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Volumn 66, Issue 2 SUPPL. 1, 2006, Pages

Preferential degradation of oxidized proteins by the 20S proteasome may be inhibited in aging and in inflammatory neuromuscular diseases

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; FREE RADICAL; PROTEASOME; PROTEIN; REACTIVE OXYGEN METABOLITE; UBIQUITIN;

EID: 33644859926     PISSN: 00283878     EISSN: None     Source Type: Journal    
DOI: 10.1212/01.wnl.0000192308.43151.63     Document Type: Conference Paper
Times cited : (69)

References (61)
  • 1
    • 77049308856 scopus 로고
    • Aging: A theory based on free radical and radiation chemistry
    • Harman D. Aging: a theory based on free radical and radiation chemistry. J Gerontol 1956;2:298-300.
    • (1956) J Gerontol , vol.2 , pp. 298-300
    • Harman, D.1
  • 2
    • 0032538346 scopus 로고    scopus 로고
    • Aging of C. elegans: Mosaics and mechanisms
    • Wood WB. Aging of C. elegans: mosaics and mechanisms. Cell 1998;95:147-150.
    • (1998) Cell , vol.95 , pp. 147-150
    • Wood, W.B.1
  • 3
    • 0032908347 scopus 로고    scopus 로고
    • FLP recombinase-mediated induction of Cu/Zn-superoxide dismutase transgene expression can extend the life span of adult Drosophila melanogaster flies
    • Sun J, Tower J. FLP recombinase-mediated induction of Cu/Zn-superoxide dismutase transgene expression can extend the life span of adult Drosophila melanogaster flies. Mol Cell Biol 1999;19:216-228.
    • (1999) Mol Cell Biol , vol.19 , pp. 216-228
    • Sun, J.1    Tower, J.2
  • 4
    • 0035978884 scopus 로고    scopus 로고
    • Insulin-like signaling, metabolism, stress resistance and aging in Caenorhabditis elegans
    • Braeckman BP, Houthoofd K, Vanfleteren JR. Insulin-like signaling, metabolism, stress resistance and aging in Caenorhabditis elegans. Mech Ageing Dev 2001;122:673-693.
    • (2001) Mech Ageing Dev , vol.122 , pp. 673-693
    • Braeckman, B.P.1    Houthoofd, K.2    Vanfleteren, J.R.3
  • 5
    • 0023655369 scopus 로고
    • Protein damage and degradation by oxygen radicals: I. General Aspects
    • Davies KJA. Protein damage and degradation by oxygen radicals: I. General Aspects. J Biol Chem 1987;262:9895-9901.
    • (1987) J Biol Chem , vol.262 , pp. 9895-9901
    • Davies, K.J.A.1
  • 6
    • 0023655531 scopus 로고
    • Protein damage and degradation by oxygen radicals: III. Modification of secondary and tertiary structure
    • Davies KJA, Delsignore ME. Protein damage and degradation by oxygen radicals: III. Modification of secondary and tertiary structure. J Biol Chem 1987;262:9908-9913.
    • (1987) J Biol Chem , vol.262 , pp. 9908-9913
    • Davies, K.J.A.1    Delsignore, M.E.2
  • 7
    • 0023655407 scopus 로고
    • Protein damage and degradation by oxygen radicals: II. Modification of amino acids
    • Davies KJA, Delsignore ME, Lin SW. Protein damage and degradation by oxygen radicals: II. Modification of amino acids. J Biol Chem 1987;262.
    • (1987) J Biol Chem , vol.262
    • Davies, K.J.A.1    Delsignore, M.E.2    Lin, S.W.3
  • 8
    • 0023655449 scopus 로고
    • Protein damage and degradation by oxygen radicals: IV. Degradation of denatured protein
    • Davies KJA, Lin SW, Pacifici RE. Protein damage and degradation by oxygen radicals: IV. Degradation of denatured protein. J Biol Chem 1987;262:9914-9920.
    • (1987) J Biol Chem , vol.262 , pp. 9914-9920
    • Davies, K.J.A.1    Lin, S.W.2    Pacifici, R.E.3
  • 9
    • 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. J Biol Chem 1997;272:20313-20316.
