.B.1    Bhat, K.S.2
  • 9
    • 0037492957 scopus 로고    scopus 로고
    • Molecular dynamics study of early events during photo-oxidation of eye lens protein ?ß-crystallin
    • Kubiak, K; Kowalska, M; Nowak, W. Molecular dynamics study of early events during photo-oxidation of eye lens protein ?ß-crystallin. Journal of Molecular Structure (Theochem), 2003, 630, 315-25.
    • (2003) Journal of Molecular Structure (Theochem) , vol.630 , pp. 315-325
    • Kubiak, K.1    Kowalska, M.2    Nowak, W.3
  • 10
    • 16644388652 scopus 로고    scopus 로고
    • The damaging effect of UV-C irradiation on lens alpha-crystallin
    • Fujii, N; Uchida, H; Saito, T. The damaging effect of UV-C irradiation on lens alpha-crystallin. Molecular Vision, 2004, 10, 814-20.
    • (2004) Molecular Vision , vol.10 , pp. 814-820
    • Fujii, N.1    Uchida, H.2    Saito, T.3
  • 11
    • 0000394046 scopus 로고
    • Ultraviolet radiation and plants: Burning questions
    • Stapleton, AE. Ultraviolet radiation and plants: Burning questions. Plant Cell, 1992, 4, 1353-8.
    • (1992) Plant Cell , vol.4 , pp. 1353-1358
    • Stapleton, A.E.1
  • 12
    • 0000019999 scopus 로고
    • Ultraviolet-induced photodegradation of cucumber (Cucumis sativus L.) microsomal and soluble protein tryptophanyl residues in vitro
    • Caldwell, CR. Ultraviolet-induced photodegradation of cucumber (Cucumis sativus L.) microsomal and soluble protein tryptophanyl residues in vitro. Plant Physiology, 1993, 101, 947-53.
    • (1993) Plant Physiology , vol.101 , pp. 947-953
    • Caldwell, C.R.1
  • 13
    • 0001835116 scopus 로고    scopus 로고
    • Tryptophan photolysis leads to a UVB-induced 66 kDa photoproduct of ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) in vitro and in vivo
    • Gerhardt, KE; Wilson, MI; Greenberg, BM. Tryptophan photolysis leads to a UVB-induced 66 kDa photoproduct of ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) in vitro and in vivo. Photochemistry and Photobiology, 1999, 70, 49-56.
    • (1999) Photochemistry and Photobiology , vol.70 , pp. 49-56
    • Gerhardt, K.E.1    Wilson, M.I.2    Greenberg, B.M.3
  • 14
    • 0023992403 scopus 로고
    • Possible long-term changes in biologically active ultraviolet radiation reaching the ground
    • Frederick, JE; Lubin, D. Possible long-term changes in biologically active ultraviolet radiation reaching the ground. Photochemistry and Photobiology, 1988, 47, 571-8.
    • (1988) Photochemistry and Photobiology , vol.47 , pp. 571-578
    • Frederick, J.E.1    Lubin, D.2
  • 15
    • 84989674897 scopus 로고
    • The photophysics and photochemistry of the near-UV absorbing amino acids -II. Tyrosine and its simple derivatives
    • Creed, D. The photophysics and photochemistry of the near-UV absorbing amino acids -II. Tyrosine and its simple derivatives. Photochemistry and Photobiology, 1984, 39, 563-75.
    • (1984) Photochemistry and Photobiology , vol.39 , pp. 563-575
    • Creed, D.1
  • 16
    • 84989712905 scopus 로고
    • The photophysics and photochemistry of the near-UV absorbing amino acids-I. Tryptophan and its simple derivatives
    • Creed, D. The photophysics and photochemistry of the near-UV absorbing amino acids-I. Tryptophan and its simple derivatives. Photochemistry and Photobiology 1984, 39, 537-62.
    • (1984) Photochemistry and Photobiology , vol.39 , pp. 537-562
    • Creed, D.1
  • 17
    • 77953613724 scopus 로고    scopus 로고
    • Lipid and protein damage provoked by ultraviolet radiation: Mechanisms of indirect photo-oxidative damage
    • In: Giacomoni, PU, editor., Cambridge, UK: RSC Publishing
    • Girotti, AW; Giacomoni, PU. Lipid and protein damage provoked by ultraviolet radiation: Mechanisms of indirect photo-oxidative damage. In: Giacomoni, PU, editor. Biophysical and Physiological Effects of Solar Radiation on Human Skin. Cambridge, UK: RSC Publishing; 2007, 271-91.
    • (2007) Biophysical and Physiological Effects of Solar Radiation on Human Skin. , pp. 271-291
    • Girotti, A.W.1    Giacomoni, P.U.2
  • 18
    • 39949085602 scopus 로고    scopus 로고
    • Tryptophan-derived ultraviolet filter compounds covalently bound to lens proteins are photosensitizers of oxidative damage
    • Mizdrak, J; Hains, PG; Truscott, RJW, et al. Tryptophan-derived ultraviolet filter compounds covalently bound to lens proteins are photosensitizers of oxidative damage. Free Radical Biology and Medicine, 2008, 44, 1108-19.
    • (2008) Free Radical Biology and Medicine , vol.44 , pp. 1108-1119
    • Mizdrak, J.1    Hains, P.G.2    Truscott, R.J.W.3
  • 19
    • 3042688696 scopus 로고    scopus 로고
    • Reactive species formed on proteins exposed to singlet oxygen
    • Davies, MJ. Reactive species formed on proteins exposed to singlet oxygen. Photochemical and Photobiological Sciences, 2004, 3, 17-25.
    • (2004) Photochemical and Photobiological Sciences , vol.3 , pp. 17-25
    • Davies, M.J.1
  • 21
  • 24
    • 0035857421 scopus 로고    scopus 로고
    • Sites of hydroxyl radical reaction with amino acids identified by 2H NMR detection of induced 1H/2H exchange
    • Nukuna, BN; Goshe, MB; Anderson, VE. Sites of hydroxyl radical reaction with amino acids identified by 2H NMR detection of induced 1H/2H exchange. Journal of the American Chemical Society, 2001, 123, 1208-14.
