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Volumn 50, Issue 1, 2011, Pages 86-92

Age-related loss of stress-induced nuclear proteasome activation is due to low PARP-1 activity

Author keywords

Aging; Free radicals; Nucleus; PARP; Proteasome; Protein oxidation

Indexed keywords

NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 1; PROTEASOME;

EID: 78650687669     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2010.10.700     Document Type: Article
Times cited : (28)

References (73)
  • 2
    • 0027417395 scopus 로고
    • Dityrosine, a specific marker of oxidation, is synthesized by the myeloperoxidase-hydrogen peroxide system of human neutrophils and macrophages
    • J.W. Heinecke, W. Li, H.L. Daehnke, and J.A. Goldstein Dityrosine, a specific marker of oxidation, is synthesized by the myeloperoxidase-hydrogen peroxide system of human neutrophils and macrophages J. Biol. Chem. 268 1993 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
  • 5
    • 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
    • J.M. Carney, P.E. Starke-Reed, C.N. Oliver, R.W. Landum, M.S. Cheng, J.F. Wu, and R.A. Floyd 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. USA 88 1991 3633 3636
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 3633-3636
    • Carney, J.M.1    Starke-Reed, P.E.2    Oliver, C.N.3    Landum, R.W.4    Cheng, M.S.5    Wu, J.F.6    Floyd, R.A.7
  • 6
    • 0028136152 scopus 로고
    • Aging and protein oxidative damage
    • S. Agarwal, and R.S. Sohal Aging and protein oxidative damage Mech. Ageing Dev. 75 1994 11 19
    • (1994) Mech. Ageing Dev. , vol.75 , pp. 11-19
    • Agarwal, S.1    Sohal, R.S.2
  • 7
    • 0029972278 scopus 로고    scopus 로고
    • Biochemical basis of lipofuscin, ceroid, and age pigment-like fluorophores
    • D. Yin Biochemical basis of lipofuscin, ceroid, and age pigment-like fluorophores Free Radic. Biol. Med. 21 1996 871 888
    • (1996) Free Radic. Biol. Med. , vol.21 , pp. 871-888
    • Yin, D.1
  • 8
    • 33749675104 scopus 로고    scopus 로고
    • Accumulation of oxidative damage during replicative aging of the yeast Saccharomyces cerevisiae
    • A. Grzelak, E. Macierzyńska, and G. Bartosz Accumulation of oxidative damage during replicative aging of the yeast Saccharomyces cerevisiae Exp. Gerontol. 41 2006 813 818
    • (2006) Exp. Gerontol. , vol.41 , pp. 813-818
    • Grzelak, A.1    Macierzyńska, E.2    Bartosz, G.3
  • 10
    • 33645099414 scopus 로고    scopus 로고
    • Age-associated analysis of oxidative stress parameters in human plasma and erythrocytes
    • L. Gil, W. Siems, B. Mazurek, J. Gross, P. Schroeder, P. Voss, and T. Grune Age-associated analysis of oxidative stress parameters in human plasma and erythrocytes Free Radic. Res. 40 2006 495 505
    • (2006) Free Radic. Res. , vol.40 , pp. 495-505
    • Gil, L.1    Siems, W.2    Mazurek, B.3    Gross, J.4    Schroeder, P.5    Voss, P.6    Grune, T.7
  • 11
    • 0033673408 scopus 로고    scopus 로고
    • Protein oxidation and degradation during cellular senescence of human BJ- fibroblasts. Part I. Effects of proliferative senescence
    • N. Sitte, M. Merker, T. von Zglinicki, T. Grune, and K.J.A. Davies Protein oxidation and degradation during cellular senescence of human BJ- fibroblasts. Part I. Effects of proliferative senescence FASEB J. 14 2000 2495 2502
    • (2000) FASEB J. , vol.14 , pp. 2495-2502
    • Sitte, N.1    Merker, M.2    Von Zglinicki, T.3    Grune, T.4    Davies, K.J.A.5
  • 13