    • (1997) J Biol Chem , vol.272 , pp. 20313-20316
    • Berlett, B.S.1    Stadtman, E.R.2
  • 10
    • 0030988742 scopus 로고    scopus 로고
    • Biochemistry and pathology of radical-mediated protein oxidation
    • Dean RT, Shanlin F, Stocker R, Davies MJ. Biochemistry and pathology of radical-mediated protein oxidation. Biochem J 1997;324:1-18.
    • (1997) Biochem J , vol.324 , pp. 1-18
    • Dean, R.T.1    Shanlin, F.2    Stocker, R.3    Davies, M.J.4
  • 11
    • 0026795635 scopus 로고
    • Protein oxidation and aging
    • Stadtman ER. Protein oxidation and aging. Science 1992;257:1220-1224.
    • (1992) Science , vol.257 , pp. 1220-1224
    • Stadtman, E.R.1
  • 12
    • 0030952676 scopus 로고    scopus 로고
    • Modification of protein surface hydrophobicity and methionine oxidation by oxidative systems
    • USA
    • Chao C, Ma Y, Stadtman ER. Modification of protein surface hydrophobicity and methionine oxidation by oxidative systems. Proc Natl Acad Sci USA 1997;94:2969-2974.
    • (1997) Proc Natl Acad Sci , vol.94 , pp. 2969-2974
    • Chao, C.1    Ma, Y.2    Stadtman, E.R.3
  • 15
    • 0030982143 scopus 로고    scopus 로고
    • Degradation of oxidized proteins in mammalian cells
    • Grune T, Reinheckel T, Davies KJA. Degradation of oxidized proteins in mammalian cells. FASEB J 1997;11:526-534.
    • (1997) FASEB J , vol.11 , pp. 526-534
    • Grune, T.1    Reinheckel, T.2    Davies, K.J.A.3
  • 16
    • 0028885790 scopus 로고
    • The essential function of protein-disulfide isomerase is to unscramble non-native disulfide bonds
    • Laboissiere MC, Sturley SL, Raines RT. The essential function of protein-disulfide isomerase is to unscramble non-native disulfide bonds. J Biol Chem 1995;270:28006-28009.
    • (1995) J Biol Chem , vol.270 , pp. 28006-28009
    • Laboissiere, M.C.1    Sturley, S.L.2    Raines, R.T.3
  • 17
    • 0035968194 scopus 로고    scopus 로고
    • Mechanism of the formation and proteolytic release of H2O2-induced dityrosine and tyrosine oxidation products in hemoglobin and red blood cells
    • Giulivi C, Davies KJ. Mechanism of the formation and proteolytic release of H2O2-induced dityrosine and tyrosine oxidation products in hemoglobin and red blood cells. J Biol Chem 2001;276:24129-24136.
    • (2001) J Biol Chem , vol.276 , pp. 24129-24136
    • Giulivi, C.1    Davies, K.J.2
  • 18
    • 0027414020 scopus 로고
    • Dityrosine and tyrosine oxidation products are endogenous markers for selective proteolysis of oxidatively modified red blood cell hemoglobin by (the 19S) proteasome
    • Giulivi C, Davies KJA. Dityrosine and tyrosine oxidation products are endogenous markers for selective proteolysis of oxidatively modified red blood cell hemoglobin by (the 19S) proteasome. J Biol Chem 1993;268:8752-8759.
    • (1993) J Biol Chem , vol.268 , pp. 8752-8759
    • Giulivi, C.1    Davies, K.J.A.2
  • 19
    • 0028245961 scopus 로고
    • Exposure of hydrophobic moieties promotes the selective degradation of hydrogen peroxide-modified hemoglobin by the multicatalytic proteinase complex, proteasome
    • Giulivi C, Pacifici RE, Davies KJA. Exposure of hydrophobic moieties promotes the selective degradation of hydrogen peroxide-modified hemoglobin by the multicatalytic proteinase complex, proteasome. Arch Bioch Biophys 1994;311:329-341.