    • (2001) Journal of the American Chemical Society , vol.123 , pp. 1208-1214
    • Nukuna, B.N.1    Goshe, M.B.2    Anderson, V.E.3
  • 25
    • 70350493279 scopus 로고    scopus 로고
    • Photoproducts formed in the photoyellowing of collagen in the presence of a fluorescent whitening agent
    • In Press.
    • Dyer, J; Clerens, S; Cornellison, C, et al. Photoproducts formed in the photoyellowing of collagen in the presence of a fluorescent whitening agent. Photochemistry and Photobiology, 2009, In Press.
    • (2009) Photochemistry and Photobiology
    • Dyer, J.1    Clerens, S.2    Cornellison, C.3
  • 26
    • 3142654685 scopus 로고    scopus 로고
    • Peroxynitrite reaction with eye lens proteins: a-crystallin retains its activity despite modification
    • Thiagarajan, G; Lakshmanan, J; Chalasani, M, et al. Peroxynitrite reaction with eye lens proteins: a-crystallin retains its activity despite modification. Investigative Ophthalmology and Visual Science, 2004, 45, 2115-21.
    • (2004) Investigative Ophthalmology and Visual Science , vol.45 , pp. 2115-2121
    • Thiagarajan, G.1    Lakshmanan, J.2    Chalasani, M.3
  • 27
    • 31544462306 scopus 로고    scopus 로고
    • Modification of tryptophan and tryptophan residues in proteins by reactive nitrogen species
    • Yamakura, F; Ikeda, K. Modification of tryptophan and tryptophan residues in proteins by reactive nitrogen species. Nitric Oxide Biology and Chemistry, 2006, 14, 152-61.
    • (2006) Nitric Oxide Biology and Chemistry , vol.14 , pp. 152-161
    • Yamakura, F.1    Ikeda, K.2
  • 29
  • 30
    • 84889453656 scopus 로고    scopus 로고
    • Chemical modification of proteins by reactive oxygen species
    • In: I; Dalle-Donne, A; Scaloni, DA, Butterfield, editors., Hoboken: John Wiley and Sons, Inc.
    • Stadtman, ER; Levine, RL. Chemical modification of proteins by reactive oxygen species. In: I; Dalle-Donne, A; Scaloni, DA, Butterfield, editors. Redox Proteomics - From Protein Modifications to Cellular Dysfunctions and Diseases. Hoboken: John Wiley and Sons, Inc.; 2006, 3-23.
    • (2006) Redox Proteomics - From Protein Modifications to Cellular Dysfunctions and Diseases. , pp. 3-23
    • Stadtman, E.R.1    Levine, R.L.2
  • 31
    • 0034676088 scopus 로고    scopus 로고
    • Post-translational hydroxylation at the N-terminus of the prion protein reveals presence of PPII structure in vivo
    • Gill, AC; Ritchie, MA; Hunt, LG, et al. Post-translational hydroxylation at the N-terminus of the prion protein reveals presence of PPII structure in vivo. EMBO Journal, 2000, 19, 5324-31.
    • (2000) EMBO Journal , vol.19 , pp. 5324-5331
    • Gill, A.C.1    Ritchie, M.A.2    Hunt, L.G.3
  • 32
    • 0003828324 scopus 로고
    • Chemistry and biochemistry of the amino acids
    • London: Chapman & Hall
    • Bender, DA; Barrett, GC. Chemistry and biochemistry of the amino acids. London: Chapman & Hall; 1985.
    • (1985)
    • Bender, D.A.1    Barrett, G.C.2
  • 33
    • 0005227479 scopus 로고    scopus 로고
    • Identification of the sites of hydroxyl radical reaction with peptides by hydrogen/deuterium exchange: prevalence of reactions with the side chains
    • Goshe, MB; Chen, YH; Anderson, VE. Identification of the sites of hydroxyl radical reaction with peptides by hydrogen/deuterium exchange: prevalence of reactions with the side chains. Biochemistry, 2000, 39, 1761-70.
    • (2000) Biochemistry , vol.39 , pp. 1761-1770
    • Goshe, M.B.1    Chen, Y.H.2    Anderson, V.E.3
  • 34
    • 0030841350 scopus 로고    scopus 로고
    • Protein oxidation in aging, disease, and oxidative stress
    • Berlett, BS; Stadtman, ER. Protein oxidation in aging, disease, and oxidative stress. Journal of Biological Chemistry, 1997, 272, 20313-6.
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 20313-20316
    • Berlett, B.S.1    Stadtman, E.R.2
  • 36
    • 0006593626 scopus 로고
    • Effects of ultraviolet radiation as related to the yellowing of wool
    • Asquith, RS; Hirst, L; Rivett, DE. Effects of ultraviolet radiation as related to the yellowing of wool. Applied Polymer Symposium; 1971, 333-5.
    • (1971) Applied Polymer Symposium , pp. 333-335
    • Asquith, R.S.1    Hirst, L.2    Rivett, D.E.3
  • 37
    • 0014537639 scopus 로고
    • The photolysis of tyrosine and its possible relationship to the yellowing of wool
    • Asquith, RS; Rivett, DE. The photolysis of tyrosine and its possible relationship to the yellowing of wool. Textile Research Journal, 1969, 39, 633-7.
    • (1969) Textile Research Journal , vol.39 , pp. 633-637
    • Asquith, R.S.1    Rivett, D.E.2
  • 39
    • 48749112804 scopus 로고    scopus 로고
    • Indirect photodegradation of dissolved free amino acids: The contribution of singlet oxygen and the differential reactivity of DOM from various sources
    • Boreen, AL; Edhlund, BL; Cotner, JB, et al. Indirect photodegradation of dissolved free amino acids: The contribution of singlet oxygen and the differential reactivity of DOM from various sources. Environmental Science and Technology, 2008, 42, 5492-8.
    • (2008) Environmental Science and Technology , vol.42 , pp. 5492-5498
    • Boreen, A.L.1    Edhlund, B.L.2    Cotner, J.B.3
  • 40
    • 0030988742 scopus 로고    scopus 로고
    • Biochemistry and pathology of radical-mediated protein oxidation
    • Dean, RT; Fu, S; Stocker, R, et al. Biochemistry and pathology of radical-mediated protein oxidation. Biochemical Journal, 1997, 324, 1-18.
