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Volumn 33, Issue 1, 2014, Pages 21-48

Protein carbonylation: Proteomics, specificity and relevance to aging

Author keywords

aging; carbonyl detection; metal catalyzed oxidation; oxidative stress; protein carbonylation; proteomics; specific damage

Indexed keywords

BIOLOGICAL SAMPLES; DETECTION AND QUANTIFICATIONS; METAL-CATALYZED OXIDATIONS; PROTEIN CARBONYLATION; PROTEIN CARBONYLS; PROTEOMIC; PROTEOMICS; SPECIFIC DAMAGE;

EID: 84889879806     PISSN: 02777037     EISSN: 10982787     Source Type: Journal    
DOI: 10.1002/mas.21375     Document Type: Article
Times cited : (67)

References (167)
  • 1
    • 65249129156 scopus 로고    scopus 로고
    • Creatine and its potential therapeutic value for targeting cellular energy impairment in neurodegenerative diseases
    • Adhihetty PJ, Beal MF,. 2008. Creatine and its potential therapeutic value for targeting cellular energy impairment in neurodegenerative diseases. Neuromol Med 10: 275-290.
    • (2008) Neuromol Med , vol.10 , pp. 275-290
    • Adhihetty, P.J.1    Beal, M.F.2
  • 2
    • 0028221322 scopus 로고
    • Aging and proteolysis of oxidized proteins
    • Agarwal S, Sohal RS,. 1994. Aging and proteolysis of oxidized proteins. Arch Biochem Biophys 309: 24-28.
    • (1994) Arch Biochem Biophys , vol.309 , pp. 24-28
    • Agarwal, S.1    Sohal, R.S.2
  • 3
    • 0242585476 scopus 로고    scopus 로고
    • Asymmetric inheritance of oxidatively damaged proteins during cytokinesis
    • Aguilaniu H, Gustafsson L, Rigoulet M, Nyström T,. 2003. Asymmetric inheritance of oxidatively damaged proteins during cytokinesis. Science 299: 1751-1753.
    • (2003) Science , vol.299 , pp. 1751-1753
    • Aguilaniu, H.1    Gustafsson, L.2    Rigoulet, M.3    Nyström, T.4
  • 5
    • 0023127085 scopus 로고
    • Use of fluorescein hydrazide and fluorescein thiosemicarbazide reagents for the fluorometric determination of protein carbonyl groups and for the detection of oxidized protein on polyacrylamide gels
    • Ahn B, Rhee SG, Stadtman ER,. 1987. Use of fluorescein hydrazide and fluorescein thiosemicarbazide reagents for the fluorometric determination of protein carbonyl groups and for the detection of oxidized protein on polyacrylamide gels. Anal Biochem 161: 245-257.
    • (1987) Anal Biochem , vol.161 , pp. 245-257
    • Ahn, B.1    Rhee, S.G.2    Stadtman, E.R.3
  • 6
    • 0034024347 scopus 로고    scopus 로고
    • Oxidative modification of creatine kinase BB in Alzheimer's disease brain
    • Aksenov M, Aksenova M, Butterfield DA, Markesbery WR,. 2000. Oxidative modification of creatine kinase BB in Alzheimer's disease brain. J Neurochem 74: 2520-2527.
    • (2000) J Neurochem , vol.74 , pp. 2520-2527
    • Aksenov, M.1    Aksenova, M.2    Butterfield, D.A.3    Markesbery, W.R.4
  • 7
    • 84866371799 scopus 로고    scopus 로고
    • The essential iron-sulfur protein Rli1 is an important target accounting for inhibition of cell growth by reactive oxygen species
    • Alhebshi A, Sideri TC, Holland SL, Avery SV,. 2012. The essential iron-sulfur protein Rli1 is an important target accounting for inhibition of cell growth by reactive oxygen species. Mol Biol Cell 23: 3582-3590.
    • (2012) Mol Biol Cell , vol.23 , pp. 3582-3590
    • Alhebshi, A.1    Sideri, T.C.2    Holland, S.L.3    Avery, S.V.4
  • 8
    • 0024514390 scopus 로고
    • Conversion of amino acid residues in proteins and amino acid homopolymers to carbonyl derivatives by metal-catalyzed oxidation reactions
    • Amici A, Levine RL, Tsai L, Stadtman ER,. 1989. Conversion of amino acid residues in proteins and amino acid homopolymers to carbonyl derivatives by metal-catalyzed oxidation reactions. J Biol Chem 264: 3341-3346.
    • (1989) J Biol Chem , vol.264 , pp. 3341-3346
    • Amici, A.1    Levine, R.L.2    Tsai, L.3    Stadtman, E.R.4
  • 9
    • 79251595904 scopus 로고    scopus 로고
    • Effect of aging and oxidative stress on elongation factor-2 in hypothalamus and hypophysis
    • Argüelles S, Cano M, Machado A, Ayala A,. 2011. Effect of aging and oxidative stress on elongation factor-2 in hypothalamus and hypophysis. Mech Ageing Dev 132: 55-64.
    • (2011) Mech Ageing Dev , vol.132 , pp. 55-64
    • Argüelles, S.1    Cano, M.2    Machado, A.3    Ayala, A.4
  • 10
    • 79951518607 scopus 로고    scopus 로고
    • Molecular targets of oxidative stress
    • Avery SV,. 2011. Molecular targets of oxidative stress. Biochem J 434: 201-210.
    • (2011) Biochem J , vol.434 , pp. 201-210
    • Avery, S.V.1
  • 11
    • 13944278132 scopus 로고    scopus 로고
    • Mitochondria, oxidants, and aging
    • Balaban RS, Nemoto S, Finkel T,. 2005. Mitochondria, oxidants, and aging. Cell 120: 483-495.
    • (2005) Cell , vol.120 , pp. 483-495
    • Balaban, R.S.1    Nemoto, S.2    Finkel, T.3
  • 12
    • 0035903569 scopus 로고    scopus 로고
    • Bacterial senescence: Protein oxidation in non-proliferating cells is dictated by the accuracy of the ribosomes
    • Ballesteros M, Fredriksson A, Henriksson J, Nystrom T,. 2001. Bacterial senescence: Protein oxidation in non-proliferating cells is dictated by the accuracy of the ribosomes. EMBO J 20: 5280-5289.
    • (2001) EMBO J , vol.20 , pp. 5280-5289
    • Ballesteros, M.1    Fredriksson, A.2    Henriksson, J.3    Nystrom, T.4
  • 13
    • 84869051809 scopus 로고    scopus 로고
    • Protein oxidative damage at the crossroads of cellular senescence, aging, and age-related diseases
    • Article ID 919832
    • Baraibar MA, Liu L, Ahmed EK, Friguet B,. 2012. Protein oxidative damage at the crossroads of cellular senescence, aging, and age-related diseases. Oxid Med Cell Longev 2012: Article ID 919832: 8 pages.
    • (2012) Oxid Med Cell Longev , vol.2012 , pp. 8
    • Baraibar, M.A.1    Liu, L.2    Ahmed, E.K.3    Friguet, B.4
  • 15
    • 75149149380 scopus 로고    scopus 로고
    • Protein carbonylation in skeletal muscles: Impact on function
    • Barreiro E, Hussain SN,. 2010. Protein carbonylation in skeletal muscles: Impact on function. Antioxid Redox Signal 12: 417-429.
    • (2010) Antioxid Redox Signal , vol.12 , pp. 417-429
    • Barreiro, E.1    Hussain, S.N.2
  • 16
    • 28644451208 scopus 로고    scopus 로고
    • Expression and carbonylation of creatine kinase in the quadriceps femoris muscles of patients with chronic obstructive pulmonary disease
    • Barreiro E, Gea J, Matar G, Hussain SN,. 2005. Expression and carbonylation of creatine kinase in the quadriceps femoris muscles of patients with chronic obstructive pulmonary disease. Am J Respir Cell Mol Biol 33: 636-642.
    • (2005) Am J Respir Cell Mol Biol , vol.33 , pp. 636-642
    • Barreiro, E.1    Gea, J.2    Matar, G.3    Hussain, S.N.4
  • 17
    • 0032013732 scopus 로고    scopus 로고
    • Immunological detection and quantification of oxidized proteins by labelling with digoxigenin
    • Bautista J, Mateos-Nevado MD,. 1998. Immunological detection and quantification of oxidized proteins by labelling with digoxigenin. Biosci Biotechnol Biochem 62: 419-423.
    • (1998) Biosci Biotechnol Biochem , vol.62 , pp. 419-423
    • Bautista, J.1    Mateos-Nevado, M.D.2
  • 18
    • 0030296755 scopus 로고    scopus 로고
    • 2+-catalyzed fragmentation of the soluble F1-ATPase
    • 2+- catalyzed fragmentation of the soluble F1-ATPase. Arch Biochem Biophys 335: 131-138.