    • (1994) Arch Bioch Biophys , vol.311 , pp. 329-341
    • Giulivi, C.1    Pacifici, R.E.2    Davies, K.J.A.3
  • 20
    • 0027417395 scopus 로고
    • Dityrosine, a specific marker for oxidation, is synthesized by the myeloperoxidase-hydrogen peroxide system of human neutrophiles and macrophages
    • Heinecke JW, Li W, Daehnke HL, Goldstein JA. Dityrosine, a specific marker for oxidation, is synthesized by the myeloperoxidase-hydrogen peroxide system of human neutrophiles and macrophages. J. Biol. Chem. 1993;268:4069-4077.
    • (1993) J. Biol. Chem. , vol.268 , pp. 4069-4077
    • Heinecke, J.W.1    Li, W.2    Daehnke, H.L.3    Goldstein, J.A.4
  • 21
    • 0029972278 scopus 로고    scopus 로고
    • Biochemical basis of lipofuscin, ceroid and AGE pigment-like fluorophores
    • DaZhong Y. Biochemical basis of lipofuscin, ceroid and AGE pigment-like fluorophores. Free Radic Biol Med 1996;21:871-888.
    • (1996) Free Radic Biol Med , vol.21 , pp. 871-888
    • Dazhong, Y.1
  • 22
    • 0029984892 scopus 로고    scopus 로고
    • Degradation of oxidized proteins in K562 human hematopoietic cells by proteasome
    • Grune T, Reinheckel T, Davies KJA. Degradation of oxidized proteins in K562 human hematopoietic cells by proteasome. J Biol Chem 1996;271:15504-15509.
    • (1996) J Biol Chem , vol.271 , pp. 15504-15509
    • Grune, T.1    Reinheckel, T.2    Davies, K.J.A.3
  • 23
    • 0028912676 scopus 로고
    • Proteolysis in cultured liver epithelial cells during oxidative stress. Role of the Multicatalytic proteinase complex, proteasome
    • Grune T, Reinheckel T, Joshi M, Davies KJA. Proteolysis in cultured liver epithelial cells during oxidative stress. Role of the Multicatalytic proteinase complex, proteasome. J Biol Chem 1995;270:2344-2351.
    • (1995) J Biol Chem , vol.270 , pp. 2344-2351
    • Grune, T.1    Reinheckel, T.2    Joshi, M.3    Davies, K.J.A.4
  • 24
    • 0027324284 scopus 로고
    • Hydrophobicity as the signal for selective degradation of hydroxyl radical-modified hemoglobin by the multicatalytic proteinase complex, proteasome
    • Pacifici RE, Kono Y, Davies KJA. Hydrophobicity as the signal for selective degradation of hydroxyl radical-modified hemoglobin by the multicatalytic proteinase complex, proteasome. J Biol Chem 1993;268:15405-15411.
    • (1993) J Biol Chem , vol.268 , pp. 15405-15411
    • Pacifici, R.E.1    Kono, Y.2    Davies, K.J.A.3
  • 25
    • 0024843661 scopus 로고
    • Macroxyproteinase (M.O.P.): A 670 kDa proteinase complex that selectively degrades oxidatively denatured proteins in red blood cells
    • Pacifici RE, Salo DC, Davies KJA. Macroxyproteinase (M.O.P.): A 670 kDa proteinase complex that selectively degrades oxidatively denatured proteins in red blood cells. Free RadicBiol Med 1989;7:521-536.
    • (1989) Free RadicBiol Med , vol.7 , pp. 521-536
    • Pacifici, R.E.1    Salo, D.C.2    Davies, K.J.A.3
  • 26
    • 0025358959 scopus 로고
    • Superoxide dismutase undergoes proteolysis and fragmentation following oxidative modification and inactivation
    • Salo DC, Pacifici RE, Lin SW, Giulivi C, Davies KJA. Superoxide dismutase undergoes proteolysis and fragmentation following oxidative modification and inactivation. J Biol Chem 1990;265:11919-11927.