    • 0034117954 scopus 로고    scopus 로고
    • Protein oxidation and degradation during proliferative senescence of human MRC-5 fibroblasts
    • DOI 10.1016/S0891-5849(99)00279-8, PII S0891584999002798
    • N. Sitte, K. Merker, T. von Zglinicki, and T. Grune Protein oxidation and degradation during proliferative senescence of human MRC-5 fibroblasts Free Radic. Biol. Med. 28 2000 701 708 (Pubitemid 30171283)
    • (2000) Free Radical Biology and Medicine , vol.28 , Issue.5 , pp. 701-708
    • Sitte, N.1    Merker, K.2    Von Zglinicki, T.3    Grune, T.4
  • 14
    • 0033674181 scopus 로고    scopus 로고
    • Protein oxidation and degradation during cellular senescence of human BJ- fibroblasts. Part II. Aging of non-dividing cells
    • N. Sitte, M. Merker, T. von Zglinicki, K.J.A. Davies, and T. Grune Protein oxidation and degradation during cellular senescence of human BJ- fibroblasts. Part II. Aging of non-dividing cells FASEB J. 14 2000 2503 2510
    • (2000) FASEB J. , vol.14 , pp. 2503-2510
    • Sitte, N.1    Merker, M.2    Von Zglinicki, T.3    Davies, K.J.A.4    Grune, T.5
  • 17
    • 70449411818 scopus 로고    scopus 로고
    • Oxidatively modified, mitochondria-relevant brain proteins in subjects with Alzheimer disease and mild cognitive impairment
    • R. Sultana, and D.A. Butterfield Oxidatively modified, mitochondria-relevant brain proteins in subjects with Alzheimer disease and mild cognitive impairment J. Bioenerg. Biomembr. 41 2009 441 446
    • (2009) J. Bioenerg. Biomembr. , vol.41 , pp. 441-446
    • Sultana, R.1    Butterfield, D.A.2
  • 18
    • 77449110410 scopus 로고    scopus 로고
    • Proteomics identification of carbonylated and HNE-bound brain proteins in Alzheimer's disease
    • R. Sultana, and D.-A. Butterfield Proteomics identification of carbonylated and HNE-bound brain proteins in Alzheimer's disease Methods Mol. Biol. 566 2009 123 135
    • (2009) Methods Mol. Biol. , vol.566 , pp. 123-135
    • Sultana, R.1    Butterfield, D.-A.2
  • 19
    • 77249155512 scopus 로고    scopus 로고
    • Age-related changes in mitochondrial respiration and oxidative damage in the cerebral cortex of the Fischer 344 rat
    • L.K. Gilmer, M.A. Ansari, K.N. Roberts, and S.W. Scheff Age-related changes in mitochondrial respiration and oxidative damage in the cerebral cortex of the Fischer 344 rat Mech. Ageing Dev. 131 2010 133 143
    • (2010) Mech. Ageing Dev. , vol.131 , pp. 133-143
    • Gilmer, L.K.1    Ansari, M.A.2    Roberts, K.N.3    Scheff, S.W.4
  • 20
    • 28244454785 scopus 로고    scopus 로고
    • Aconitase is the main functional target of aging in the citric acid cycle of kidney mitochondria from mice
    • C.S. Yarian, D. Toroser, and R.S. Sohal Aconitase is the main functional target of aging in the citric acid cycle of kidney mitochondria from mice Mech. Ageing Dev. 127 2006 79 84
    • (2006) Mech. Ageing Dev. , vol.127 , pp. 79-84
    • Yarian, C.S.1    Toroser, D.2    Sohal, R.S.3
  • 21
    • 66749163678 scopus 로고    scopus 로고
    • Disulfide formation in the ER and mitochondria: Two solutions to a common process
    • J. Riemer, N. Bulleid, and J.M. Herrmann Disulfide formation in the ER and mitochondria: two solutions to a common process Science 324 2009 1284 1287
    • (2009) Science , vol.324 , pp. 1284-1287
    • Riemer, J.1    Bulleid, N.2    Herrmann, J.M.3
  • 22
    • 35848957485 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and oxidative stress: A vicious cycle or a double-edged sword?