    • (1996) Arch Biochem Biophys , vol.335 , pp. 131-138
    • Belogrudov, G.I.1
  • 19
    • 0037184911 scopus 로고    scopus 로고
    • Covalent modification of epithelial fatty acid-binding protein by 4-hydroxynonenal in vitro and in vivo. Evidence for a role in antioxidant biology
    • Bennaars-Eiden A, Higgins L, Hertzel AV, Kapphahn RJ, Ferrington DA, Bernlohr DA,. 2002. Covalent modification of epithelial fatty acid-binding protein by 4-hydroxynonenal in vitro and in vivo. Evidence for a role in antioxidant biology. J Biol Chem 277: 50693-50702.
    • (2002) J Biol Chem , vol.277 , pp. 50693-50702
    • Bennaars-Eiden, A.1    Higgins, L.2    Hertzel, A.V.3    Kapphahn, R.J.4    Ferrington, D.A.5    Bernlohr, D.A.6
  • 20
    • 0030841350 scopus 로고    scopus 로고
    • Protein oxidation in aging, disease, and oxidative stress
    • Berlett BS, Stadtman ER,. 1997. Protein oxidation in aging, disease, and oxidative stress. J Biol Chem 272: 20313-20316.
    • (1997) J Biol Chem , vol.272 , pp. 20313-20316
    • Berlett, B.S.1    Stadtman, E.R.2
  • 21
    • 34249891333 scopus 로고    scopus 로고
    • Two neurons mediate diet-restriction-induced longevity in C. Elegans
    • Bishop NA, Guarente L,. 2007. Two neurons mediate diet-restriction- induced longevity in C. elegans. Nature 447: 545-549.
    • (2007) Nature , vol.447 , pp. 545-549
    • Bishop, N.A.1    Guarente, L.2
  • 22
    • 0037160097 scopus 로고    scopus 로고
    • Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of yeast sir2 and human SIRT1
    • Bitterman KJ, Anderson RM, Cohen HY, Latorre-Esteves M, Sinclair D,. 2002. Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of yeast sir2 and human SIRT1. J Biol Chem 277: 45099-45107.
    • (2002) J Biol Chem , vol.277 , pp. 45099-45107
    • Bitterman, K.J.1    Anderson, R.M.2    Cohen, H.Y.3    Latorre-Esteves, M.4    Sinclair, D.5
  • 23
    • 0141677687 scopus 로고    scopus 로고
    • Longevity regulation in Saccharomyces cerevisiae: Linking metabolism, genome stability, and heterochromatin
    • Bitterman KJ, Medvedik O, Sinclair D,. 2003. Longevity regulation in Saccharomyces cerevisiae: Linking metabolism, genome stability, and heterochromatin. Microbiol Mol Biol Rev 67: 376-399.
    • (2003) Microbiol Mol Biol Rev , vol.67 , pp. 376-399
    • Bitterman, K.J.1    Medvedik, O.2    Sinclair, D.3
  • 24
    • 0037021453 scopus 로고    scopus 로고
    • Modulation of Lon protease activity and aconitase turnover during aging and oxidative stress
    • Bota DA, Van Remmen H, Davies KJ,. 2002. Modulation of Lon protease activity and aconitase turnover during aging and oxidative stress. FEBS Lett 532: 103-106.
    • (2002) FEBS Lett , vol.532 , pp. 103-106
    • Bota, D.A.1    Van Remmen, H.2    Davies, K.J.3
  • 25
    • 15744387176 scopus 로고    scopus 로고
    • Proteomic identification of proteins specifically oxidized by intracerebral injection of amyloid beta-peptide (1-42) into rat brain: Implications for Alzheimer's disease
    • Boyd-Kimball D, Sultana R, Poon HF, Lynn BC, Casamenti F, Pepeu G, Klein JB, Butterfield DA,. 2005a. Proteomic identification of proteins specifically oxidized by intracerebral injection of amyloid beta-peptide (1-42) into rat brain: Implications for Alzheimer's disease. Neuroscience 132: 313-324.
    • (2005) Neuroscience , vol.132 , pp. 313-324
    • Boyd-Kimball, D.1    Sultana, R.2    Poon, H.F.3    Lynn, B.C.4    Casamenti, F.5    Pepeu, G.6    Klein, J.B.7    Butterfield, D.A.8
  • 27
    • 33745990556 scopus 로고    scopus 로고
    • Proteomic identification of proteins specifically oxidized in Caenorhabditis elegans expressing human Abeta (1-42): Implications for Alzheimer's disease
    • Boyd-Kimball D, Poon HF, Lynn BC, Cai J, Pierce WM, Jr., Klein JB, Ferguson J, Link CD, Butterfield DA,. 2006. Proteomic identification of proteins specifically oxidized in Caenorhabditis elegans expressing human Abeta (1-42): Implications for Alzheimer's disease. Neurobiol Aging 27: 1239-1249.
    • (2006) Neurobiol Aging , vol.27 , pp. 1239-1249
    • Boyd-Kimball, D.1    Poon, H.F.2    Lynn, B.C.3    Cai, J.4    Pierce, Jr.W.M.5    Klein, J.B.6    Ferguson, J.7    Link, C.D.8    Butterfield, D.A.9
  • 30
    • 0028181759 scopus 로고
    • 2+ dehydrogenases. Consensus target sequence between propanediol oxidoreductase of Escherichia coli and alcohol dehydrogenase II of Zymomonas mobilis
    • 2+ dehydrogenases. Consensus target sequence between propanediol oxidoreductase of Escherichia coli and alcohol dehydrogenase II of Zymomonas mobilis. J Biol Chem 269: 6592-6597.
    • (1994) J Biol Chem , vol.269 , pp. 6592-6597
    • Cabiscol, E.1    Aguilar, J.2    Ros, J.3
  • 31
    • 0034282468 scopus 로고    scopus 로고
    • Oxidative stress promotes specific protein damage in Saccharomyces cerevisiae
    • Cabiscol E, Piulats E, Echave P, Herrero E, Ros J,. 2000. Oxidative stress promotes specific protein damage in Saccharomyces cerevisiae. J Biol Chem 275: 27393-27398.
    • (2000) J Biol Chem , vol.275 , pp. 27393-27398
    • Cabiscol, E.1    Piulats, E.2    Echave, P.3    Herrero, E.4    Ros, J.5
  • 32
    • 0036733145 scopus 로고    scopus 로고
    • Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part II: Dihydropyrimidinase-related protein 2, alpha-enolase and heat shock cognate 71
    • Castegna A, Aksenov M, Thongboonkerd V, Klein JB, Pierce WM, Booze R, Markesbery WR, Butterfield DA,. 2002. Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part II: Dihydropyrimidinase- related protein 2, alpha-enolase and heat shock cognate 71. J Neurochem 82: 1524-1532.
    • (2002) J Neurochem , vol.82 , pp. 1524-1532
    • Castegna, A.1    Aksenov, M.2    Thongboonkerd, V.3    Klein, J.B.4    Pierce, W.M.5    Booze, R.6    Markesbery, W.R.7    Butterfield, D.A.8
  • 33
    • 34247363723 scopus 로고    scopus 로고
    • Oxidative modification of proteins: Age-related changes
    • Chakravarti B, Chakravarti DN,. 2007. Oxidative modification of proteins: Age-related changes. Gerontology 53: 128-139.
    • (2007) Gerontology , vol.53 , pp. 128-139
    • Chakravarti, B.1    Chakravarti, D.N.2
  • 35
    • 1842634504 scopus 로고    scopus 로고
    • Proteomic identification of specific oxidized proteins in ApoE-knockout mice: Relevance to Alzheimer's disease
    • Choi J, Forster MJ, McDonald SR, Weintraub ST, Carroll CA, Gracy RW,. 2004. Proteomic identification of specific oxidized proteins in ApoE-knockout mice: Relevance to Alzheimer's disease. Free Radic Biol Med 36: 1155-1162.
    • (2004) Free Radic Biol Med , vol.36 , pp. 1155-1162
    • Choi, J.1    Forster, M.J.2    McDonald, S.R.3    Weintraub, S.T.4    Carroll, C.A.5    Gracy, R.W.6
  • 36
    • 0026051445 scopus 로고
    • Oxidation of the active site of glutamine synthetase: Conversion of arginine-344 to gamma-glutamyl semialdehyde
    • Climent I, Levine RL,. 1991. Oxidation of the active site of glutamine synthetase: Conversion of arginine-344 to gamma-glutamyl semialdehyde. Arch Biochem Biophys 289: 371-375.
    • (1991) Arch Biochem Biophys , vol.289 , pp. 371-375
    • Climent, I.1    Levine, R.L.2
  • 39
    • 0036890134 scopus 로고    scopus 로고
    • Hydrogen peroxide-induced carbonylation of key metabolic enzymes in Saccharomyces cerevisiae: The involvement of the oxidative stress response regulators Yap1 and Skn7
    • Costa VM, Amorim MA, Quintanilha A, Moradas-Ferreira P,. 2002. Hydrogen peroxide-induced carbonylation of key metabolic enzymes in Saccharomyces cerevisiae: The involvement of the oxidative stress response regulators Yap1 and Skn7. Free Radic Biol Med 33: 1507-1515.