    • (1990) J Biol Chem , vol.265 , pp. 11919-11927
    • Salo, D.C.1    Pacifici, R.E.2    Lin, S.W.3    Giulivi, C.4    Davies, K.J.A.5
  • 27
    • 0021928777 scopus 로고
    • Preferential degradation of the oxidatively modified form of glutamine synthetase by intracellular mammalian proteases
    • Rivett AJ. Preferential degradation of the oxidatively modified form of glutamine synthetase by intracellular mammalian proteases. J Biol Chem 1985;260:300-305.
    • (1985) J Biol Chem , vol.260 , pp. 300-305
    • Rivett, A.J.1
  • 28
    • 0022374263 scopus 로고
    • Purification of a liver alkaline protease which degrades oxidatively modified glutamine synthetase. Characterization as a high molecular weight cysteine protease
    • Rivett AJ. Purification of a liver alkaline protease which degrades oxidatively modified glutamine synthetase. Characterization as a high molecular weight cysteine protease. J Biol Chem 1985;260:12600-12606.
    • (1985) J Biol Chem , vol.260 , pp. 12600-12606
    • Rivett, A.J.1
  • 29
    • 0023654044 scopus 로고
    • Purification of a protease from Escherichia coli with specificity for oxidized glutamine synthetase
    • Roseman JE, Levine RL. Purification of a protease from Escherichia coli with specificity for oxidized glutamine synthetase. J Biol Chem 1987;262:2101-2110.
    • (1987) J Biol Chem , vol.262 , pp. 2101-2110
    • Roseman, J.E.1    Levine, R.L.2
  • 30
    • 0026555037 scopus 로고
    • Proteases and proteolysis in the lysosome
    • Bohley P, Seglen PO. Proteases and proteolysis in the lysosome. Experentia 1992;48:151-157.
    • (1992) Experentia , vol.48 , pp. 151-157
    • Bohley, P.1    Seglen, P.O.2
  • 31
    • 0023546546 scopus 로고
    • Calcium-dependent proteases: An enzyme system active at cellular membranes?
    • Mellgren RL. Calcium-dependent proteases: an enzyme system active at cellular membranes? FASEB J 1987;1:110-115.
    • (1987) FASEB J , vol.1 , pp. 110-115
    • Mellgren, R.L.1
  • 32
    • 0000701060 scopus 로고    scopus 로고
    • Structure and functions of the 20S and 26S proteasomes
    • Coux O, Tanaka K, Goldberg AL. Structure and functions of the 20S and 26S proteasomes. Ann Rev Biochem 1996;29:10289-10297.
    • (1996) Ann Rev Biochem , vol.29 , pp. 10289-10297
    • Coux, O.1    Tanaka, K.2    Goldberg, A.L.3
  • 33
    • 0035072229 scopus 로고    scopus 로고
    • Degradation of oxidized proteins by the 20S proteasome
    • Davies KJ. Degradation of oxidized proteins by the 20S proteasome. Biochimie 2001;83:301-310.
    • (2001) Biochimie , vol.83 , pp. 301-310
    • Davies, K.J.1
  • 34
    • 0023766518 scopus 로고
    • Modulation of the hydrophobicity of glutamine synthetase by mixed- Function oxidation
    • Cervera J, Levine RL. Modulation of the hydrophobicity of glutamine synthetase by mixed- function oxidation. FASEB J 1988;2:2591-2595.
    • (1988) FASEB J , vol.2 , pp. 2591-2595
    • Cervera, J.1    Levine, R.L.2
  • 35
    • 0019195859 scopus 로고
    • Cation-sensitive neutral endopeptidase: Isolation and specificity of the bovine pituitary enzyme
    • Wilk S, Orlowski M. Cation-sensitive neutral endopeptidase: Isolation and specificity of the bovine pituitary enzyme. J Neurochem 1980;35:1172-1182.
    • (1980) J Neurochem , vol.35 , pp. 1172-1182
    • Wilk, S.1    Orlowski, M.2
  • 36
    • 0030977793 scopus 로고    scopus 로고
    • Inhibition of multicatalytic proteinase (proteasome) by 4-hydroxynonenal cross-linked protein
    • Friguet B, Swezda LI. Inhibition of multicatalytic proteinase (proteasome) by 4-hydroxynonenal cross-linked protein. FEBS Lett 1997;405:21-25.