    • J.D. Malhotra, and R.J. Kaufman Endoplasmic reticulum stress and oxidative stress: a vicious cycle or a double-edged sword? Antioxid. Redox Signal. 9 2007 2277 2293
    • (2007) Antioxid. Redox Signal. , vol.9 , pp. 2277-2293
    • Malhotra, J.D.1    Kaufman, R.J.2
  • 23
    • 1342294159 scopus 로고    scopus 로고
    • Stability of the nuclear protein turnover during cellular senescence of human fibroblasts
    • K. Merker, O. Ullrich, H. Schmidt, N. Sitte, and T. Grune Stability of the nuclear protein turnover during cellular senescence of human fibroblasts FASEB J. 17 2003 1963 1965
    • (2003) FASEB J. , vol.17 , pp. 1963-1965
    • Merker, K.1    Ullrich, O.2    Schmidt, H.3    Sitte, N.4    Grune, T.5
  • 24
    • 0034161834 scopus 로고    scopus 로고
    • Hydrogen peroxide mediated protein oxidation in young and old human MRC-5 fibroblasts
    • K. Merker, N. Sitte, and T. Grune Hydrogen peroxide mediated protein oxidation in young and old human MRC-5 fibroblasts Arch. Biochem. Biophys. 375 2000 50 54
    • (2000) Arch. Biochem. Biophys. , vol.375 , pp. 50-54
    • Merker, K.1    Sitte, N.2    Grune, T.3
  • 25
    • 0028245961 scopus 로고
    • Exposure of hydrophobic moieties promotes the selective degradation of hydrogen peroxide-modified hemoglobin by the multicatalytic proteinase complex, proteasome
    • C. Guilivi, R.E. Pacifici, and K.J.A. Davies Exposure of hydrophobic moieties promotes the selective degradation of hydrogen peroxide-modified hemoglobin by the multicatalytic proteinase complex, proteasome Arch. Biochem. Biophys. 311 1994 329 341
    • (1994) Arch. Biochem. Biophys. , vol.311 , pp. 329-341
    • Guilivi, C.1    Pacifici, R.E.2    Davies, K.J.A.3
  • 26
    • 0021928777 scopus 로고
    • Preferential degradation of the oxidatively modified form of glutamine synthetase by intracellular mammalian proteases
    • A.J. Rivett Preferential degradation of the oxidatively modified form of glutamine synthetase by intracellular mammalian proteases J. Biol. Chem. 260 1985 300 305
    • (1985) J. Biol. Chem. , vol.260 , pp. 300-305
    • Rivett, A.J.1
  • 27
    • 0027990369 scopus 로고
    • Modification of glucose-6-phosphate dehydrogenase by 4-hydroxynonenal: Formation of cross-linked protein that inhibits the multicatalytic protease
    • B. Friguet, E.R. Stadtman, and L.I. Sweda Modification of glucose-6-phosphate dehydrogenase by 4-hydroxynonenal: formation of cross-linked protein that inhibits the multicatalytic protease J. Biol. Chem. 269 1994 21639 21643
    • (1994) J. Biol. Chem. , vol.269 , pp. 21639-21643
    • Friguet, B.1    Stadtman, E.R.2    Sweda, L.I.3
  • 28
    • 0028340636 scopus 로고
    • Susceptibility of glucose-6-phosphate dehydrogenase modified 4-hydroxynonenal and metal-catalyzed oxidation to proteolysis by multicatalytic protease