    • (2002) Free Radic Biol Med , vol.33 , pp. 1507-1515
    • Costa, V.M.1    Amorim, M.A.2    Quintanilha, A.3    Moradas-Ferreira, P.4
  • 43
    • 0035890871 scopus 로고    scopus 로고
    • Selectivity of protein oxidative damage during aging in Drosophila melanogaster
    • Das N, Levine RL, Orr WC, Sohal RS,. 2001. Selectivity of protein oxidative damage during aging in Drosophila melanogaster. Biochem J 360: 209-216.
    • (2001) Biochem J , vol.360 , pp. 209-216
    • Das, N.1    Levine, R.L.2    Orr, W.C.3    Sohal, R.S.4
  • 44
    • 0035879703 scopus 로고    scopus 로고
    • Measurements of protein carbonyls, ortho- and meta-tyrosine and oxidative phosphorylation complex activity in mitochondria from young and old rats
    • Davies SM, Poljak A, Duncan MW, Smythe GA, Murphy MP,. 2001. Measurements of protein carbonyls, ortho- and meta-tyrosine and oxidative phosphorylation complex activity in mitochondria from young and old rats. Free Radic Biol Med 31: 181-190.
    • (2001) Free Radic Biol Med , vol.31 , pp. 181-190
    • Davies, S.M.1    Poljak, A.2    Duncan, M.W.3    Smythe, G.A.4    Murphy, M.P.5
  • 45
    • 0030988742 scopus 로고    scopus 로고
    • Biochemistry and pathology of radical-mediated protein oxidation
    • Dean RT, Fu S, Stocker R, Davies MJ,. 1997. Biochemistry and pathology of radical-mediated protein oxidation. Biochem J 324: 1-18.
    • (1997) Biochem J , vol.324 , pp. 1-18
    • Dean, R.T.1    Fu, S.2    Stocker, R.3    Davies, M.J.4
  • 46
    • 28244466940 scopus 로고    scopus 로고
    • Caloric restriction in humans: Potential pitfalls and health concerns
    • Dirks AJ, Leeuwenburgh C,. 2006. Caloric restriction in humans: Potential pitfalls and health concerns. Mech Ageing Dev 127: 1-7.
    • (2006) Mech Ageing Dev , vol.127 , pp. 1-7
    • Dirks, A.J.1    Leeuwenburgh, C.2
  • 47
    • 0032213238 scopus 로고    scopus 로고
    • Bacterial senescence: Stasis results in increased and differential oxidation of cytoplasmic proteins leading to developmental induction of the heat shock regulon
    • Dukan S, Nyström T,. 1998. Bacterial senescence: Stasis results in increased and differential oxidation of cytoplasmic proteins leading to developmental induction of the heat shock regulon. Genes Dev 12: 3431-3441.
    • (1998) Genes Dev , vol.12 , pp. 3431-3441
    • Dukan, S.1    Nyström, T.2
  • 48
    • 0033543618 scopus 로고    scopus 로고
    • Oxidative stress defense and deterioration of growth-arrested Escherichia coli cells
    • Dukan S, Nyström T,. 1999. Oxidative stress defense and deterioration of growth-arrested Escherichia coli cells. J Biol Chem 274: 26027-26032.
    • (1999) J Biol Chem , vol.274 , pp. 26027-26032
    • Dukan, S.1    Nyström, T.2
  • 49
    • 0042029733 scopus 로고    scopus 로고
    • Novel antioxidant role of alcohol dehydrogenase e from Escherichia coli
    • Echave P, Tamarit J, Cabiscol E, Ros J,. 2003. Novel antioxidant role of alcohol dehydrogenase E from Escherichia coli. J Biol Chem 278: 30193-30198.
    • (2003) J Biol Chem , vol.278 , pp. 30193-30198
    • Echave, P.1    Tamarit, J.2    Cabiscol, E.3    Ros, J.4
  • 50
    • 2942632777 scopus 로고    scopus 로고
    • Identification of carbonylated proteins by MALDI-TOF mass spectroscopy reveals susceptibility of ER
    • England K, Cotter T,. 2004. Identification of carbonylated proteins by MALDI-TOF mass spectroscopy reveals susceptibility of ER. Biochem Biophys Res Commun 320: 123-130.
    • (2004) Biochem Biophys Res Commun , vol.320 , pp. 123-130
    • England, K.1    Cotter, T.2
  • 51
    • 1542359582 scopus 로고    scopus 로고
    • Carbonylation of glycolytic proteins is a key response to drug-induced oxidative stress and apoptosis
    • England K, Driscoll CO, Cotter TG,. 2004. Carbonylation of glycolytic proteins is a key response to drug-induced oxidative stress and apoptosis. Cell Death Differ 11: 252-260.
    • (2004) Cell Death Differ , vol.11 , pp. 252-260
    • England, K.1    Driscoll, C.O.2    Cotter, T.G.3
  • 52
    • 33749330425 scopus 로고    scopus 로고
    • ROS and protein oxidation in early stages of cytotoxic drug induced apoptosis
    • England K, Driscoll CO, Cotter TG,. 2006. ROS and protein oxidation in early stages of cytotoxic drug induced apoptosis. Free Radic Res 40: 1124-1137.
    • (2006) Free Radic Res , vol.40 , pp. 1124-1137
    • England, K.1    Driscoll, C.O.2    Cotter, T.G.3
  • 53
    • 34948846000 scopus 로고    scopus 로고
    • Accelerated aging and failure to segregate damaged proteins in Sir2 mutants can be suppressed by overproducing the protein aggregation-remodeling factor Hsp104p
    • Erkjavec N, Larsson L, Grantham J, Nystrom T,. 2007. Accelerated aging and failure to segregate damaged proteins in Sir2 mutants can be suppressed by overproducing the protein aggregation-remodeling factor Hsp104p. Genes Dev 21: 2410-2421.
    • (2007) Genes Dev , vol.21 , pp. 2410-2421
    • Erkjavec, N.1    Larsson, L.2    Grantham, J.3    Nystrom, T.4
  • 54
    • 0028066642 scopus 로고
    • Nitrogen metabolism in senescing leaves
    • Feller U, Fischer A,. 1994. Nitrogen metabolism in senescing leaves. Crit Rev Plant Sci 13: 241-273.
    • (1994) Crit Rev Plant Sci , vol.13 , pp. 241-273
    • Feller, U.1    Fischer, A.2
  • 55
    • 57149096282 scopus 로고    scopus 로고
    • Quantitative proteomic profiling of muscle type-dependent and age-dependent protein carbonylation in rat skeletal muscle mitochondria
    • Feng J, Xie H, Meany DL, Thompson LV, Arriaga EA, Griffin TJ,. 2008. Quantitative proteomic profiling of muscle type-dependent and age-dependent protein carbonylation in rat skeletal muscle mitochondria. J Gerontol A Biol Sci Med Sci 63: 1137-1152.
    • (2008) J Gerontol A Biol Sci Med Sci , vol.63 , pp. 1137-1152
    • Feng, J.1    Xie, H.2    Meany, D.L.3    Thompson, L.V.4    Arriaga, E.A.5    Griffin, T.J.6
  • 56
    • 20444480246 scopus 로고    scopus 로고
    • Defense against protein carbonylation by DnaK/DnaJ and proteases of the heat shock regulon
    • Fredriksson A, Ballesteros M, Dukan S, Nystrom T,. 2005. Defense against protein carbonylation by DnaK/DnaJ and proteases of the heat shock regulon. J Bacteriol 187: 4207-4213.
    • (2005) J Bacteriol , vol.187 , pp. 4207-4213
    • Fredriksson, A.1    Ballesteros, M.2    Dukan, S.3    Nystrom, T.4
  • 57
    • 34548148201 scopus 로고    scopus 로고
    • Hydrogen peroxide: A metabolic by-product or a common mediator of ageing signals
    • Giorgio M, Trinei M, Migliaccio E, Pelicci PG,. 2007. Hydrogen peroxide: A metabolic by-product or a common mediator of ageing signals ? Nat Rev Mol Cell Biol 8: 722-728.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 722-728
    • Giorgio, M.1    Trinei, M.2    Migliaccio, E.3    Pelicci, P.G.4
  • 58
    • 34247361278 scopus 로고    scopus 로고
    • Carbonylation of adipose proteins in obesity and insulin resistance: Identification of adipocyte fatty acid-binding protein as a cellular target of 4-hydroxynonenal
    • Grimsrud PA, Picklo MJ, Sr., Griffin TJ, Bernlohr DA,. 2007. Carbonylation of adipose proteins in obesity and insulin resistance: Identification of adipocyte fatty acid-binding protein as a cellular target of 4-hydroxynonenal. Mol Cell Proteomics 6: 624-637.
    • (2007) Mol Cell Proteomics , vol.6 , pp. 624-637
    • Grimsrud, P.A.1    Picklo, Sr.M.J.2    Griffin, T.J.3    Bernlohr, D.A.4
  • 59
    • 52049088770 scopus 로고    scopus 로고
    • Oxidative stress and covalent modification of protein with bioactive aldehydes
    • Grimsrud PA, Xie H, Griffin TJ, Bernlohr DA,. 2008. Oxidative stress and covalent modification of protein with bioactive aldehydes. J Biol Chem 283: 21837-21841.