    • (1997) FEBS Lett , vol.405 , pp. 21-25
    • Friguet, B.1    Swezda, L.I.2
  • 37
    • 0033712579 scopus 로고    scopus 로고
    • 4-Hydroxynonenal-modified amyloid-beta peptide inhibits the proteasome: Possible importance in Alzheimer's disease
    • Shringarpure R, Grune T, Sitte N, Davies KJA. 4-Hydroxynonenal-modified amyloid-beta peptide inhibits the proteasome: possible importance in Alzheimer's disease. Cell Mol Life Sci 2000;57:1802-1808.
    • (2000) Cell Mol Life Sci , vol.57 , pp. 1802-1808
    • Shringarpure, R.1    Grune, T.2    Sitte, N.3    Davies, K.J.A.4
  • 39
    • 0033674181 scopus 로고    scopus 로고
    • Protein oxidation and degradation during cellular senescence of human BJ fibroblasts: Part II- Aging of nondividing cells
    • Sitte N, Merker K von Zglinicki T, Davies KJA, Grune T. Protein oxidation and degradation during cellular senescence of human BJ fibroblasts: part II- aging of nondividing cells. FASEB J 2000;14:2503-2510.
    • (2000) FASEB J , vol.14 , pp. 2503-2510
    • Sitte, N.1    Merker, K.2    Von Zglinicki, T.3    Davies, K.J.A.4    Grune, T.5
  • 40
    • 0033673408 scopus 로고    scopus 로고
    • Protein oxidation and degradation during cellular senescence of human BJ fibroblasts: Part I-effects of proliferative senescence
    • Sitte N, Merker K, von Zglinicki T, Grune T, Davies KJA. Protein oxidation and degradation during cellular senescence of human BJ fibroblasts: part I-effects of proliferative senescence. FASEB J 2000;14:2495-2502.
    • (2000) FASEB J , vol.14 , pp. 2495-2502
    • Sitte, N.1    Merker, K.2    Von Zglinicki, T.3    Grune, T.4    Davies, K.J.A.5
  • 41
    • 0027358327 scopus 로고
    • Inefficient degradation of oxidized regions of protein molecules
    • Grant AJ, Jessup W, Dean RT. Inefficient degradation of oxidized regions of protein molecules. Free Radic Res Commun 1993;18:259-267.
    • (1993) Free Radic Res Commun , vol.18 , pp. 259-267
    • Grant, A.J.1    Jessup, W.2    Dean, R.T.3
  • 42
    • 0034640520 scopus 로고    scopus 로고
    • Hybrid Proteasomes. Induction by interferon-gamma and contribution to ATP-dependent proteolysis
    • Tanahashi N, Murakami Y, Minami Y, Hendil KB, Tanaka K. Hybrid Proteasomes. Induction by interferon-gamma and contribution to ATP-dependent proteolysis. J Biol Chem 2000;275:14336-14345.
    • (2000) J Biol Chem , vol.275 , pp. 14336-14345
    • Tanahashi, N.1    Murakami, Y.2    Minami, Y.3    Hendil, K.B.4    Tanaka, K.5
  • 43
    • 0034652143 scopus 로고    scopus 로고
    • Subcellular localization of the proteasomes and their regulatory complexes in mammalian cells
    • Brooks P, Fuertes G, Murray RZ, et al. Subcellular localization of the proteasomes and their regulatory complexes in mammalian cells. Biochem J 2000;346:155-161.
    • (2000) Biochem J , vol.346 , pp. 155-161
    • Brooks, P.1    Fuertes, G.2    Murray, R.Z.3
  • 44
    • 0028234770 scopus 로고
    • Distinct 19S and 20S sub-complexes of the 26S proteasome and their distribution in the nucleus and the cytoplasm
    • Peters JM, Franke WW, Kleinschmidt JA. Distinct 19S and 20S sub-complexes of the 26S proteasome and their distribution in the nucleus and the cytoplasm. J Biol Chem 1994;269:7709-7718.