    • B. Friguet, L.I. Szweda, and E.R. Stadtman Susceptibility of glucose-6-phosphate dehydrogenase modified 4-hydroxynonenal and metal-catalyzed oxidation to proteolysis by multicatalytic protease Arch. Biochem. Biophys. 311 1994 168 173
    • (1994) Arch. Biochem. Biophys. , vol.311 , pp. 168-173
    • Friguet, B.1    Szweda, L.I.2    Stadtman, E.R.3
  • 29
    • 58149183257 scopus 로고    scopus 로고
    • Proteasome activation as a novel antiaging strategy
    • N. Chondrogianni, and E.S. Gonos Proteasome activation as a novel antiaging strategy IUBMB Life 60 2008 651 655
    • (2008) IUBMB Life , vol.60 , pp. 651-655
    • Chondrogianni, N.1    Gonos, E.S.2
  • 30
    • 17144414925 scopus 로고    scopus 로고
    • Overexpression of proteasome beta5 assembled subunit increases the amount of proteasome and confers ameliorated response to oxidative stress and higher survival rates
    • N. Chondrogianni, C. Tzavelas, A.J. Pemberton, I.P. Nezis, A.J. Rivett, and E.S. Gonos Overexpression of proteasome beta5 assembled subunit increases the amount of proteasome and confers ameliorated response to oxidative stress and higher survival rates J. Biol. Chem. 280 2005 11840 11850
    • (2005) J. Biol. Chem. , vol.280 , pp. 11840-11850
    • Chondrogianni, N.1    Tzavelas, C.2    Pemberton, A.J.3    Nezis, I.P.4    Rivett, A.J.5    Gonos, E.S.6
  • 31
    • 71849084532 scopus 로고    scopus 로고
    • Aging and dietary restriction alter proteasome biogenesis and composition in the brain and liver
    • K. Dasuri, L. Zhang, P. Ebenezer, Y. Liu, S.O. Fernandez-Kim, and J.N. Keller Aging and dietary restriction alter proteasome biogenesis and composition in the brain and liver Mech. Ageing Dev. 130 2009 777 783
    • (2009) Mech. Ageing Dev. , vol.130 , pp. 777-783
    • Dasuri, K.1    Zhang, L.2    Ebenezer, P.3    Liu, Y.4    Fernandez-Kim, S.O.5    Keller, J.N.6
  • 32
    • 0034087369 scopus 로고    scopus 로고
    • Decreased levels of proteasome activity and proteasome expression in aging spinal cord
    • J.N. Keller, F.F. Huang, and W.R. Markesbery Decreased levels of proteasome activity and proteasome expression in aging spinal cord Neuroscience 98 2000 149 156
    • (2000) Neuroscience , vol.98 , pp. 149-156
    • Keller, J.N.1    Huang, F.F.2    Markesbery, W.R.3
  • 33
    • 0028912676 scopus 로고
    • Protein degradation in cultured liver epithelial cells during oxidative stress
    • T. Grune, T. Reinheckel, M. Joshi, and K.J.A. Davies Protein degradation in cultured liver epithelial cells during oxidative stress J. Biol. Chem. 270 1995 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
  • 34
    • 0029984892 scopus 로고    scopus 로고
    • Degradation of oxidized proteins in K562 human hematopoietic cells by proteasome
    • T. Grune, T. Reinheckel, and K.J.A. Davies Degradation of oxidized proteins in K562 human hematopoietic cells by proteasome J. Biol. Chem. 271 1996 15504 15509
    • (1996) J. Biol. Chem. , vol.271 , pp. 15504-15509
    • Grune, T.1    Reinheckel, T.2    Davies, K.J.A.3