    • (1997) Biochemical Journal , vol.324 , pp. 1-18
    • Dean, R.T.1    Fu, S.2    Stocker, R.3
  • 41
    • 0033429334 scopus 로고    scopus 로고
    • Stable markers of oxidant damage to proteins and their application in the study of human disease
    • Davies, MJ; Fu, S; Wang, H, et al. Stable markers of oxidant damage to proteins and their application in the study of human disease. Free Radical Biology and Medicine, 1999, 27, 1151-63.
    • (1999) Free Radical Biology and Medicine , vol.27 , pp. 1151-1163
    • Davies, M.J.1    Fu, S.2    Wang, H.3
  • 43
    • 0000217491 scopus 로고    scopus 로고
    • Oxidation of free tryptophan and tryptophan residues in peptides and proteins
    • Simat, TJ; Steinhart, H. Oxidation of free tryptophan and tryptophan residues in peptides and proteins. Journal of Agricultural & Food Chemistry, 1998, 46, 490-8.
    • (1998) Journal of Agricultural & Food Chemistry , vol.46 , pp. 490-498
    • Simat, T.J.1    Steinhart, H.2
  • 45
    • 8644286364 scopus 로고    scopus 로고
    • o-Tyrosine hydroxylation by OH. radicals. 2, 3-DOPA and 2,5-DOPA formation in ?-irradiated aqueous solution
    • Zegota, H; Kolodziejczyk, K; Król, M, et al. o-Tyrosine hydroxylation by OH. radicals. 2, 3-DOPA and 2,5-DOPA formation in ?-irradiated aqueous solution. Radiation Physics and Chemistry, 2005, 72, 25-33.
    • (2005) Radiation Physics and Chemistry , vol.72 , pp. 25-33
    • Zegota, H.1    Kolodziejczyk, K.2    Król, M.3
  • 46
    • 33745728806 scopus 로고    scopus 로고
    • Characterisation of photo-oxidation products within photoyellowed wool proteins: tryptophan and tyrosine derived chromophores
    • Dyer, JM; Bringans, S; Bryson, WG. Characterisation of photo-oxidation products within photoyellowed wool proteins: tryptophan and tyrosine derived chromophores. Photochemical and Photobiological Sciences, 2006, 5, 698-706.
    • (2006) Photochemical and Photobiological Sciences , vol.5 , pp. 698-706
    • Dyer, J.M.1    Bringans, S.2    Bryson, W.G.3
  • 47
    • 33646235182 scopus 로고    scopus 로고
    • Determination of photo-oxidation products within photoyellowed bleached wool proteins
    • Dyer, JM; Bringans, SD; Bryson, WG. Determination of photo-oxidation products within photoyellowed bleached wool proteins. Photochemistry and Photobiology, 2006, 82, 551-7.
    • (2006) Photochemistry and Photobiology , vol.82 , pp. 551-557
    • Dyer, J.M.1    Bringans, S.D.2    Bryson, W.G.3
  • 48
    • 67650904556 scopus 로고    scopus 로고
    • Oxidation of bovine serum albumin: identification of oxidation products and structural modifications
    • Guedes, S; Vitorino, R; Domingues, Rr, et al. Oxidation of bovine serum albumin: identification of oxidation products and structural modifications. Rapid Communications in Mass Spectrometry, 2009, 23, 2307-15.
    • (2009) Rapid Communications in Mass Spectrometry , vol.23 , pp. 2307-2315
    • Guedes, S.1    Vitorino, R.2    Domingues, R.3
  • 49
    • 0026644326 scopus 로고
    • The hydroxylation of phenylalanine and tyrosine: A comparison with salicylate and tryptophan
    • Maskos, Z; Rush, JD; Koppenol, WH. The hydroxylation of phenylalanine and tyrosine: A comparison with salicylate and tryptophan. Archives of Biochemistry and Biophysics, 1992, 296, 521-9.
    • (1992) Archives of Biochemistry and Biophysics , vol.296 , pp. 521-529
    • Maskos, Z.1    Rush, J.D.2    Koppenol, W.H.3
  • 50
    • 34248340542 scopus 로고    scopus 로고
    • Luminescence and Raman spectroscopic studies on the damage of tryptophan, histidine and carnosine by singlet oxygen
    • Wei, C; Song, B; Yuan, J, et al. Luminescence and Raman spectroscopic studies on the damage of tryptophan, histidine and carnosine by singlet oxygen. Journal of Photochemistry and Photobiology A: Chemistry, 2007, 189, 39-45.
    • (2007) Journal of Photochemistry and Photobiology A: Chemistry , vol.189 , pp. 39-45
    • Wei, C.1    Song, B.2    Yuan, J.3
  • 51
    • 0001516275 scopus 로고
    • The ultraviolet fluorescence of proteins in neutral solution
    • Teale, WWJ. The ultraviolet fluorescence of proteins in neutral solution. Biochemical Journal, 1960, 76, 381-8.
    • (1960) Biochemical Journal , vol.76 , pp. 381-388
    • Teale, W.W.J.1
  • 52
    • 0017578095 scopus 로고
    • Electronic energy transfer between tyrosine and tryptophan in the peptides trp-(pro)n-Tyr
    • Chiu, HC; Bersohn, R. Electronic energy transfer between tyrosine and tryptophan in the peptides trp-(pro)n-Tyr. Biopolymers, 1977, 16, 277-88.
    • (1977) Biopolymers , vol.16 , pp. 277-288
    • Chiu, H.C.1    Bersohn, R.2
  • 53
    • 33746609431 scopus 로고
    • Origins of variation in the fluorescence patterns of wool and wool proteins
    • Proceedings of the 9th International Wool Textile Research Conference; 1995 1995; Biella, Italy
    • Simpson, WS. Origins of variation in the fluorescence patterns of wool and wool proteins. Proceedings of the 9th International Wool Textile Research Conference; 1995 1995; Biella, Italy, 1995, 429-39.
    • (1995) , pp. 429-439
    • Simpson, W.S.1
  • 55
    • 0034029857 scopus 로고    scopus 로고
    • A critical review of the structural mechanics of wool and hair fibres
    • Hearle, JW. A critical review of the structural mechanics of wool and hair fibres. International Journal of Biological Macromolecules, 2000, 27, 123-38.