    • (1994) J Biol Chem , vol.269 , pp. 7709-7718
    • Peters, J.M.1    Franke, W.W.2    Kleinschmidt, J.A.3
  • 45
    • 0030724889 scopus 로고    scopus 로고
    • Regulation of ubiquitin-cojugating enzymes by glutathione following oxidative stress
    • Jahngen-Hodge J, Obin MS, Gong X, et al. Regulation of ubiquitin-cojugating enzymes by glutathione following oxidative stress. J Biol Chem 1997;272:28218-28226.
    • (1997) J Biol Chem , vol.272 , pp. 28218-28226
    • Jahngen-Hodge, J.1    Obin, M.S.2    Gong, X.3
  • 47
    • 0034194227 scopus 로고    scopus 로고
    • Differential impairment of 20S and 26S proteasome activities in human hematopoietic K562 cells during oxidative stress
    • Reinheckel T, Ullrich O, Sitte N, Grune T. Differential impairment of 20S and 26S proteasome activities in human hematopoietic K562 cells during oxidative stress. Arch Biochem Biophys 2000;377:65-68.
    • (2000) Arch Biochem Biophys , vol.377 , pp. 65-68
    • Reinheckel, T.1    Ullrich, O.2    Sitte, N.3    Grune, T.4
  • 48
    • 0030881029 scopus 로고    scopus 로고
    • Activity of ubiquitin-dependent pathway in response to oxidative stress
    • Shang F, Gong X, Taylor A. Activity of ubiquitin-dependent pathway in response to oxidative stress. J Biol Chem 1997;272:23086-23093.
    • (1997) J Biol Chem , vol.272 , pp. 23086-23093
    • Shang, F.1    Gong, X.2    Taylor, A.3
  • 49
    • 0034798361 scopus 로고    scopus 로고
    • Protein oxidation and 20S proteasome-dependent proteolysis in mammalian cells
    • Shringarpure R, Grune T, Davies KJA. Protein oxidation and 20S proteasome-dependent proteolysis in mammalian cells. Cell Mol Life Sci 2001;58:1442-1450.
    • (2001) Cell Mol Life Sci , vol.58 , pp. 1442-1450
    • Shringarpure, R.1    Grune, T.2    Davies, K.J.A.3
  • 50
    • 0037414834 scopus 로고    scopus 로고
    • Ubiquitin-conjugation is not required for the degradation of oxidized proteins by proteasome
    • Shringarpure R, Grune T, Davies KJA. Ubiquitin-conjugation is not required for the degradation of oxidized proteins by proteasome. J Biol Chem 2003;278:311-318.
    • (2003) J Biol Chem , vol.278 , pp. 311-318
    • Shringarpure, R.1    Grune, T.2    Davies, K.J.A.3
  • 51
    • 0025102226 scopus 로고
    • Determination of carbonyl content in oxidatively modified proteins
    • Levine RL, Garland D, Oliver CN, et al. Determination of carbonyl content in oxidatively modified proteins. Methods Enzymol 1990;186:464-478.
    • (1990) Methods Enzymol , vol.186 , pp. 464-478
    • Levine, R.L.1    Garland, D.2    Oliver, C.N.3
  • 52
  • 53
    • 0025832844 scopus 로고
    • Reversal of age-related increase in brain protein oxidation, decrease in enzyme activity, and loss in temporal and spatial memory by chronic administration of the spin-trapping compound N-tert-butyl-alpha- Phenylnitrone
    • U S A
    • Carney JM, Starke-Reed PE, Oliver CN, et al. Reversal of age-related increase in brain protein oxidation, decrease in enzyme activity, and loss in temporal and spatial memory by chronic administration of the spin-trapping compound N-tert-butyl-alpha- phenylnitrone. Proc Natl Acad Sci U S A 1991;88:3633-3636.
    • (1991) Proc Natl Acad Sci , vol.88 , pp. 3633-3636
    • Carney, J.M.1    Starke-Reed, P.E.2    Oliver, C.N.3
  • 54
    • 0025790342 scopus 로고
    • Excess brain protein oxidation and enzyme dysfunction in normal aging and in Alzheimer disease
    • U S A
    • Smith CD, Carney JM, Starke-Reed PE, et al. Excess brain protein oxidation and enzyme dysfunction in normal aging and in Alzheimer disease. Proc Natl Acad Sci U S A 1991;88:10540-10543.