  • 36
    • 0032438035 scopus 로고    scopus 로고
    • Proteasome-dependent degradation of oxidized proteins in MRC-5 fibroblasts
    • N. Sitte, K. Merker, and T. Grune Proteasome-dependent degradation of oxidized proteins in MRC-5 fibroblasts FEBS Lett. 440 1998 399 402
    • (1998) FEBS Lett. , vol.440 , pp. 399-402
    • Sitte, N.1    Merker, K.2    Grune, T.3
  • 37
    • 0032080117 scopus 로고    scopus 로고
    • Peroxynitrite increases the degradation of aconitase and other cellular proteins by proteasome
    • T. Grune, I.E. Blasig, N. Sitte, B. Roloff, R. Haseloff, and K.J.A. Davies Peroxynitrite increases the degradation of aconitase and other cellular proteins by proteasome J. Biol. Chem. 273 1998 10857 10862
    • (1998) J. Biol. Chem. , vol.273 , pp. 10857-10862
    • Grune, T.1    Blasig, I.E.2    Sitte, N.3    Roloff, B.4    Haseloff, R.5    Davies, K.J.A.6
  • 38
    • 10644232372 scopus 로고    scopus 로고
    • Oxidation-induced ferritin turnover in microglial cells: Role of proteasome
    • J. Mehlhase, G. Sandig, K. Pantopoulos, and T. Grune Oxidation-induced ferritin turnover in microglial cells: role of proteasome Free Radic. Biol. Med. 38 2005 276 285
    • (2005) Free Radic. Biol. Med. , vol.38 , pp. 276-285
    • Mehlhase, J.1    Sandig, G.2    Pantopoulos, K.3    Grune, T.4
  • 39
    • 33749365979 scopus 로고    scopus 로고
    • Ferritin oxidation and proteasomal degradation: Protection by antioxidants
    • P. Voss, L. Horáková, M. Jakstadt, D. Kiekebusch, and T. Grune Ferritin oxidation and proteasomal degradation: protection by antioxidants Free Radic. Res. 40 2006 673 683
    • (2006) Free Radic. Res. , vol.40 , pp. 673-683
    • Voss, P.1    Horáková, L.2    Jakstadt, M.3    Kiekebusch, D.4    Grune, T.5
  • 40
    • 34447631179 scopus 로고    scopus 로고
    • Hyperammonemia causes protein oxidation and enhanced proteasomal activity in response to mitochondria-mediated oxidative stress in rat primary astrocytes
    • R. Widmer, B. Kaiser, M. Engels, T. Jung, and T. Grune Hyperammonemia causes protein oxidation and enhanced proteasomal activity in response to mitochondria-mediated oxidative stress in rat primary astrocytes Arch. Biochem. Biophys. 464 2007 1 11
    • (2007) Arch. Biochem. Biophys. , vol.464 , pp. 1-11
    • Widmer, R.1    Kaiser, B.2    Engels, M.3    Jung, T.4    Grune, T.5
  • 41
    • 50249175909 scopus 로고    scopus 로고
    • Heat shock and oxygen radicals stimulate ubiquitin-dependent degradation mainly of newly synthesized proteins
    • B. Medicherla, and A.L. Goldberg Heat shock and oxygen radicals stimulate ubiquitin-dependent degradation mainly of newly synthesized proteins J. Cell Biol. 182 2010 663 673
    • (2010) J. Cell Biol. , vol.182 , pp. 663-673
    • Medicherla, B.1    Goldberg, A.L.2
  • 43
    • 0036844724 scopus 로고    scopus 로고
    • PARP-mediated proteasome activation: A co-ordination of DNA repair and protein degradation?
