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Volumn 15, Issue 5, 2016, Pages 1692-1709

Global protein oxidation profiling suggests efficient mitochondrial proteome homeostasis during aging

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID DERIVATIVE; IRON CHELATING AGENT; PROTEOME; FUNGAL PROTEIN; METHIONINE; MITOCHONDRIAL PROTEIN; REACTIVE OXYGEN METABOLITE;

EID: 84964792168     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M115.055616     Document Type: Article
Times cited : (13)

References (91)
  • 1
    • 0025326942 scopus 로고
    • The antioxidants of human extracellular fluids
    • Halliwell, B., and Gutteridge, J. (1990) The antioxidants of human extracellular fluids. Arch. Biochem. Biophys. 280, 1-8
    • (1990) Arch. Biochem. Biophys. , vol.280 , pp. 1-8
    • Halliwell, B.1    Gutteridge, J.2
  • 2
    • 34648813720 scopus 로고    scopus 로고
    • ROS as signalling molecules: Mechanisms that generate specificity in ROS homeostasis
    • D'Autreaux, B., and Toledano, M. B. (2007) ROS as signalling molecules: mechanisms that generate specificity in ROS homeostasis. Nat. Rev. Mol. Cell Biol. 8, 813-824
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 813-824
    • D'Autreaux, B.1    Toledano, M.B.2
  • 3
    • 84884673437 scopus 로고    scopus 로고
    • Molecular mechanisms of superoxide production by complex III: A bacterial versus human mitochondrial comparative case study
    • Lanciano, P., Khalfaoui-Hassani, B., Selamoglu, N., Ghelli, A., Rugolo, M., and Daldal, F. (2013) Molecular mechanisms of superoxide production by complex III: a bacterial versus human mitochondrial comparative case study. Biochim. Biophys. Acta 1827, 1332-1339
    • (2013) Biochim. Biophys. Acta , vol.1827 , pp. 1332-1339
    • Lanciano, P.1    Khalfaoui-Hassani, B.2    Selamoglu, N.3    Ghelli, A.4    Rugolo, M.5    Daldal, F.6
  • 4
    • 84863738048 scopus 로고    scopus 로고
    • Molecular mechanisms of superoxide production by the mitochondrial respiratory chain
    • Dröse, S., and Brandt, U. (2012) Molecular mechanisms of superoxide production by the mitochondrial respiratory chain. Adv. Exp. Med. Biol. 748, 145-169
    • (2012) Adv. Exp. Med. Biol. , vol.748 , pp. 145-169
    • Dröse, S.1    Brandt, U.2
  • 5
    • 0034864018 scopus 로고    scopus 로고
    • Mitochondrial involvement in brain function and dysfunction: Relevance to aging, neurodegenerative disorders and longevity
    • Calabrese, V., Scapagnini, G., Giuffrida Stella, A. M., Bates, T. E., and Clark, J. B. (2001) Mitochondrial involvement in brain function and dysfunction: relevance to aging, neurodegenerative disorders and longevity. Neurochem. Res. 26, 739-764
    • (2001) Neurochem. Res. , vol.26 , pp. 739-764
    • Calabrese, V.1    Scapagnini, G.2    Giuffrida Stella, A.M.3    Bates, T.E.4    Clark, J.B.5
  • 7
    • 84864748949 scopus 로고    scopus 로고
    • Modulating protein activity and cellular function by methionine residue oxidation
    • Cui, Z. J., Han, Z. Q., and Li, Z. Y. (2011) Modulating protein activity and cellular function by methionine residue oxidation. Amino Acids 43, 505-517
    • (2011) Amino Acids , vol.43 , pp. 505-517
    • Cui, Z.J.1    Han, Z.Q.2    Li, Z.Y.3
  • 8
    • 84881587735 scopus 로고    scopus 로고
    • Oxidative stress response elicited by mitochondrial dysfunction: Implication in the pathophysiology of aging
    • Wang, C. H., Wu, S. B., Wu, Y. T., and Wei, Y. H. (2013) Oxidative stress response elicited by mitochondrial dysfunction: implication in the pathophysiology of aging. Exp. Biol. Med. (Maywood) 238, 450-460
    • (2013) Exp. Biol. Med. (Maywood) , vol.238 , pp. 450-460
    • Wang, C.H.1    Wu, S.B.2    Wu, Y.T.3    Wei, Y.H.4
  • 9
    • 0037378026 scopus 로고    scopus 로고
    • Oxidative stress in Parkinson's disease
    • discussion S36-38
    • Jenner, P. (2003) Oxidative stress in Parkinson's disease. Ann. Neurol. 53 Suppl 3, S26-36; discussion S36-38
    • (2003) Ann. Neurol. , vol.53 , pp. S26-36
    • Jenner, P.1
  • 10
    • 33750347347 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases
    • Lin, M. T., and Beal, M. F. (2006) Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases. Nature 443, 787-795
    • (2006) Nature , vol.443 , pp. 787-795
    • Lin, M.T.1    Beal, M.F.2
  • 11
    • 77049308856 scopus 로고
    • Aging: A theory based on free radical and radiation chemistry
    • Harman, D. (1956) Aging: a theory based on free radical and radiation chemistry. J. Gerontol. 11, 298-300
    • (1956) J. Gerontol. , vol.11 , pp. 298-300
    • Harman, D.1
  • 12
    • 0015319592 scopus 로고
    • The biologic clock: The mitochondria?