    • (1991) Proc Natl Acad Sci , vol.88 , pp. 10540-10543
    • Smith, C.D.1    Carney, J.M.2    Starke-Reed, P.E.3
  • 55
    • 0032579227 scopus 로고    scopus 로고
    • Protein oxidation and enzyme activity decline in old brown Norway rats are reduced by dietary restriction
    • Aksenova MV, Aksenov MY, Carney JM, Butterfield DA. Protein oxidation and enzyme activity decline in old brown Norway rats are reduced by dietary restriction. Mech Ageing Dev 1998;100:157-168.
    • (1998) Mech Ageing Dev , vol.100 , pp. 157-168
    • Aksenova, M.V.1    Aksenov, M.Y.2    Carney, J.M.3    Butterfield, D.A.4
  • 56
    • 0032860808 scopus 로고    scopus 로고
    • The age-related accumulation of protein carbonyl in rat liver correlates with the age-related decline in liver proteolytic activities
    • Vittorini S, Paradiso C, Donati A, et al. The age-related accumulation of protein carbonyl in rat liver correlates with the age-related decline in liver proteolytic activities. J Gerontol A Biol Sci Med Sci 1999;54:B318-323.
    • (1999) J Gerontol a Biol Sci Med Sci , vol.54
    • Vittorini, S.1    Paradiso, C.2    Donati, A.3
  • 57
    • 0023600801 scopus 로고
    • Protein oxidation and loss of protease activity may lead to cataract formation in the aged lens
    • Taylor A, Davies KJ. Protein oxidation and loss of protease activity may lead to cataract formation in the aged lens. Free Radic Biol Med 1987;3:371-377.
    • (1987) Free Radic Biol Med , vol.3 , pp. 371-377
    • Taylor, A.1    Davies, K.J.2
  • 58
    • 0031992238 scopus 로고    scopus 로고
    • Markers of protein oxidation by hydroxyl radical and reactive nitrogen species in tissues of aging rats
    • Leeuwenburgh C, Hansen P, Shaish A, Holloszy JO, Heinecke JW. Markers of protein oxidation by hydroxyl radical and reactive nitrogen species in tissues of aging rats. Am J Physiol 1998;274:R453-461.
    • (1998) Am J Physiol , vol.274
    • Leeuwenburgh, C.1    Hansen, P.2    Shaish, A.3    Holloszy, J.O.4    Heinecke, J.W.5
  • 59
    • 0034122917 scopus 로고    scopus 로고
    • Increase of oxidatively modified protein is associated with a decrease of proteasome activity and content in aging epidermal cells
    • Petropoulos I, Conconi M, Wang X, et al. Increase of oxidatively modified protein is associated with a decrease of proteasome activity and content in aging epidermal cells. J Gerontol A Biol Sci Med Sci 2000;55:B220-227.
    • (2000) J Gerontol A Biol Sci Med Sci , vol.55
    • Petropoulos, I.1    Conconi, M.2    Wang, X.3
  • 60
    • 0028268734 scopus 로고
    • Mitochondrial oxidative damage, hydrogen peroxide release, and aging
    • Sohal RS, Dubey A. Mitochondrial oxidative damage, hydrogen peroxide release, and aging. Free Radic Biol Med 1994;16:621-626.
    • (1994) Free Radic Biol Med , vol.16 , pp. 621-626
    • Sohal, R.S.1    Dubey, A.2
  • 61
    • 0033796250 scopus 로고    scopus 로고
    • Mitochondrial free radical generation, oxidative stress, and aging
    • Cadenas E, Davies KJ. Mitochondrial free radical generation, oxidative stress, and aging. Free Radical Biology & Medicine 2000;29:222-230.
    • (2000) Free Radical Biology & Medicine , vol.29 , pp. 222-230
    • Cadenas, E.1    Davies, K.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.