    • J. Arnold, and T. Grune PARP-mediated proteasome activation: a co-ordination of DNA repair and protein degradation? BioEssays 24 2002 1060 1065
    • (2002) BioEssays , vol.24 , pp. 1060-1065
    • Arnold, J.1    Grune, T.2
  • 44
    • 0035478982 scopus 로고    scopus 로고
    • Proteasomal degradation of oxidatively damaged endogenous histones in K562 human leukemic cells
    • O. Ullrich, and T. Grune Proteasomal degradation of oxidatively damaged endogenous histones in K562 human leukemic cells Free Radic. Biol. Med. 31 2001 887 893
    • (2001) Free Radic. Biol. Med. , vol.31 , pp. 887-893
    • Ullrich, O.1    Grune, T.2
  • 46
    • 0033033698 scopus 로고    scopus 로고
    • Poly-ADP ribose polymerase activates nuclear proteasome to degrade oxidatively damaged histones
    • O. Ullrich, T. Reinheckel, N. Sitte, R. Hass, T. Grune, and K.J. Davies Poly-ADP ribose polymerase activates nuclear proteasome to degrade oxidatively damaged histones Proc. Natl Acad. Sci. USA 96 1999 6223 6228
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 6223-6228
    • Ullrich, O.1    Reinheckel, T.2    Sitte, N.3    Hass, R.4    Grune, T.5    Davies, K.J.6
  • 47
    • 0034669699 scopus 로고    scopus 로고
    • Proteasome activation by poly-ADP-ribose polymerase in human myelomonocytic cells after oxidative stress
    • O. Ullrich, O. Ciftci, and R. Hass Proteasome activation by poly-ADP-ribose polymerase in human myelomonocytic cells after oxidative stress Free Radic. Biol. Med. 29 2000 995 1004
    • (2000) Free Radic. Biol. Med. , vol.29 , pp. 995-1004
    • Ullrich, O.1    Ciftci, O.2    Hass, R.3
  • 48
    • 0035353155 scopus 로고    scopus 로고
    • Regulation of the nuclear proteasome activity in myelomonocytic human leukemia cells after adriamycin treatment
    • O. Ciftci, O. Ullrich, C.A. Schmidt, A. Diestel, and R. Hass Regulation of the nuclear proteasome activity in myelomonocytic human leukemia cells after adriamycin treatment Blood 97 2001 2830 2838
    • (2001) Blood , vol.97 , pp. 2830-2838
    • Ciftci, O.1    Ullrich, O.2    Schmidt, C.A.3    Diestel, A.4    Hass, R.5
  • 49
    • 0035377369 scopus 로고    scopus 로고
    • Turnover of oxidatively damaged nuclear proteins in BV-2 microglial cells is linked to their activation state by poly-ADP-ribose polymerase
    • O. Ullrich, A. Diestel, I. Bechmann, M. Homberg, T. Grune, R. Hass, and R. Nitsch Turnover of oxidatively damaged nuclear proteins in BV-2 microglial cells is linked to their activation state by poly-ADP-ribose polymerase FASEB J. 15 2001 1460 1462
    • (2001) FASEB J. , vol.15 , pp. 1460-1462
    • Ullrich, O.1    Diestel, A.2    Bechmann, I.3    Homberg, M.4    Grune, T.5    Hass, R.6    Nitsch, R.7
  • 51
    • 0027081044 scopus 로고
    • Poly(ADP-ribose) polymerase activity in mononuclear leukocytes of 13 mammalian species correlates with species-specific life span
    • K. Grube, and A. Bürkle Poly(ADP-ribose) polymerase activity in mononuclear leukocytes of 13 mammalian species correlates with species-specific life span Proc. Natl Acad. Sci. USA 89 1992 11759 11763
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 11759-11763
    • Grube, K.1    Bürkle, A.2
  • 52
    • 38049012963 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ation in mammalian ageing
    • S. Beneke, and A. Bürkle Poly(ADP-ribosyl)ation in mammalian ageing Nucleic Acids Res. 35 2007 7456 7465
    • (2007) Nucleic Acids Res. , vol.35 , pp. 7456-7465