    • (2000) International Journal of Biological Macromolecules , vol.27 , pp. 123-138
    • Hearle, J.W.1
  • 56
    • 0033533380 scopus 로고    scopus 로고
    • Disulfide bonds in the outer layer of keratin fibers confer higher mechanical rigidity: correlative nano-indentation and elasticity measurement with an AFM
    • Parbhu, AN; Bryson, WG; Lal, R. Disulfide bonds in the outer layer of keratin fibers confer higher mechanical rigidity: correlative nano-indentation and elasticity measurement with an AFM. Biochemistry, 1999, 38, 11755-61.
    • (1999) Biochemistry , vol.38 , pp. 11755-11761
    • Parbhu, A.N.1    Bryson, W.G.2    Lal, R.3
  • 57
    • 0034682789 scopus 로고    scopus 로고
    • Localization of disulfide bonds in the cystine knot domain of human von Willebrand factor
    • Katsumi, A; Tuley, EA; Bodo, I, et al. Localization of disulfide bonds in the cystine knot domain of human von Willebrand factor. Journal of Biological Chemistry, 2000, 275, 25585-94.
    • (2000) Journal of Biological Chemistry , vol.275 , pp. 25585-25594
    • Katsumi, A.1    Tuley, E.A.2    Bodo, I.3
  • 58
    • 0026780261 scopus 로고
    • Temperature dependence of the disulfide perturbation to the triplet state of tryptophan
    • Li, Z; Bruce, A; Galley, WC. Temperature dependence of the disulfide perturbation to the triplet state of tryptophan. Biophysical Journal, 1992, 61, 1364-71.
    • (1992) Biophysical Journal , vol.61 , pp. 1364-1371
    • Li, Z.1    Bruce, A.2    Galley, W.C.3
  • 59
    • 0009831754 scopus 로고
    • Lanthionine formation in keratin
    • Earland, C; Raven, DJ. Lanthionine formation in keratin. Nature, 1961, 191, 384-.
    • (1961) Nature , vol.191 , pp. 384
    • Earland, C.1    Raven, D.J.2
  • 62
    • 0000197645 scopus 로고
    • Oxidative degradation of collagen and its model peptide by ultraviolet irradiation
    • Kato, Y; Uchida, K; Kawakishi, S. Oxidative degradation of collagen and its model peptide by ultraviolet irradiation. Journal of Agriculture and Food Chemistry, 1992, 40, 373-9.
    • (1992) Journal of Agriculture and Food Chemistry , vol.40 , pp. 373-379
    • Kato, Y.1    Uchida, K.2    Kawakishi, S.3
  • 64
    • 0027319565 scopus 로고
    • Protein-bound 3,4-dihydroxyphenylalanine is a major reductant formed during hydroxyl radical damage to proteins
    • Gieseg, S; Simpson, JA; Charlton, TS, et al. Protein-bound 3,4-dihydroxyphenylalanine is a major reductant formed during hydroxyl radical damage to proteins. Biochemistry, 1993, 32, 4780-6.
    • (1993) Biochemistry , vol.32 , pp. 4780-4786
    • Gieseg, S.1    Simpson, J.A.2    Charlton, T.S.3
  • 65
    • 0017533121 scopus 로고
    • The formation of carbonyl groups during irradiation of wool and its relevance to photoyellowing
    • Holt, LA; Milligan, B. The formation of carbonyl groups during irradiation of wool and its relevance to photoyellowing. Textile Research Journal, 1977, 47, 620-4.
    • (1977) Textile Research Journal , vol.47 , pp. 620-624
    • Holt, L.A.1    Milligan, B.2
  • 66
    • 33750710080 scopus 로고    scopus 로고
    • Protein oxidation and aging
    • Stadtman, ER. Protein oxidation and aging. Free Radical Research, 2006, 40, 1250-8.
    • (2006) Free Radical Research , vol.40 , pp. 1250-1258
    • Stadtman, E.R.1
  • 67
    • 84889305988 scopus 로고    scopus 로고
    • Mass spectrometry approaches for the molecular characterisation of oxidatively/nitrosatively modified proteins
    • In: Dalle-Donne, I; Scaloni, A; Desiderio, DM; Nibbering, NM, editors.
    • Scaloni, A. Mass spectrometry approaches for the molecular characterisation of oxidatively/nitrosatively modified proteins. In: Dalle-Donne, I; Scaloni, A; Desiderio, DM; Nibbering, NM, editors. Redox Proteomics, 2006.
    • (2006) Redox Proteomics
    • Scaloni, A.1
  • 68
    • 84889411742 scopus 로고    scopus 로고
    • Redox Proteomics - From Protein Modifications to Cellular Dysfunctions and Diseases
    • Hoboken: John Wiley and Sons, Inc.
    • Dalle-Donne, I; Scaloni, A; Butterfield, DA, editors. Redox Proteomics - From Protein Modifications to Cellular Dysfunctions and Diseases. Hoboken: John Wiley and Sons, Inc., 2006.
    • (2006)
    • Dalle-Donne, I.1    Scaloni, A.2    Butterfield, D.A.3
  • 70
    • 34547408364 scopus 로고    scopus 로고
    • Histidinoalanine: a crosslinking amino acid
    • Taylor, CM; Wang, W. Histidinoalanine: a crosslinking amino acid. Tetrahedron, 2007, 63, 9033-47.
    • (2007) Tetrahedron , vol.63 , pp. 9033-9047
    • Taylor, C.M.1    Wang, W.2
  • 71
    • 67749106073 scopus 로고    scopus 로고
    • Biophysical and Physiological Effects of Solar Radiation on Human Skin
    • Cambridge, UK: RSC Publishing
    • Giacomoni, PU, editor. Biophysical and Physiological Effects of Solar Radiation on Human Skin. Cambridge, UK: RSC Publishing; 2007.
    • (2007)
    • Giacomoni, P.U.1
  • 73
    • 0018264716 scopus 로고
    • Human skin collagen. Presence of type I and type III at all levels of the dermis
    • Epstein, EH, Jr.; Munderloh, NH. Human skin collagen. Presence of type I and type III at all levels of the dermis. Journal of Biological Chemistry, 1978, 253, 1336-7.