    • (2008) J Biol Chem , vol.283 , pp. 21837-21841
    • Grimsrud, P.A.1    Xie, H.2    Griffin, T.J.3    Bernlohr, D.A.4
  • 60
    • 4344677922 scopus 로고    scopus 로고
    • Decreased proteolysis caused by protein aggregates, inclusion bodies, plaques, lipofuscin, ceroid, and 'aggresomes' during oxidative stress, aging, and disease
    • Grune T, Jung T, Merker K, Davies KJ,. 2004. Decreased proteolysis caused by protein aggregates, inclusion bodies, plaques, lipofuscin, ceroid, and 'aggresomes' during oxidative stress, aging, and disease. Int J Biochem Cell Biol 36: 2519-2530.
    • (2004) Int J Biochem Cell Biol , vol.36 , pp. 2519-2530
    • Grune, T.1    Jung, T.2    Merker, K.3    Davies, K.J.4
  • 61
    • 79551641369 scopus 로고    scopus 로고
    • Does calorie restriction induce mitochondrial biogenesis? A reevaluation
    • Hancock CR, Han DH, Higashida K, Kim SH, Holloszy JO,. 2011. Does calorie restriction induce mitochondrial biogenesis? A reevaluation. FASEB J 25: 785-791.
    • (2011) FASEB J , vol.25 , pp. 785-791
    • Hancock, C.R.1    Han, D.H.2    Higashida, K.3    Kim, S.H.4    Holloszy, J.O.5
  • 62
    • 0030936995 scopus 로고    scopus 로고
    • Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK
    • Harrison CJ, Hayer-Hartl M, Di Liberto M, Hartl F, Kuriyan J,. 1997. Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK. Science 276: 431-435.
    • (1997) Science , vol.276 , pp. 431-435
    • Harrison, C.J.1    Hayer-Hartl, M.2    Di Liberto, M.3    Hartl, F.4    Kuriyan, J.5
  • 63
    • 0027597690 scopus 로고
    • Developmental and age-related processes that influence the longevity and senescence of photosynthetic tissues in Arabidopsis
    • Hensel LL, Grbic V, Baumgarten DA, Bleecker AB,. 1993. Developmental and age-related processes that influence the longevity and senescence of photosynthetic tissues in Arabidopsis. Plant Cell 5: 553-564.
    • (1993) Plant Cell , vol.5 , pp. 553-564
    • Hensel, L.L.1    Grbic, V.2    Baumgarten, D.A.3    Bleecker, A.B.4
  • 64
    • 0036897875 scopus 로고    scopus 로고
    • Stationary phase in yeast
    • Herman PK,. 2002. Stationary phase in yeast. Curr Opin Microbiol 5: 602-607.
    • (2002) Curr Opin Microbiol , vol.5 , pp. 602-607
    • Herman, P.K.1
  • 67
    • 84862834264 scopus 로고    scopus 로고
    • Enriching carbonylated proteins inside a microchip through the use of oxalyldihydrazide as a crosslinker
    • Hollins BC, Soper SA, Feng J,. 2012. Enriching carbonylated proteins inside a microchip through the use of oxalyldihydrazide as a crosslinker. Lab Chip 12: 2526-2532.
    • (2012) Lab Chip , vol.12 , pp. 2526-2532
    • Hollins, B.C.1    Soper, S.A.2    Feng, J.3
  • 68
    • 41549083260 scopus 로고    scopus 로고
    • Major targets of iron-induced protein oxidative damage in frataxin-deficient yeasts are magnesium-binding proteins
    • Irazusta V, Moreno-Cermeno A, Cabiscol E, Ros J, Tamarit J,. 2008. Major targets of iron-induced protein oxidative damage in frataxin-deficient yeasts are magnesium-binding proteins. Free Radic Biol Med 44: 1712-1723.
    • (2008) Free Radic Biol Med , vol.44 , pp. 1712-1723
    • Irazusta, V.1    Moreno-Cermeno, A.2    Cabiscol, E.3    Ros, J.4    Tamarit, J.5
  • 70
    • 73449091792 scopus 로고    scopus 로고
    • Yeast frataxin mutants display decreased superoxide dismutase activity crucial to promote protein oxidative damage
    • Irazusta V, Obis E, Moreno-Cermeno A, Cabiscol E, Ros J, Tamarit J,. 2010b. Yeast frataxin mutants display decreased superoxide dismutase activity crucial to promote protein oxidative damage. Free Radic Biol Med 48: 411-420.
    • (2010) Free Radic Biol Med , vol.48 , pp. 411-420
    • Irazusta, V.1    Obis, E.2    Moreno-Cermeno, A.3    Cabiscol, E.4    Ros, J.5    Tamarit, J.6
  • 71
    • 0037082118 scopus 로고    scopus 로고
    • Specificity of age related carbonylation of plasma proteins in the mouse and rat
    • Jana CK, Das N, Sohal RS,. 2002. Specificity of age related carbonylation of plasma proteins in the mouse and rat. Arch Biochem Biophys 397: 433-439.
    • (2002) Arch Biochem Biophys , vol.397 , pp. 433-439
    • Jana, C.K.1    Das, N.2    Sohal, R.S.3
  • 72
    • 26944480801 scopus 로고    scopus 로고
    • Patterns of protein oxidation in Arabidopsis seeds and during germination
    • Job C, Rajjou L, Lovigny Y, Belghazi M, Job D,. 2005. Patterns of protein oxidation in Arabidopsis seeds and during germination. Plant Physiol 138: 790-802.
    • (2005) Plant Physiol , vol.138 , pp. 790-802
    • Job, C.1    Rajjou, L.2    Lovigny, Y.3    Belghazi, M.4    Job, D.5
  • 73
    • 2542431031 scopus 로고    scopus 로고
    • Progression and specificity of protein oxidation in the life cycle of Arabidopsis thaliana
    • Johansson E, Olsson O, Nystrom T,. 2004. Progression and specificity of protein oxidation in the life cycle of Arabidopsis thaliana. J Biol Chem 279: 22204-22208.
    • (2004) J Biol Chem , vol.279 , pp. 22204-22208
    • Johansson, E.1    Olsson, O.2    Nystrom, T.3
  • 74
    • 0022404292 scopus 로고
    • Inactivation of glycerol dehydrogenase of Klebsiella pneumoniae and the role of divalent cations
    • Johnson EA, Levine RL, Lin EC,. 1985. Inactivation of glycerol dehydrogenase of Klebsiella pneumoniae and the role of divalent cations. J Bacteriol 164: 479-483.
    • (1985) J Bacteriol , vol.164 , pp. 479-483
    • Johnson, E.A.1    Levine, R.L.2    Lin, E.C.3
  • 75
    • 84855217371 scopus 로고    scopus 로고
    • Protein oxidative modification in the aging organism and the role of the ubiquitin proteasomal system
    • Kastle M, Grune T,. 2011. Protein oxidative modification in the aging organism and the role of the ubiquitin proteasomal system. Curr Pharm Des 17: 4007-4022.
    • (2011) Curr Pharm des , vol.17 , pp. 4007-4022
    • Kastle, M.1    Grune, T.2
  • 77
    • 78649699273 scopus 로고    scopus 로고
    • Dynamics of protein damage in yeast frataxin mutant exposed to oxidative stress
    • Kim JH, Sedlak M, Gao Q, Riley CP, Regnier FE, Adamec J,. 2010. Dynamics of protein damage in yeast frataxin mutant exposed to oxidative stress. OMICS 14: 689-699.
    • (2010) OMICS , vol.14 , pp. 689-699
    • Kim, J.H.1    Sedlak, M.2    Gao, Q.3    Riley, C.P.4    Regnier, F.E.5    Adamec, J.6
  • 78
    • 80054863111 scopus 로고    scopus 로고
    • Protein carbonylation detected with light and heavy isotope-labeled 2,4-dinitrophenylhydrazine by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • Kinumi T, Hayashi A, Kawai T, Matsumoto H, Tsujimoto K,. 2009. Protein carbonylation detected with light and heavy isotope-labeled 2,4- dinitrophenylhydrazine by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. J Mass Spectrom Soc Jpn 57: 371-377.
    • (2009) J Mass Spectrom Soc Jpn , vol.57 , pp. 371-377
    • Kinumi, T.1    Hayashi, A.2    Kawai, T.3    Matsumoto, H.4    Tsujimoto, K.5
  • 81
    • 0037312020 scopus 로고    scopus 로고
    • How does calorie restriction work
    • Koubova J, Guarente L,. 2003. How does calorie restriction work ? Genes Dev 17: 313-321.
    • (2003) Genes Dev , vol.17 , pp. 313-321
    • Koubova, J.1    Guarente, L.2
  • 82
    • 0032497420 scopus 로고    scopus 로고
    • Thiol-dependent metal-catalyzed oxidation of copper, zinc superoxide dismutase
    • Kwon OJ, Lee SM, Floyd RA, Park JW,. 1998. Thiol-dependent metal-catalyzed oxidation of copper, zinc superoxide dismutase Biochim Biophys Acta 1387: 249-256.