    • Beneke, S.1    Bürkle, A.2
  • 54
    • 58149350129 scopus 로고    scopus 로고
    • The proteasome and its role in the degradation of oxidized proteins
    • T. Jung, and T. Grune The proteasome and its role in the degradation of oxidized proteins IUBMB Life 60 2008 743 752
    • (2008) IUBMB Life , vol.60 , pp. 743-752
    • Jung, T.1    Grune, T.2
  • 55
    • 59849107267 scopus 로고    scopus 로고
    • Age-related differences in oxidative protein-damage in young and senescent fibroblasts
    • T. Jung, A. Höhn, B. Catalgol, and T. Grune Age-related differences in oxidative protein-damage in young and senescent fibroblasts Arch. Biochem. Biophys. 483 2009 127 135
    • (2009) Arch. Biochem. Biophys. , vol.483 , pp. 127-135
    • Jung, T.1    Höhn, A.2    Catalgol, B.3    Grune, T.4
  • 56
    • 33646058316 scopus 로고    scopus 로고
    • Intracellular distribution of oxidized proteins and proteasome in HT22 cells during oxidative stress
    • T. Jung, M. Engels, B. Kaiser, D. Poppek, and T. Grune Intracellular distribution of oxidized proteins and proteasome in HT22 cells during oxidative stress Free Radic. Biol. Med. 40 2006 1303 1312
    • (2006) Free Radic. Biol. Med. , vol.40 , pp. 1303-1312
    • Jung, T.1    Engels, M.2    Kaiser, B.3    Poppek, D.4    Grune, T.5
  • 57
    • 33847028670 scopus 로고    scopus 로고
    • Nitrotyrosine and protein carbonyls are equally distributed in HT22 cells after nitrosative stress
    • T. Jung, M. Engels, L.D. Klotz, K.D. Kröncke, and T. Grune Nitrotyrosine and protein carbonyls are equally distributed in HT22 cells after nitrosative stress Free Radic. Biol. Med. 42 2007 773 786
    • (2007) Free Radic. Biol. Med. , vol.42 , pp. 773-786
    • Jung, T.1    Engels, M.2    Klotz, L.D.3    Kröncke, K.D.4    Grune, T.5
  • 58
    • 0036142055 scopus 로고    scopus 로고
    • Detection of poly(ADP-ribose) polymerase activation in oxidatively stressed cells and tissues using biotinylated NAD substrate
    • E. Bakondi, P. Bai, E. Szabo, J. Hunyadi, P. Gergely, C. Szabo, and L. Virag Detection of poly(ADP-ribose) polymerase activation in oxidatively stressed cells and tissues using biotinylated NAD substrate J. Histochem. Cytochem. 50 2002 91 98
    • (2002) J. Histochem. Cytochem. , vol.50 , pp. 91-98
    • Bakondi, E.1    Bai, P.2    Szabo, E.3    Hunyadi, J.4    Gergely, P.5    Szabo, C.6    Virag, L.7
  • 60
    • 0024419843 scopus 로고
    • Hydrogen peroxide insult in cultured mammalian cells: Relationships between DNA single strand breakage, poly(ADP-ribose) metabolism and cell killing
    • O. Cantoni, F. Cattabeni, V. Stocchi, R.E. Meyn, P. Cerutti, and D. Murray Hydrogen peroxide insult in cultured mammalian cells: relationships between DNA single strand breakage, poly(ADP-ribose) metabolism and cell killing Biochim. Biophys. Acta 1014 1989 1 7
    • (1989) Biochim. Biophys. Acta , vol.1014 , pp. 1-7
    • Cantoni, O.1    Cattabeni, F.2    Stocchi, V.3    Meyn, R.E.4    Cerutti, P.5    Murray, D.6
  • 61
    • 0027523401 scopus 로고
    • Identification of potential active site residues in the human poly(ADP-ribose) polymerase
    • F. Simonin, O. Poch, M. Delarue, and G. de Murcia Identification of potential active site residues in the human poly(ADP-ribose) polymerase J. Biol. Chem. 268 1993 8529 8535
    • (1993) J. Biol. Chem. , vol.268 , pp. 8529-8535
    • Simonin, F.1    Poch, O.2    Delarue, M.3    De Murcia, G.4
  • 62
    • 0023905860 scopus 로고