    • (1978) Journal of Biological Chemistry , vol.253 , pp. 1336-1337
    • Epstein Jr., E.H.1    Munderloh, N.H.2
  • 74
    • 0034793435 scopus 로고    scopus 로고
    • Distinct melanogenic response of human melanocytes in mono-culture, in co-culture with keratinocytes and in reconstructed epidermis, to UV exposure
    • Duval, C; Regnier, M; Schmidt, R. Distinct melanogenic response of human melanocytes in mono-culture, in co-culture with keratinocytes and in reconstructed epidermis, to UV exposure. Pigment Cell Research, 2001, 14, 348-55.
    • (2001) Pigment Cell Research , vol.14 , pp. 348-355
    • Duval, C.1    Regnier, M.2    Schmidt, R.3
  • 76
    • 0029967027 scopus 로고    scopus 로고
    • A review of skin ageing and its medical therapy
    • Gilchrest, BA. A review of skin ageing and its medical therapy. British Journal of Dermatology, 1996, 135, 867-75.
    • (1996) British Journal of Dermatology , vol.135 , pp. 867-875
    • Gilchrest, B.A.1
  • 77
    • 0036223839 scopus 로고    scopus 로고
    • Photoaging is associated with protein oxidation in human skin in vivo
    • Sander, CS; Chang, H; Salzmann, S, et al. Photoaging is associated with protein oxidation in human skin in vivo. Journal of Investigative Dermatology, 2002, 118, 618-25.
    • (2002) Journal of Investigative Dermatology , vol.118 , pp. 618-625
    • Sander, C.S.1    Chang, H.2    Salzmann, S.3
  • 78
    • 0024100767 scopus 로고
    • The structure of human hair
    • Hashimoto, K. The structure of human hair. Clinics in Dermatology, 1988, 6, 7-21.
    • (1988) Clinics in Dermatology , vol.6 , pp. 7-21
    • Hashimoto, K.1
  • 79
    • 34547240716 scopus 로고    scopus 로고
    • Hair - the most sophisticated biological composite material
    • Popescu, C; Höcker, H. Hair - the most sophisticated biological composite material. Chemical Society Reviews, 2007, 36, 1282-91.
    • (2007) Chemical Society Reviews , vol.36 , pp. 1282-1291
    • Popescu, C.1    Höcker, H.2
  • 80
    • 35348855675 scopus 로고    scopus 로고
    • Characterization of the exocuticle a-layer proteins of wool
    • Bringans, SD; Plowman, JE; Dyer, JM; et al. Characterization of the exocuticle a-layer proteins of wool. Experimental Dermatology, 2007, 16, 951-60.
    • (2007) Experimental Dermatology , vol.16 , pp. 951-960
    • Bringans, S.D.1    Plowman, J.E.2    Dyer, J.M.3
  • 83
    • 0029883824 scopus 로고    scopus 로고
    • Hair: Its structure and response to cosmetic preparations
    • Dawber, R. Hair: Its structure and response to cosmetic preparations. Clinics in Dermatology, 1996, 14, 105-12.
    • (1996) Clinics in Dermatology , vol.14 , pp. 105-112
    • Dawber, R.1
  • 84
    • 33747888015 scopus 로고    scopus 로고
    • Oxidation, antioxidants and cataract formation: a literature review
    • Williams, DL. Oxidation, antioxidants and cataract formation: a literature review. Veterinary Ophthamology, 2006, 9, 292-8.
    • (2006) Veterinary Ophthamology , vol.9 , pp. 292-298
    • Williams, D.L.1
  • 85
    • 0017225249 scopus 로고
    • Identification of ß-carbolines isolated from fluorescent human lens proteins
    • Dillon, J; Spector, A; Nakanishi, K. Identification of ß-carbolines isolated from fluorescent human lens proteins. Nature, 1976, 259, 422-3.
    • (1976) Nature , vol.259 , pp. 422-423
    • Dillon, J.1    Spector, A.2    Nakanishi, K.3
  • 86
    • 0025506306 scopus 로고
    • The reaction of singlet oxygen with proteins, with special reference to crystallins
    • Balasubramanian, D; Du, X; Zigler, JS. The reaction of singlet oxygen with proteins, with special reference to crystallins. Photochemistry and Photobiology, 1990, 52, 761-8.
    • (1990) Photochemistry and Photobiology , vol.52 , pp. 761-768
    • Balasubramanian, D.1    Du, X.2    Zigler, J.S.3
  • 87
    • 0031791713 scopus 로고    scopus 로고
    • Identification of tryptophan oxidation products in bovine a-crystallin
    • Finley, EL; Dillon, J; Crouch, RK, et al. Identification of tryptophan oxidation products in bovine a-crystallin. Protein Science, 1998, 7, 2391-7.
    • (1998) Protein Science , vol.7 , pp. 2391-2397
    • Finley, E.L.1    Dillon, J.2    Crouch, R.K.3
  • 88
  • 89
    • 58349121970 scopus 로고    scopus 로고
    • Advanced glycation endproducts induce photocrosslinking and oxidation of bovine lens tissue through Type-I mechanism
    • Fuentealba, D; Friguet, B; Silva, E. Advanced glycation endproducts induce photocrosslinking and oxidation of bovine lens tissue through Type-I mechanism. Photochemistry and Photobiology, 2009, 85, 185-94.
    • (2009) Photochemistry and Photobiology , vol.85 , pp. 185-194
    • Fuentealba, D.1    Friguet, B.2    Silva, E.3
  • 90
    • 85129915117 scopus 로고    scopus 로고
    • Pharmaceutical Photostability and Stabilization Technology
    • Informa HealthCare
    • Piechocki, JT; Thoma, K, editors. Pharmaceutical Photostability and Stabilization Technology: Informa HealthCare; 2006.
    • (2006)
    • Piechocki, J.T.1    Thoma, K.2
  • 92
    • 0035897596 scopus 로고    scopus 로고
    • Chemical reactivity in solid-state pharmaceuticals: formulation implications
    • Byrn, SR; Xu, W; Newman, AW. Chemical reactivity in solid-state pharmaceuticals: formulation implications. Advanced Drug Delivery Reviews, 2001, 48, 115-36.
    • (2001) Advanced Drug Delivery Reviews , vol.48 , pp. 115-136
    • Byrn, S.R.1    Xu, W.2    Newman, A.W.3
  • 93
    • 84903931192 scopus 로고    scopus 로고
    • Improving the Sensory and Nutritional Quality of Fresh Meat
    • Cambridge: Woodhead Publishing Limited
    • Kerry, JP; Ledward, D; editors. Improving the Sensory and Nutritional Quality of Fresh Meat. Cambridge: Woodhead Publishing Limited, 2009.