    • (1998) Biochim Biophys Acta , vol.1387 , pp. 249-256
    • Kwon, O.J.1    Lee, S.M.2    Floyd, R.A.3    Park, J.W.4
  • 83
    • 33644846943 scopus 로고    scopus 로고
    • Method to site-specifically identify and quantitate carbonyl end products of protein oxidation using oxidation-dependent element coded affinity tags (O-ECAT) and nanoliquid chromatography Fourier transform mass spectrometry
    • Lee S, Young NL, Whetstone PA, Cheal SM, Benner WH, Lebrilla CB, Meares CF,. 2006. Method to site-specifically identify and quantitate carbonyl end products of protein oxidation using oxidation-dependent element coded affinity tags (O-ECAT) and nanoliquid chromatography Fourier transform mass spectrometry. J Proteome Res 5: 539-547.
    • (2006) J Proteome Res , vol.5 , pp. 539-547
    • Lee, S.1    Young, N.L.2    Whetstone, P.A.3    Cheal, S.M.4    Benner, W.H.5    Lebrilla, C.B.6    Meares, C.F.7
  • 84
    • 0021100174 scopus 로고
    • Oxidative modification of glutamine synthetase. I. Inactivation is due to loss of one histidine residue
    • Levine RL,. 1983. Oxidative modification of glutamine synthetase. I. Inactivation is due to loss of one histidine residue. J Biol Chem 258: 11823-11827.
    • (1983) J Biol Chem , vol.258 , pp. 11823-11827
    • Levine, R.L.1
  • 85
    • 84889399538 scopus 로고    scopus 로고
    • Carbonylated proteins and their implication in physiology and pathology
    • Dalle-Donne I. Scaloni A. Butterfield D.A. editors. United States of America: Wiley-Interscience
    • Levine RL, Stadtman ER,. 2006. Carbonylated proteins and their implication in physiology and pathology. In:, Dalle-Donne I, Scaloni A, Butterfield DA, editors. Redox proteomics: From protein modifications to cellular dysfunction and diseases. United States of America: Wiley-Interscience. pp 123-168.
    • (2006) Redox Proteomics: From Protein Modifications to Cellular Dysfunction and Diseases , pp. 123-168
    • Levine, R.L.1    Stadtman, E.R.2
  • 86
  • 87
    • 74549184412 scopus 로고    scopus 로고
    • The polarisome is required for segregation and retrograde transport of protein aggregates
    • Liu B, Larsson L, Caballero A, Hao X, Oling D, Grantham J, Nyström T,. 2010. The polarisome is required for segregation and retrograde transport of protein aggregates. Cell 140: 257-267.
    • (2010) Cell , vol.140 , pp. 257-267
    • Liu, B.1    Larsson, L.2    Caballero, A.3    Hao, X.4    Oling, D.5    Grantham, J.6    Nyström, T.7
  • 89
    • 77949776207 scopus 로고    scopus 로고
    • Profiling carbonylated proteins in human plasma
    • Madian AG, Regnier FE,. 2010a. Profiling carbonylated proteins in human plasma. J Proteome Res 9: 1330-1343.
    • (2010) J Proteome Res , vol.9 , pp. 1330-1343
    • Madian, A.G.1    Regnier, F.E.2
  • 90
    • 77955455232 scopus 로고    scopus 로고
    • Proteomic identification of carbonylated proteins and their oxidation sites
    • Madian AG, Regnier FE,. 2010b. Proteomic identification of carbonylated proteins and their oxidation sites. J Proteome Res 9: 3766-3780.
    • (2010) J Proteome Res , vol.9 , pp. 3766-3780
    • Madian, A.G.1    Regnier, F.E.2
  • 92
    • 4344604345 scopus 로고    scopus 로고
    • Selectivity of protein carbonylation in the apoptotic response to oxidative stress associated with photodynamic therapy: A cell biochemical and proteomic investigation
    • Magi B, Ettorre A, Liberatori S, Bini L, Andreassi M, Frosali S, Neri P, Pallini V, Di Stefano A,. 2004. Selectivity of protein carbonylation in the apoptotic response to oxidative stress associated with photodynamic therapy: A cell biochemical and proteomic investigation. Cell Death Differ 11: 842-852.
    • (2004) Cell Death Differ , vol.11 , pp. 842-852
    • Magi, B.1    Ettorre, A.2    Liberatori, S.3    Bini, L.4    Andreassi, M.5    Frosali, S.6    Neri, P.7    Pallini, V.8    Di Stefano, A.9
  • 93
    • 53849102546 scopus 로고    scopus 로고
    • Carbonylated proteins are detectable only in a degradation-resistant aggregate state in Escherichia coli
    • Maisonneuve E, Fraysse L, Lignon S, Capron L, Dukan S,. 2008. Carbonylated proteins are detectable only in a degradation-resistant aggregate state in Escherichia coli. J Bacteriol 190: 6609-6614.
    • (2008) J Bacteriol , vol.190 , pp. 6609-6614
    • Maisonneuve, E.1    Fraysse, L.2    Lignon, S.3    Capron, L.4    Dukan, S.5
  • 97
    • 75949083202 scopus 로고    scopus 로고
    • Protein targets of oxidative damage in human neurodegenerative diseases with abnormal protein aggregates
    • Martínez A, Portero-Otin M, Pamplona R, Ferrer I,. 2010. Protein targets of oxidative damage in human neurodegenerative diseases with abnormal protein aggregates. Brain Pathol 20: 281-297.
    • (2010) Brain Pathol , vol.20 , pp. 281-297
    • Martínez, A.1    Portero-Otin, M.2    Pamplona, R.3    Ferrer, I.4
  • 99
    • 0035044082 scopus 로고    scopus 로고
    • Chronological lifespan of stationary phase yeast cells; A model for investigating the factors that might influence the ageing of postmitotic tissues in higher organisms
    • McLean M, Harris N, Piper PW,. 2001. Chronological lifespan of stationary phase yeast cells; a model for investigating the factors that might influence the ageing of postmitotic tissues in higher organisms. Yeast 18: 499-509.
    • (2001) Yeast , vol.18 , pp. 499-509
    • McLean, M.1    Harris, N.2    Piper, P.W.3
  • 100
    • 34247464726 scopus 로고    scopus 로고
    • Identification of carbonylated proteins from enriched rat skeletal muscle mitochondria using affinity chromatography-stable isotope labeling and tandem mass spectrometry
    • Meany DL, Xie H, Thompson LV, Arriaga EA, Griffin TJ,. 2007. Identification of carbonylated proteins from enriched rat skeletal muscle mitochondria using affinity chromatography-stable isotope labeling and tandem mass spectrometry. Proteomics 7: 1150-1163.
    • (2007) Proteomics , vol.7 , pp. 1150-1163
    • Meany, D.L.1    Xie, H.2    Thompson, L.V.3    Arriaga, E.A.4    Griffin, T.J.5
  • 101
    • 33750350410 scopus 로고    scopus 로고
    • Identification and quantification of protein carbonylation using light and heavy isotope labeled Girard's P reagent
    • Mirzaei H, Regnier F,. 2006a. Identification and quantification of protein carbonylation using light and heavy isotope labeled Girard's P reagent. J Chromatogr A 1134: 122-133.
    • (2006) J Chromatogr A , vol.1134 , pp. 122-133
    • Mirzaei, H.1    Regnier, F.2
  • 102
    • 33748289451 scopus 로고    scopus 로고
    • Creation of allotypic active sites during oxidative stress
    • Mirzaei H, Regnier F,. 2006b. Creation of allotypic active sites during oxidative stress. J Proteome Res 5: 2159-2168.
    • (2006) J Proteome Res , vol.5 , pp. 2159-2168
    • Mirzaei, H.1    Regnier, F.2
  • 103
    • 33846025822 scopus 로고    scopus 로고
    • Identification of yeast oxidized proteins: Chromatographic top-down approach for identification of carbonylated, fragmented and cross-linked proteins in yeast
    • Mirzaei H, Regnier F,. 2007. Identification of yeast oxidized proteins: Chromatographic top-down approach for identification of carbonylated, fragmented and cross-linked proteins in yeast. J Chromatogr A 1141: 22-31.
    • (2007) J Chromatogr A , vol.1141 , pp. 22-31
    • Mirzaei, H.1    Regnier, F.2
  • 104
    • 42049099009 scopus 로고    scopus 로고
    • Identification of oxidized proteins in rat plasma using avidin chromatography and tandem mass spectrometry
    • Mirzaei H, Baena B, Barbas C, Regnier F,. 2008. Identification of oxidized proteins in rat plasma using avidin chromatography and tandem mass spectrometry. Proteomics 8: 1516-1527.