    • Establishment of three bleomycin-resistant human carcinoma cell lines and their cross-resistance to other antitumor agents
    • M. Urade, M. Sugi, and T. Miyazaki Establishment of three bleomycin-resistant human carcinoma cell lines and their cross-resistance to other antitumor agents Cancer 61 1988 1501 1507
    • (1988) Cancer , vol.61 , pp. 1501-1507
    • Urade, M.1    Sugi, M.2    Miyazaki, T.3
  • 63
    • 0030060632 scopus 로고    scopus 로고
    • Identification of a 116 kDa protein able to bind 1, 3-bis(2-chloroethyl)- 1-nitrosourea-damaged DNA as poly(ADP-ribose) polymerase
    • A. Malapetsa, A.J. Noe, G.G. Poirier, S. Desnoyers, N.A. Berger, and L.C. Panasci Identification of a 116 kDa protein able to bind 1, 3-bis(2-chloroethyl)-1-nitrosourea-damaged DNA as poly(ADP-ribose) polymerase Mutat. Res. 362 1996 41 50
    • (1996) Mutat. Res. , vol.362 , pp. 41-50
    • Malapetsa, A.1    Noe, A.J.2    Poirier, G.G.3    Desnoyers, S.4    Berger, N.A.5    Panasci, L.C.6
  • 64
    • 77954490419 scopus 로고    scopus 로고
    • Oxidized mitochondrial protein degradation and repair in aging and oxidative stress
    • N. Ugarte, I. Petropoulos, and B. Friguet Oxidized mitochondrial protein degradation and repair in aging and oxidative stress Antioxid. Redox Signal. 13 2010 539 549
    • (2010) Antioxid. Redox Signal. , vol.13 , pp. 539-549
    • Ugarte, N.1    Petropoulos, I.2    Friguet, B.3
  • 66
    • 33745367509 scopus 로고    scopus 로고
    • Proteasome response to interferon-gamma is altered in senescent human fibroblasts
    • F.L. Stratford, N. Chondrogianni, I.P. Trougakos, E.S. Gonos, and A.J. Rivett Proteasome response to interferon-gamma is altered in senescent human fibroblasts FEBS Lett. 580 2006 3989 3994
    • (2006) FEBS Lett. , vol.580 , pp. 3989-3994
    • Stratford, F.L.1    Chondrogianni, N.2    Trougakos, I.P.3    Gonos, E.S.4    Rivett, A.J.5
  • 67
    • 77950338981 scopus 로고    scopus 로고
    • DNA repair in premature aging disorders and neurodegeneration
    • F. Coppedè, and L. Migliore DNA repair in premature aging disorders and neurodegeneration Curr. Aging Sci. 3 2010 3 19
    • (2010) Curr. Aging Sci. , vol.3 , pp. 3-19
    • Coppedè, F.1    Migliore, L.2
  • 69
    • 77953944814 scopus 로고    scopus 로고
    • Chromatin modifications: The driving force of senescence and aging?
    • T. Dimauro, and G. David Chromatin modifications: the driving force of senescence and aging? Aging (Albany NY) 1 2009 182 190
    • (2009) Aging (Albany NY) , vol.1 , pp. 182-190
    • Dimauro, T.1    David, G.2
  • 70
    • 0038449141 scopus 로고    scopus 로고
    • PARP-1, a determinant of cell survival in response to DNA damage
    • V.J. Bouchard, M. Rouleau, and G.G. Poirier PARP-1, a determinant of cell survival in response to DNA damage Exp. Hematol. 31 2003 446 454
    • (2003) Exp. Hematol. , vol.31 , pp. 446-454
    • Bouchard, V.J.1    Rouleau, M.2    Poirier, G.G.3
  • 72
    • 0032761171 scopus 로고    scopus 로고
    • Age-related increases of 8-hydroxy-2′-deoxyguanosine and DNA-protein crosslinks in mouse organs
    • A. Izzotti, C. Cartiglia, M. Taningher, S. De Flora, and R. Balansky Age-related increases of 8-hydroxy-2′-deoxyguanosine and DNA-protein crosslinks in mouse organs Mutat. Res. 446 1999 215 223
    • (1999) Mutat. Res. , vol.446 , pp. 215-223
    • Izzotti, A.1    Cartiglia, C.2    Taningher, M.3    De Flora, S.4    Balansky, R.5


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