    • (2009)
    • Kerry, J.P.1    Ledward, D.2
  • 94
    • 1042267981 scopus 로고    scopus 로고
    • Meat flavor: contribution of proteins and peptides to the flavor of beef
    • In: Shahidi, F, editor., Kluwer Academic/Plenum Publishers
    • Spanier, AM; Flores, M; Toldra, F, et al. Meat flavor: contribution of proteins and peptides to the flavor of beef. In: Shahidi, F, editor. Quality of fresh and processed foods: Kluwer Academic/Plenum Publishers; 2004, 33-49.
    • (2004) Quality of fresh and processed foods , pp. 33-49
    • Spanier, A.M.1    Flores, M.2    Toldra, F.3
  • 95
    • 0035545697 scopus 로고    scopus 로고
    • Aldehyde reactivity with 2-thiobarbituric acid and TBARS in freeze-dried beef during accelerated storage
    • Sun, Q; Faustman, C; Senecal, A; et al. Aldehyde reactivity with 2-thiobarbituric acid and TBARS in freeze-dried beef during accelerated storage. Meat Science, 2001, 57, 55-60.
    • (2001) Meat Science , vol.57 , pp. 55-60
    • Sun, Q.1    Faustman, C.2    Senecal, A.3
  • 96
    • 0000016866 scopus 로고    scopus 로고
    • Lipid oxidation: Flavor and nutritional quality deterioration in frozen foods
    • In: MP; Erickson, YC, Hung, editors., Springer
    • Erickson, MC. Lipid oxidation: Flavor and nutritional quality deterioration in frozen foods. In: MP; Erickson, YC, Hung, editors. Quality in Frozen Food: Springer; 1997.
    • (1997) Quality in Frozen Food
    • Erickson, M.C.1
  • 98
    • 0036316607 scopus 로고    scopus 로고
    • Photo-oxidation of nitrosylmyoglobin at low oxygen pressure. Quantum yields and reaction stoechiometries
    • Møller, JKS; Bertelsen, G; Skibsted, LH. Photo-oxidation of nitrosylmyoglobin at low oxygen pressure. Quantum yields and reaction stoechiometries. Meat Science, 2002, 60, 421-5.
    • (2002) Meat Science , vol.60 , pp. 421-425
    • Møller, J.K.S.1    Bertelsen, G.2    Skibsted, L.H.3
  • 100
    • 0242396711 scopus 로고    scopus 로고
    • Protein oxidation and implications for muscle food quality
    • In: E; Decker, C; Faustman, CJ; Lopez-Bote, editors., Wiley Interscience
    • Xiong, YL. Protein oxidation and implications for muscle food quality. In: E; Decker, C; Faustman, CJ; Lopez-Bote, editors. Antioxidants in Muscle Foods - Nutritional Strategies to Improve Quality: Wiley Interscience; 2000, 85-112.
    • (2000) Antioxidants in Muscle Foods - Nutritional Strategies to Improve Quality , pp. 85-112
    • Xiong, Y.L.1
  • 101
    • 34250895759 scopus 로고    scopus 로고
    • Proteomic studies on protein oxidation in bonito (Katsuwonus pelamis) muscle
    • Kinoshita, Y; Sato, T. (2007). Proteomic studies on protein oxidation in bonito (Katsuwonus pelamis) muscle. Food Science and Technology Research, 13, 133-8.
    • (2007) Food Science and Technology Research , vol.13 , pp. 133-138
    • Kinoshita, Y.1    Sato, T.2
  • 102
    • 8444228209 scopus 로고    scopus 로고
    • Two-dimensional gel electrophoresis detection of protein oxidation in fresh and tainted rainbow trout muscle
    • Kjaersgard, IVH; Jessen, F. Two-dimensional gel electrophoresis detection of protein oxidation in fresh and tainted rainbow trout muscle. Journal of Agricultural and Food Chemistry, 2004, 52, 7101-7.
    • (2004) Journal of Agricultural and Food Chemistry , vol.52 , pp. 7101-7107
    • Kjaersgard, I.V.H.1    Jessen, F.2
  • 103
    • 38349042205 scopus 로고    scopus 로고
    • Protein and lipid oxidation during frozen storage of rainbow trout (Oncorhynchus mykiss)
    • Baron, CP; Jessen, F, et al. Protein and lipid oxidation during frozen storage of rainbow trout (Oncorhynchus mykiss). Journal of Agricultural and Food Chemistry, 2007, 55, 8118-25.
    • (2007) Journal of Agricultural and Food Chemistry , vol.55 , pp. 8118-8125
    • Baron, C.P.1    Jessen, F.2
  • 104
    • 34247538316 scopus 로고    scopus 로고
    • The effects of an iron-catalyzed oxidation system on lipids and proteins of dark muscle fish
    • Tokur, B; Korkmaz, K. The effects of an iron-catalyzed oxidation system on lipids and proteins of dark muscle fish. Food Chemistry, 2007, 104, 754-60.
    • (2007) Food Chemistry , vol.104 , pp. 754-760
    • Tokur, B.1    Korkmaz, K.2
  • 106
    • 15044344030 scopus 로고    scopus 로고
    • Protective influence of several packaging materials on light oxidation of milk
    • Mestdagh, F; De Meulenaer, B; De Clippeleer, J, et al. Protective influence of several packaging materials on light oxidation of milk. Journal of Dairy Science, 2005, 88, 499-510.
    • (2005) Journal of Dairy Science , vol.88 , pp. 499-510
    • Mestdagh, F.1    De Meulenaer, B.2    De Clippeleer, J.3
  • 107
    • 2642571186 scopus 로고    scopus 로고
    • Influence of feeding different types of roughage on the oxidative stability of milk
    • Havemose, MS; Weisbjerg, MR; Bredie, WLP; et al. Influence of feeding different types of roughage on the oxidative stability of milk. International Dairy Journal, 2004, 14, 563-70.