    • (2008) Proteomics , vol.8 , pp. 1516-1527
    • Mirzaei, H.1    Baena, B.2    Barbas, C.3    Regnier, F.4
  • 105
    • 80053041158 scopus 로고    scopus 로고
    • Protein carbonylation and metal-catalyzed protein oxidation in a cellular perspective
    • Møller IM, Rogowska-Wrzesinska A, Rao RS,. 2011. Protein carbonylation and metal-catalyzed protein oxidation in a cellular perspective. J Proteomics 74: 2228-2242.
    • (2011) J Proteomics , vol.74 , pp. 2228-2242
    • Møller, I.M.1    Rogowska-Wrzesinska, A.2    Rao, R.S.3
  • 106
    • 0027373145 scopus 로고
    • Age-related changes in human ceruloplasmin. Evidence for oxidative modifications
    • Musci G, Bonaccorsi di Patti MC, Fagiolo U, Calabrese L,. 1993. Age-related changes in human ceruloplasmin. Evidence for oxidative modifications. J Biol Chem 268: 13388-13395.
    • (1993) J Biol Chem , vol.268 , pp. 13388-13395
    • Musci, G.1    Bonaccorsi Di Patti, M.C.2    Fagiolo, U.3    Calabrese, L.4
  • 107
    • 1642422767 scopus 로고    scopus 로고
    • Mitochondrial enzyme activities as biochemical markers of aging
    • Navarro A,. 2004. Mitochondrial enzyme activities as biochemical markers of aging. Mol Aspects Med 25: 37-48.
    • (2004) Mol Aspects Med , vol.25 , pp. 37-48
    • Navarro, A.1
  • 108
    • 36749065049 scopus 로고    scopus 로고
    • Identification of enzymes and regulatory proteins in Escherichia coli that are oxidized under nitrogen, carbon, or phosphate starvation
    • Noda Y, Berlett BS, Stadtman ER, Aponte A, Morgan M, Shen RF,. 2007. Identification of enzymes and regulatory proteins in Escherichia coli that are oxidized under nitrogen, carbon, or phosphate starvation. Proc Natl Acad Sci USA 104: 18456-18460.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 18456-18460
    • Noda, Y.1    Berlett, B.S.2    Stadtman, E.R.3    Aponte, A.4    Morgan, M.5    Shen, R.F.6
  • 109
  • 110
    • 0036725380 scopus 로고    scopus 로고
    • Translational fidelity, protein oxidation, and senescence: Lessons from bacteria
    • Nyström T,. 2002. Translational fidelity, protein oxidation, and senescence: lessons from bacteria. Ageing Res Rev 1: 693-703.
    • (2002) Ageing Res Rev , vol.1 , pp. 693-703
    • Nyström, T.1
  • 111
    • 17844403545 scopus 로고    scopus 로고
    • Role of oxidative carbonylation in protein quality control and senescence
    • Nyström T,. 2005. Role of oxidative carbonylation in protein quality control and senescence. EMBO J 24: 1311-1317.
    • (2005) EMBO J , vol.24 , pp. 1311-1317
    • Nyström, T.1
  • 112
    • 0037218503 scopus 로고    scopus 로고
    • Proteomic method detects oxidatively induced protein carbonyls in muscles of a diabetes model Otsuka Long-Evans Tokushima Fatty (OLETF) rat
    • Oh-Ishi M, Ueno T, Maeda T,. 2003. Proteomic method detects oxidatively induced protein carbonyls in muscles of a diabetes model Otsuka Long-Evans Tokushima Fatty (OLETF) rat. Free Radic Biol Med 34: 11-22.
    • (2003) Free Radic Biol Med , vol.34 , pp. 11-22
    • Oh-Ishi, M.1    Ueno, T.2    Maeda, T.3
  • 115
    • 20444373701 scopus 로고    scopus 로고
    • Proteins in human brain cortex are modified by oxidation, glycoxidation, and lipoxidation. Effects of Alzheimer disease and identification of lipoxidation targets
    • Pamplona R, Dalfo E, Ayala V, Bellmunt MJ, Prat J, Ferrer I, Portero-Otin M,. 2005. Proteins in human brain cortex are modified by oxidation, glycoxidation, and lipoxidation. Effects of Alzheimer disease and identification of lipoxidation targets. J Biol Chem 280: 21522-21530.
    • (2005) J Biol Chem , vol.280 , pp. 21522-21530
    • Pamplona, R.1    Dalfo, E.2    Ayala, V.3    Bellmunt, M.J.4    Prat, J.5    Ferrer, I.6    Portero-Otin, M.7
  • 116
    • 0030974273 scopus 로고    scopus 로고
    • Ozone-induced oxidative stress: Mechanisms of action and reaction
    • Pell EJ, Schlagnhaufer CD, Arteca RN,. 1997. Ozone-induced oxidative stress: Mechanisms of action and reaction. Physiol Plant 100: 264-273.
    • (1997) Physiol Plant , vol.100 , pp. 264-273
    • Pell, E.J.1    Schlagnhaufer, C.D.2    Arteca, R.N.3
  • 118
    • 84866848255 scopus 로고    scopus 로고
    • 4-Hydroxy-2-nonenal, a reactive product of lipid peroxidation, and neurodegenerative diseases: A toxic combination illuminated by redox proteomics studies
    • Perluigi M, Coccia R, Butterfield DA,. 2012. 4-Hydroxy-2-nonenal, a reactive product of lipid peroxidation, and neurodegenerative diseases: A toxic combination illuminated by redox proteomics studies. Antioxid Redox Signal 17: 1590-1609.
    • (2012) Antioxid Redox Signal , vol.17 , pp. 1590-1609
    • Perluigi, M.1    Coccia, R.2    Butterfield, D.A.3
  • 120
    • 14544284095 scopus 로고    scopus 로고
    • Proteomic analysis of specific brain proteins in aged SAMP8 mice treated with alpha-lipoic acid: Implications for aging and age-related neurodegenerative disorders
    • Poon HF, Farr SA, Thongboonkerd V, Lynn BC, Banks WA, Morley JE, Klein JB, Butterfield DA,. 2005a. Proteomic analysis of specific brain proteins in aged SAMP8 mice treated with alpha-lipoic acid: Implications for aging and age-related neurodegenerative disorders. Neurochem Int 46: 159-168.
    • (2005) Neurochem Int , vol.46 , pp. 159-168
    • Poon, H.F.1    Farr, S.A.2    Thongboonkerd, V.3    Lynn, B.C.4    Banks, W.A.5    Morley, J.E.6    Klein, J.B.7    Butterfield, D.A.8
  • 121
    • 22744455017 scopus 로고    scopus 로고
    • Proteomic identification of less oxidized brain proteins in aged senescence-accelerated mice following administration of antisense oligonucleotide directed at the Abeta region of amyloid precursor protein
    • Poon HF, Farr SA, Banks WA, Pierce WM, Klein JB, Morley JE, Butterfield DA,. 2005b. Proteomic identification of less oxidized brain proteins in aged senescence-accelerated mice following administration of antisense oligonucleotide directed at the Abeta region of amyloid precursor protein. Mol Brain Res 138: 8-16.
    • (2005) Mol Brain Res , vol.138 , pp. 8-16
    • Poon, H.F.1    Farr, S.A.2    Banks, W.A.3    Pierce, W.M.4    Klein, J.B.5    Morley, J.E.6    Butterfield, D.A.7
  • 122
    • 33646517324 scopus 로고    scopus 로고
    • Quantitative proteomics analysis of differential protein expression and oxidative modification of specific proteins in the brains of old mice
    • Poon HF, Vaishnav RA, Getchell TV, Getchell ML, Butterfield DA,. 2006a. Quantitative proteomics analysis of differential protein expression and oxidative modification of specific proteins in the brains of old mice. Neurobiol Aging 27: 1010-1019.
    • (2006) Neurobiol Aging , vol.27 , pp. 1010-1019
    • Poon, H.F.1    Vaishnav, R.A.2    Getchell, T.V.3    Getchell, M.L.4    Butterfield, D.A.5
  • 123
    • 33646699107 scopus 로고    scopus 로고
    • Proteomics analyses of specific protein oxidation and protein expression in aged rat brain and its modulation by L-acetylcarnitine: Insights into the mechanisms of action of this proposed therapeutic agent for CNS disorders associated with oxidative stress
    • Poon HF, Calabrese V, Calvani M, Butterfield DA,. 2006b. Proteomics analyses of specific protein oxidation and protein expression in aged rat brain and its modulation by L-acetylcarnitine: Insights into the mechanisms of action of this proposed therapeutic agent for CNS disorders associated with oxidative stress. Antioxid Redox Signal 8: 381-394.
    • (2006) Antioxid Redox Signal , vol.8 , pp. 381-394
    • Poon, H.F.1    Calabrese, V.2    Calvani, M.3    Butterfield, D.A.4
  • 124
    • 33646708957 scopus 로고    scopus 로고
    • Proteomics analysis provides insight into caloric restriction mediated oxidation and expression of brain proteins associated with age-related impaired cellular processes: Mitochondrial dysfunction, glutamate dysregulation and impaired protein synthesis
    • Poon HF, Shepherd HM, Reed TT, Calabrese V, Stella AM, Pennisi G, Cai J, Pierce WM, Klein JB, Butterfield DA,. 2006c. Proteomics analysis provides insight into caloric restriction mediated oxidation and expression of brain proteins associated with age-related impaired cellular processes: Mitochondrial dysfunction, glutamate dysregulation and impaired protein synthesis. Neurobiol Aging 27: 1020-1034.