    • (2004) International Dairy Journal , vol.14 , pp. 563-570
    • Havemose, M.S.1    Weisbjerg, M.R.2    Bredie, W.L.P.3
  • 108
    • 0031860170 scopus 로고    scopus 로고
    • Singlet oxygen and ascorbic acid effects on dimethyl disulfide and off-flavor in skim milk exposed to light
    • Jung, MY; Yoon, SH; Lee, HO; et al. Singlet oxygen and ascorbic acid effects on dimethyl disulfide and off-flavor in skim milk exposed to light. Journal of Food Science, 1998, 63, 408-12.
    • (1998) Journal of Food Science , vol.63 , pp. 408-412
    • Jung, M.Y.1    Yoon, S.H.2    Lee, H.O.3
  • 109
    • 23944448624 scopus 로고    scopus 로고
    • Deactivation of riboflavin triplet-excited state by phenolic antioxidants: mechanism behind protective effects in photo-oxidation of milk-based beverages
    • Becker, EM; Cardoso, DR; Skibsted, LH. Deactivation of riboflavin triplet-excited state by phenolic antioxidants: mechanism behind protective effects in photo-oxidation of milk-based beverages. European Food Research & Technology, 2005, 221, 382-6.
    • (2005) European Food Research & Technology , vol.221 , pp. 382-386
    • Becker, E.M.1    Cardoso, D.R.2    Skibsted, L.H.3
  • 112
    • 64249132475 scopus 로고    scopus 로고
    • Effect of photo-oxidation of major milk proteins on protein structure and hydrolysis by chymosin
    • Dalsgaard, TK; Larsen, LB. Effect of photo-oxidation of major milk proteins on protein structure and hydrolysis by chymosin. International Dairy Journal, 2009.
    • (2009) International Dairy Journal
    • Dalsgaard, T.K.1    Larsen, L.B.2
  • 114
    • 55249125700 scopus 로고    scopus 로고
    • Redox proteomics: basic principles and future perspectives for the detection of protein oxidation in plants
    • Rinalducci, S; Murgiano, L; Zolla, L. Redox proteomics: basic principles and future perspectives for the detection of protein oxidation in plants. Journal of Experimental Botany, 2008, 59, 3781-801.
    • (2008) Journal of Experimental Botany , vol.59 , pp. 3781-3801
    • Rinalducci, S.1    Murgiano, L.2    Zolla, L.3
  • 115
    • 0036094894 scopus 로고    scopus 로고
    • Differences between sensory profiles and development of rancidity during long-term storage of native and processed oat
    • Heinio, RL; Lehtinen, P; Oksman-Caldentey, KM; et al. Differences between sensory profiles and development of rancidity during long-term storage of native and processed oat. Cereal Chemistry, 2002, 79, 367.
    • (2002) Cereal Chemistry , vol.79 , pp. 367
    • Heinio, R.L.1    Lehtinen, P.2    Oksman-Caldentey, K.M.3
  • 116
    • 0025678972 scopus 로고
    • Structure and expression of genes for a class of cysteine-rich proteins of the cuticle layers of differentiating wool and hair follicles
    • MacKinnon, PJ; Powell, BC; Rogers, GE. Structure and expression of genes for a class of cysteine-rich proteins of the cuticle layers of differentiating wool and hair follicles. Journal of Cell Biology, 1990, 111, 2587-600.
    • (1990) Journal of Cell Biology , vol.111 , pp. 2587-2600
    • MacKinnon, P.J.1    Powell, B.C.2    Rogers, G.E.3
  • 117
    • 0036981365 scopus 로고    scopus 로고
    • X-ray photoelectron spectroscopic study of silk fibroin surface
    • Jianzhong, S; Jinqiang, L; Jinhuan, Z; et al. X-ray photoelectron spectroscopic study of silk fibroin surface. Polymer International, 2002, 51, 1479-83.
    • (2002) Polymer International , vol.51 , pp. 1479-1483
    • Jianzhong, S.1    Jinqiang, L.2    Jinhuan, Z.3
  • 119
    • 0032035828 scopus 로고    scopus 로고
    • Photochemical behaviour of natural silk--II. Mechanism of fibroin photodestruction
    • Baltova, S; Vassileva, V. Photochemical behaviour of natural silk--II. Mechanism of fibroin photodestruction. Polymer Degradation and Stability, 1998, 60, 61-5.
    • (1998) Polymer Degradation and Stability , vol.60 , pp. 61-65
    • Baltova, S.1    Vassileva, V.2
  • 120
    • 37249002341 scopus 로고    scopus 로고
    • The photoyellowing of stilbene-derived fluorescent whitening agents-mass spectrometric characterization of yellow photoproducts
    • Dyer, JM; Cornellison, CD; Bringans, SD, et al. The photoyellowing of stilbene-derived fluorescent whitening agents-mass spectrometric characterization of yellow photoproducts. Photochemistry and Photobiology, 2008, 84, 145-53.
    • (2008) Photochemistry and Photobiology , vol.84 , pp. 145-153
    • Dyer, J.M.1    Cornellison, C.D.2    Bringans, S.D.3
  • 121
    • 33746301789 scopus 로고    scopus 로고
    • Photoyellowing of wool. Part 1: Factors affecting photoyellowing and experimental techniques
    • Millington, KR. Photoyellowing of wool. Part 1: Factors affecting photoyellowing and experimental techniques. Coloration Technology, 2006, 122, 169-86.
    • (2006) Coloration Technology , vol.122 , pp. 169-186
    • Millington, K.R.1
  • 122
    • 3042544639 scopus 로고    scopus 로고
    • The generation of superoxide and hydrogen peroxide by exposure of fluorescent whitening agents to UVA radiation and its relevance to the rapid photoyellowing of whitened wool
    • Millington, KR; Maurdev, G. The generation of superoxide and hydrogen peroxide by exposure of fluorescent whitening agents to UVA radiation and its relevance to the rapid photoyellowing of whitened wool. Journal of Photochemistry and Photobiology A: Chemistry, 2004, 165, 177-85.
    • (2004) Journal of Photochemistry and Photobiology A: Chemistry , vol.165 , pp. 177-185
    • Millington, K.R.1    Maurdev, G.2
  • 123
    • 53649083712 scopus 로고    scopus 로고
    • Assisted interpretation of laser-induced fluorescence spectra of egg-based binding media using total emission fluorescence spectroscopy
    • Article ID 82823
    • Nevin, A; Anglos, D. Assisted interpretation of laser-induced fluorescence spectra of egg-based binding media using total emission fluorescence spectroscopy. Laser Chemistry, 2006, Article ID 82823, 5.
    • (2006) Laser Chemistry , pp. 5
    • Nevin, A.1    Anglos, D.2
  • 125
    • 67650354415 scopus 로고    scopus 로고
    • Protein tyrosine nitration: Selectivity, physicochemical and biological consequences, denitration and proteomics methods for the identification of tyrosine-nitrated proteins
    • Abello, N; Kerstjens, HAM; Postma, DS; et al. Protein tyrosine nitration: Selectivity, physicochemical and biological consequences, denitration and proteomics methods for the identification of tyrosine-nitrated proteins. Journal of Proteome Research, 2009, 8, 3222-38.
    • (2009) Journal of Proteome Research , vol.8 , pp. 3222-3238
    • Abello, N.1    Kerstjens, H.A.M.2    Postma, D.S.3
  • 126
    • 84879815691 scopus 로고    scopus 로고
    • MudPIT (multidimensional protein identification technology) for identification of post-translational protein modifications in complex biological mixtures
    • In: I; Dalle-Donne, A; Scaloni, DA; Butterfield, editors., Hoboken: John Wiley and Sons, Inc.
    • Thomas, SN; Lu, BW; Nikolskaya, T; et al. MudPIT (multidimensional protein identification technology) for identification of post-translational protein modifications in complex biological mixtures. In: I; Dalle-Donne, A; Scaloni, DA; Butterfield, editors. Redox Proteomics - From Protein Modifications to Cellular Dysfunctions and Diseases. Hoboken: John Wiley and Sons, Inc., 2006, 233-52.
    • (2006) Redox Proteomics - From Protein Modifications to Cellular Dysfunctions and Diseases. , pp. 233-252
    • Thomas, S.N.1    Lu, B.W.2    Nikolskaya, T.3
  • 127
    • 84892057226 scopus 로고    scopus 로고
    • BLAST software. Available from:
    • BLAST software. Available from: http://blast.ncbi.nlm.nih.gov/Blast.cgi?PROGRAM=blastp&BLAST_PROGRAMS=blastp&PAGE_TYPE=BlastSearch&SHOW_DEFAULTS=on&LINK_LOC=blasthome
  • 128
    • 67349228432 scopus 로고    scopus 로고
    • Singlet-oxygen-mediated amino acid and protein oxidation: Formation of tryptophan peroxides and decomposition products
    • Gracanin, M; Hawkins, CL; Pattison, DI; et al. Singlet-oxygen-mediated amino acid and protein oxidation: Formation of tryptophan peroxides and decomposition products. Free Radical Biology and Medicine, 2009, 47, 92-102.
    • (2009) Free Radical Biology and Medicine , vol.47 , pp. 92-102
    • Gracanin, M.1    Hawkins, C.L.2    Pattison, D.I.3
  • 129
    • 77953616825 scopus 로고    scopus 로고
    • Profiling of residue-level photo-oxidative damage in peptides
    • In Press doi: 10.1007/s00726-009-0440-7.
    • Grosvenor, AJ; Morton, JD; Dyer, JM. Profiling of residue-level photo-oxidative damage in peptides. Amino Acids, 2009, In Press doi: 10.1007/s00726-009-0440-7.
    • (2009) Amino Acids
    • Grosvenor, A.J.1    Morton, J.D.2    Dyer, J.M.3
  • 130
    • 33847174067 scopus 로고    scopus 로고
    • Protein labeling by iTRAQ: A new tool for quantitative mass spectrometry in proteome research
    • Wiese, S; Reidegeld, KA; Meyer, HE; et al. Protein labeling by iTRAQ: A new tool for quantitative mass spectrometry in proteome research. Proteomics, 2007, 7, 340-50.
    • (2007) Proteomics , vol.7 , pp. 340-350
    • Wiese, S.1    Reidegeld, K.A.2    Meyer, H.E.3
  • 131
    • 33644845960 scopus 로고    scopus 로고
    • Comparative study of three proteomic quantitative methods, DIGE, cICAT, and iTRAQ, using 2D gel- or LC-MALDI TOF/TOF
    • Wu, WW; Wang, G; Baek, SJ, et al. Comparative study of three proteomic quantitative methods, DIGE, cICAT, and iTRAQ, using 2D gel- or LC-MALDI TOF/TOF. Journal of Proteome Research, 2006, 5, 651-8.
    • (2006) Journal of Proteome Research , vol.5 , pp. 651-658
    • Wu, W.W.1    Wang, G.2    Baek, S.J.3
  • 132
    • 0033543508 scopus 로고    scopus 로고
    • Protein crosslinks: Universal isolation and characterization by isotopic derivatization and electrospray ionization mass spectrometry
    • Chen, X; Chen, YH; Anderson, VE. Protein crosslinks: Universal isolation and characterization by isotopic derivatization and electrospray ionization mass spectrometry. Analytical Biochemistry, 1999, 273, 192-203.
    • (1999) Analytical Biochemistry , vol.273 , pp. 192-203
    • Chen, X.1    Chen, Y.H.2    Anderson, V.E.3
  • 133
    • 0036714166 scopus 로고    scopus 로고
    • Identification of crosslinked peptides for protein interaction studies using mass spectrometry and 18O labeling
    • Back, JW; Notenboom, V; De Koning, LJ; et al. Identification of crosslinked peptides for protein interaction studies using mass spectrometry and 18O labeling. Analytical Chemistry, 2002, 74, 4417-22.
    • (2002) Analytical Chemistry , vol.74 , pp. 4417-4422
    • Back, J.W.1    Notenboom, V.2    De Koning, L.J.3
  • 134
    • 51649130184 scopus 로고    scopus 로고
    • 18O labeling over a coffee break: A rapid strategy for quantitative proteomics
    • Mirza, SP; Greene, AS; Olivier, M. 18O labeling over a coffee break: A rapid strategy for quantitative proteomics. Journal of Proteome Research, 2008, 7, 3042-8.
    • (2008) Journal of Proteome Research , vol.7 , pp. 3042-3048
    • Mirza, S.P.1    Greene, A.S.2    Olivier, M.3


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