    • (2006) Neurobiol Aging , vol.27 , pp. 1020-1034
    • Poon, H.F.1    Shepherd, H.M.2    Reed, T.T.3    Calabrese, V.4    Stella, A.M.5    Pennisi, G.6    Cai, J.7    Pierce, W.M.8    Klein, J.B.9    Butterfield, D.A.10
  • 126
    • 43849112193 scopus 로고    scopus 로고
    • Chloroquine mediates specific proteome oxidative damage across the erythrocytic cycle of resistant Plasmodium falciparum
    • Radfar A, Diez A, Bautista JM,. 2008. Chloroquine mediates specific proteome oxidative damage across the erythrocytic cycle of resistant Plasmodium falciparum. Free Radic Biol Med 44: 2034-2042.
    • (2008) Free Radic Biol Med , vol.44 , pp. 2034-2042
    • Radfar, A.1    Diez, A.2    Bautista, J.M.3
  • 127
    • 53049084651 scopus 로고    scopus 로고
    • Proteome-wide characterization of seed aging in Arabidopsis: A comparison between artificial and natural aging protocols
    • Rajjou L, Lovigny Y, Groot SPC, Belghazi M, Job C, Job D,. 2008. Proteome-wide characterization of seed aging in Arabidopsis: A comparison between artificial and natural aging protocols. Plant Physiol 148: 620-641.
    • (2008) Plant Physiol , vol.148 , pp. 620-641
    • Rajjou, L.1    Lovigny, Y.2    Groot, S.P.C.3    Belghazi, M.4    Job, C.5    Job, D.6
  • 128
    • 45349087130 scopus 로고    scopus 로고
    • Effect of caloric restriction in non-obese humans on physiological, psychological and behavioral outcomes
    • Redman LM, Martin CK, Williamson DA, Ravussin E,. 2008. Effect of caloric restriction in non-obese humans on physiological, psychological and behavioral outcomes. Physiol Behav 94: 643-648.
    • (2008) Physiol Behav , vol.94 , pp. 643-648
    • Redman, L.M.1    Martin, C.K.2    Williamson, D.A.3    Ravussin, E.4
  • 129
    • 80052261937 scopus 로고    scopus 로고
    • Lipid peroxidation and neurodegenerative disease
    • Reed TT,. 2011. Lipid peroxidation and neurodegenerative disease. Free Radic Biol Med 51: 1302-1319.
    • (2011) Free Radic Biol Med , vol.51 , pp. 1302-1319
    • Reed, T.T.1
  • 130
    • 0035793088 scopus 로고    scopus 로고
    • Glutamic and aminoadipic semialdehydes are the main carbonyl products of metal-catalyzed oxidation of proteins
    • Requena JR, Chao CC, Levine RL, Stadtman ER,. 2001. Glutamic and aminoadipic semialdehydes are the main carbonyl products of metal-catalyzed oxidation of proteins. Proc Natl Acad Sci USA 98: 69-74.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 69-74
    • Requena, J.R.1    Chao, C.C.2    Levine, R.L.3    Stadtman, E.R.4
  • 131
    • 3843151554 scopus 로고    scopus 로고
    • Oxidative damage to specific proteins in replicative and chronological-aged Saccharomyces cerevisiae: Common targets and prevention by calorie restriction
    • Reverter-Branchat G, Cabiscol E, Tamarit J, Ros J,. 2004. Oxidative damage to specific proteins in replicative and chronological-aged Saccharomyces cerevisiae: Common targets and prevention by calorie restriction. J Biol Chem 279: 31983-31989.
    • (2004) J Biol Chem , vol.279 , pp. 31983-31989
    • Reverter-Branchat, G.1    Cabiscol, E.2    Tamarit, J.3    Ros, J.4
  • 133
    • 0040932016 scopus 로고    scopus 로고
    • Grx5 glutaredoxin plays a central role in protection against protein oxidative damage in Saccharomyces cerevisiae
    • Rodríguez-Manzaneque MT, Ros J, Cabiscol E, Sorribas A, Herrero E,. 1999. Grx5 glutaredoxin plays a central role in protection against protein oxidative damage in Saccharomyces cerevisiae. Mol Cell Biol 19: 8180-8190.
    • (1999) Mol Cell Biol , vol.19 , pp. 8180-8190
    • Rodríguez-Manzaneque, M.T.1    Ros, J.2    Cabiscol, E.3    Sorribas, A.4    Herrero, E.5
  • 134
    • 34249043563 scopus 로고    scopus 로고
    • Proteomic mapping of 4-hydroxynonenal protein modification sites by solid-phase
    • Roe MR, Xie H, Bandhakavi S, Griffin TJ,. 2007. Proteomic mapping of 4-hydroxynonenal protein modification sites by solid-phase. Anal Chem 79: 3747-3756.
    • (2007) Anal Chem , vol.79 , pp. 3747-3756
    • Roe, M.R.1    Xie, H.2    Bandhakavi, S.3    Griffin, T.J.4
  • 135
    • 77953911842 scopus 로고    scopus 로고
    • Targeted 18-O-labeling for improved proteomic analysis of carbonylated peptides by mass spectrometry
    • Roe MR, McGowan TF, Thompson LV, Griffin TJ,. 2010. Targeted 18-O-labeling for improved proteomic analysis of carbonylated peptides by mass spectrometry. J Am Soc Mass Spectrom 21: 1190-1203.
    • (2010) J Am Soc Mass Spectrom , vol.21 , pp. 1190-1203
    • Roe, M.R.1    McGowan, T.F.2    Thompson, L.V.3    Griffin, T.J.4
  • 136
    • 33845390864 scopus 로고    scopus 로고
    • Protein adducts generated from products of lipid oxidation: Focus on HNE and one
    • Sayre LM, Lin D, Yuan Q, Zhu X, Tang X,. 2006. Protein adducts generated from products of lipid oxidation: Focus on HNE and one. Drug Metab Rev 38: 651-675.
    • (2006) Drug Metab Rev , vol.38 , pp. 651-675
    • Sayre, L.M.1    Lin, D.2    Yuan, Q.3    Zhu, X.4    Tang, X.5
  • 137
    • 0021368004 scopus 로고
    • Oxygen effect in radiolysis of proteins. Part 2. Bovine serum albumin
    • Schuessler H, Schilling K,. 1984. Oxygen effect in radiolysis of proteins. Part 2. Bovine serum albumin. Int J Radiat Biol 45: 267-281.
    • (1984) Int J Radiat Biol , vol.45 , pp. 267-281
    • Schuessler, H.1    Schilling, K.2
  • 138
    • 34249816781 scopus 로고    scopus 로고
    • 2-Aminoadipic acid is a marker of protein carbonyl oxidation in the aging human skin: Effects of diabetes, renal failure and sepsis
    • Sell DR, Strauch CM, Shen W, Monnier VM,. 2007. 2-Aminoadipic acid is a marker of protein carbonyl oxidation in the aging human skin: Effects of diabetes, renal failure and sepsis. Biochem J 404: 269-277.
    • (2007) Biochem J , vol.404 , pp. 269-277
    • Sell, D.R.1    Strauch, C.M.2    Shen, W.3    Monnier, V.M.4
  • 139
    • 0028143826 scopus 로고
    • Differential susceptibility of plasma proteins to oxidative modification: Examination by Western blot immunoassay
    • Shacter E, Williams JA, Lim M, Levine RL,. 1994. Differential susceptibility of plasma proteins to oxidative modification: Examination by Western blot immunoassay. Free Radic Biol Med 17: 429-437.
    • (1994) Free Radic Biol Med , vol.17 , pp. 429-437
    • Shacter, E.1    Williams, J.A.2    Lim, M.3    Levine, R.L.4
  • 140
    • 0037198057 scopus 로고    scopus 로고
    • Paradigms and pitfalls of yeast longevity research
    • Sinclair D,. 2002. Paradigms and pitfalls of yeast longevity research. Mech Ageing Dev 123: 857-867.
    • (2002) Mech Ageing Dev , vol.123 , pp. 857-867
    • Sinclair, D.1
  • 141
    • 0031459980 scopus 로고    scopus 로고
    • Extrachromosomal rDNA circles-a cause of aging in yeast
    • Sinclair DA, Guarente L,. 1997. Extrachromosomal rDNA circles-a cause of aging in yeast. Cell 91: 1033-1042.
    • (1997) Cell , vol.91 , pp. 1033-1042
    • Sinclair, D.A.1    Guarente, L.2
  • 142
    • 0030038103 scopus 로고    scopus 로고
    • Oxidative stress, caloric restriction, and aging
    • Sohal RS, Weindruch R,. 1996. Oxidative stress, caloric restriction, and aging. Science 273: 59-63.
    • (1996) Science , vol.273 , pp. 59-63
    • Sohal, R.S.1    Weindruch, R.2
  • 143
    • 0029147191 scopus 로고
    • Mitochondrial superoxide and hydrogen peroxide generation, protein oxidative damage, and longevity in different species of flies
    • Sohal RS, Sohal BH, Orr WC,. 1995. Mitochondrial superoxide and hydrogen peroxide generation, protein oxidative damage, and longevity in different species of flies. Free Radic Biol Med 19: 499-504.
    • (1995) Free Radic Biol Med , vol.19 , pp. 499-504
    • Sohal, R.S.1    Sohal, B.H.2    Orr, W.C.3
  • 144
    • 0344084088 scopus 로고    scopus 로고
    • High-throughput proteomic-based identification of oxidatively induced protein carbonylation in mouse brain
    • Soreghan BA, Yang F, Thomas SN, Hsu J, Yang AJ,. 2003. High-throughput proteomic-based identification of oxidatively induced protein carbonylation in mouse brain. Pharm Res 20: 1713-1720.
    • (2003) Pharm Res , vol.20 , pp. 1713-1720
    • Soreghan, B.A.1    Yang, F.2    Thomas, S.N.3    Hsu, J.4    Yang, A.J.5
  • 148
    • 0031831270 scopus 로고    scopus 로고
    • Reactive oxygen-mediated protein oxidation in aging and disease
    • Stadtman ER, Berlett BS,. 1998. Reactive oxygen-mediated protein oxidation in aging and disease. Drug Metab Rev 30: 225-243.
    • (1998) Drug Metab Rev , vol.30 , pp. 225-243
    • Stadtman, E.R.1    Berlett, B.S.2
  • 149
    • 0346100345 scopus 로고    scopus 로고
    • Free radical-mediated oxidation of free amino acids and amino acid residues in proteins
    • Stadtman ER, Levine RL,. 2003. Free radical-mediated oxidation of free amino acids and amino acid residues in proteins. Amino Acids 25: 207-218.
    • (2003) Amino Acids , vol.25 , pp. 207-218
    • Stadtman, E.R.1    Levine, R.L.2
  • 150
    • 79955114990 scopus 로고    scopus 로고
    • Proteomic identification of carbonylated proteins in 1,3-dinitrobenzene neurotoxicity
    • Steiner SR, Philbert MA,. 2011. Proteomic identification of carbonylated proteins in 1,3-dinitrobenzene neurotoxicity. Neurotoxicology 32: 362-373.
    • (2011) Neurotoxicology , vol.32 , pp. 362-373
    • Steiner, S.R.1    Philbert, M.A.2
  • 151
    • 33748423353 scopus 로고    scopus 로고
    • Redox proteomics identification of oxidized proteins in Alzheimer's disease hippocampus and cerebellum: An approach to understand pathological and biochemical alterations in AD
    • Sultana R, Boyd-Kimball D, Poon HF, Cai J, Pierce WM, Klein JB, Merchant M, Markesbery WR, Butterfield DA,. 2006. Redox proteomics identification of oxidized proteins in Alzheimer's disease hippocampus and cerebellum: An approach to understand pathological and biochemical alterations in AD. Neurobiol Aging 27: 1564-1576.
    • (2006) Neurobiol Aging , vol.27 , pp. 1564-1576
    • Sultana, R.1    Boyd-Kimball, D.2    Poon, H.F.3    Cai, J.4    Pierce, W.M.5    Klein, J.B.6    Merchant, M.7    Markesbery, W.R.8    Butterfield, D.A.9
  • 152
    • 0032579371 scopus 로고    scopus 로고
    • Identification of the major oxidatively damaged proteins in Escherichia coli cells exposed to oxidative stress
    • Tamarit J, Cabiscol E, Ros J,. 1998. Identification of the major oxidatively damaged proteins in Escherichia coli cells exposed to oxidative stress. J Biol Chem 273: 3027-3032.
    • (1998) J Biol Chem , vol.273 , pp. 3027-3032
    • Tamarit, J.1    Cabiscol, E.2    Ros, J.3
  • 153
    • 84862190616 scopus 로고    scopus 로고
    • Analysis of oxidative stress-induced protein carbonylation using fluorescent hydrazides
    • Tamarit J, de Hoogh A, Obis E, Alsina D, Cabiscol E, Ros J,. 2012. Analysis of oxidative stress-induced protein carbonylation using fluorescent hydrazides. J Proteomics 75: 3778-3788.
    • (2012) J Proteomics , vol.75 , pp. 3778-3788
    • Tamarit, J.1    De Hoogh, A.2    Obis, E.3    Alsina, D.4    Cabiscol, E.5    Ros, J.6
  • 154
    • 33746268137 scopus 로고    scopus 로고
    • Identification of specific protein carbonylation sites in model oxidations of human serum albumin
    • Temple A, Yen TY, Gronert S,. 2006. Identification of specific protein carbonylation sites in model oxidations of human serum albumin. J Am Soc Mass Spectrom 17: 1172-1180.
    • (2006) J Am Soc Mass Spectrom , vol.17 , pp. 1172-1180
    • Temple, A.1    Yen, T.Y.2    Gronert, S.3
  • 156
    • 0026606054 scopus 로고
    • Modification of histidine residues in proteins by reaction with 4-hydroxynonenal
    • Uchida K, Stadtman ER,. 1992. Modification of histidine residues in proteins by reaction with 4-hydroxynonenal. Proc Natl Acad Sci USA 89: 4544-4548.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 4544-4548
    • Uchida, K.1    Stadtman, E.R.2
  • 158
    • 0028852816 scopus 로고
    • Oxidation of methionyl residues in proteins: Tools, targets, and reversal
    • Vogt W,. 1995. Oxidation of methionyl residues in proteins: Tools, targets, and reversal. Free Radic Biol Med 18: 93-105.
    • (1995) Free Radic Biol Med , vol.18 , pp. 93-105
    • Vogt, W.1
  • 159
    • 76849104804 scopus 로고    scopus 로고
    • Differential proteomics analysis of specific carbonylated proteins in the temporal cortex of aged rats: The deterioration of antioxidant system
    • Wang Q, Zhao X, He S, Liu Y, An M, Ji J,. 2010. Differential proteomics analysis of specific carbonylated proteins in the temporal cortex of aged rats: The deterioration of antioxidant system. Neurochem Res 35: 13-21.
    • (2010) Neurochem Res , vol.35 , pp. 13-21
    • Wang, Q.1    Zhao, X.2    He, S.3    Liu, Y.4    An, M.5    Ji, J.6
  • 160
    • 84857946394 scopus 로고    scopus 로고
    • Quantitation of protein carbonylation by dot blot
    • Wehr NB, Levine RL,. 2012. Quantitation of protein carbonylation by dot blot. Anal Biochem 423: 241-245.
    • (2012) Anal Biochem , vol.423 , pp. 241-245
    • Wehr, N.B.1    Levine, R.L.2
  • 163
    • 0032573066 scopus 로고    scopus 로고
    • Mitochondrial adenine nucleotide translocase is modified oxidatively during aging
    • Yan LJ, Sohal RS,. 1998. Mitochondrial adenine nucleotide translocase is modified oxidatively during aging. Proc Natl Acad Sci USA 95: 12896-12901.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 12896-12901
    • Yan, L.J.1    Sohal, R.S.2
  • 164
    • 0030881686 scopus 로고    scopus 로고
    • Oxidative damage during aging targets mitochondrial aconitase
    • Yan LJ, Levine RL, Sohal RS,. 1997. Oxidative damage during aging targets mitochondrial aconitase. Proc Natl Acad Sci USA 94: 11168-11172.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 11168-11172
    • Yan, L.J.1    Levine, R.L.2    Sohal, R.S.3
  • 165
    • 0034233138 scopus 로고    scopus 로고
    • Effects of aging and hyperoxia on oxidative damage to cytochrome c in the housefly, Musca domestica
    • Yan LJ, Levine RL, Sohal RS,. 2000. Effects of aging and hyperoxia on oxidative damage to cytochrome c in the housefly, Musca domestica. Free Radic Biol Med 29: 90-97.
    • (2000) Free Radic Biol Med , vol.29 , pp. 90-97
    • Yan, L.J.1    Levine, R.L.2    Sohal, R.S.3
  • 166
    • 3042523891 scopus 로고    scopus 로고
    • Proteomic analysis of carbonylated proteins in two-dimensional gel electrophoresis using avidin-fluorescein affinity staining
    • Yoo BS, Regnier FE,. 2004. Proteomic analysis of carbonylated proteins in two-dimensional gel electrophoresis using avidin-fluorescein affinity staining. Electrophoresis 25: 1334-1341.
    • (2004) Electrophoresis , vol.25 , pp. 1334-1341
    • Yoo, B.S.1    Regnier, F.E.2
  • 167
    • 33846548110 scopus 로고    scopus 로고
    • ER stress and diseases
    • Yoshida H,. 2007. ER stress and diseases. FEBS J 274: 630-658.
    • (2007) FEBS J , vol.274 , pp. 630-658
    • Yoshida, H.1


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