    • Harman, D. (1972) The biologic clock: the mitochondria? J. Am. Geriatr. Soc. 20, 145-147
    • (1972) J. Am. Geriatr. Soc. , vol.20 , pp. 145-147
    • Harman, D.1
  • 13
    • 0036569401 scopus 로고    scopus 로고
    • Carbonyl modified proteins in cellular regulation, aging, and disease
    • Levine, R. L. (2002) Carbonyl modified proteins in cellular regulation, aging, and disease. Free Radic. Biol. Med. 32, 790-796
    • (2002) Free Radic. Biol. Med. , vol.32 , pp. 790-796
    • Levine, R.L.1
  • 14
    • 84855394783 scopus 로고    scopus 로고
    • Oxidative stress, mitochondrial dysfunction, and aging
    • Cui, H., Kong, Y., and Zhang, H. (2012) Oxidative stress, mitochondrial dysfunction, and aging. J. Signal Transduct. 2012, 646354
    • (2012) J. Signal Transduct. , vol.2012 , pp. 646354
    • Cui, H.1    Kong, Y.2    Zhang, H.3
  • 15
    • 0026775958 scopus 로고
    • Free radical theory of aging
    • Harman, D. (1992) Free radical theory of aging. Mutat. Res. 275, 257-266
    • (1992) Mutat. Res. , vol.275 , pp. 257-266
    • Harman, D.1
  • 16
    • 0029125857 scopus 로고
    • Aging, energy, and oxidative stress in neurodegenerative diseases
    • Beal, M. F. (1995) Aging, energy, and oxidative stress in neurodegenerative diseases. Ann. Neurol. 38, 357-366
    • (1995) Ann. Neurol. , vol.38 , pp. 357-366
    • Beal, M.F.1
  • 18
    • 0036182865 scopus 로고    scopus 로고
    • Aging in fungi: Role of mitochondria in Podospora anserina
    • Osiewacz, H. D. (2002) Aging in fungi: role of mitochondria in Podospora anserina. Mech. Ageing Dev. 123, 755-764
    • (2002) Mech. Ageing Dev. , vol.123 , pp. 755-764
    • Osiewacz, H.D.1
  • 19
    • 0037029072 scopus 로고    scopus 로고
    • Mitochondrial functions and aging
    • Osiewacz, H. D. (2002) Mitochondrial functions and aging. Gene 286, 65-71
    • (2002) Gene , vol.286 , pp. 65-71
    • Osiewacz, H.D.1
  • 20
    • 33745595856 scopus 로고    scopus 로고
    • Mitochondrial metabolism and aging in the filamentous fungus Podospora anserina
    • Lorin, S., Dufour, E., and Sainsard-Chanet, A. (2006) Mitochondrial metabolism and aging in the filamentous fungus Podospora anserina. Biochim. Biophys. Acta 1757, 604-610
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 604-610
    • Lorin, S.1    Dufour, E.2    Sainsard-Chanet, A.3
  • 21
    • 84878419118 scopus 로고    scopus 로고
    • Assessing organismal aging in the filamentous fungus Podospora anserina
    • Osiewacz, H. D., Hamann, A., and Zintel, S. (2013) Assessing organismal aging in the filamentous fungus Podospora anserina. Methods Mol. Biol. 965, 439-462
    • (2013) Methods Mol. Biol. , vol.965 , pp. 439-462
    • Osiewacz, H.D.1    Hamann, A.2    Zintel, S.3
  • 22
    • 33845876643 scopus 로고    scopus 로고
    • Reducing mitochondrial fission results in increased life span and fitness of two fungal ageing models
    • Scheckhuber, C. Q., Erjavec, N., Tinazli, A., Hamann, A., Nyström, T., and Osiewacz, H. D. (2007) Reducing mitochondrial fission results in increased life span and fitness of two fungal ageing models. Nat. Cell Biol. 9, 99-105
    • (2007) Nat. Cell Biol. , vol.9 , pp. 99-105
    • Scheckhuber, C.Q.1    Erjavec, N.2    Tinazli, A.3    Hamann, A.4    Nyström, T.5    Osiewacz, H.D.6
  • 23
    • 33747877758 scopus 로고    scopus 로고
    • Mitochondrial free radical generation and lifespan control in the fungal aging model Podospora anserina
    • Gredilla, R., Grief, J., and Osiewacz, H. D. (2006) Mitochondrial free radical generation and lifespan control in the fungal aging model Podospora anserina. Exp. Gerontol. 41, 439-447
    • (2006) Exp. Gerontol. , vol.41 , pp. 439-447
    • Gredilla, R.1    Grief, J.2    Osiewacz, H.D.3
  • 24
    • 67650091290 scopus 로고    scopus 로고
    • Increasing organismal healthspan by enhancing mitochondrial protein quality control
    • Luce, K., and Osiewacz, H. D. (2009) Increasing organismal healthspan by enhancing mitochondrial protein quality control. Nat. Cell Biol. 11, 852-858
    • (2009) Nat. Cell Biol. , vol.11 , pp. 852-858
    • Luce, K.1    Osiewacz, H.D.2
  • 25
    • 52649084803 scopus 로고    scopus 로고
    • Over-expression of an Sadenosylmethionine-dependent methyltransferase leads to an extended lifespan of Podospora anserina without impairments in vital functions
    • Kunstmann, B., and Osiewacz, H. D. (2008) Over-expression of an Sadenosylmethionine-dependent methyltransferase leads to an extended lifespan of Podospora anserina without impairments in vital functions. Aging Cell 7, 651-662
    • (2008) Aging Cell , vol.7 , pp. 651-662
    • Kunstmann, B.1    Osiewacz, H.D.2
  • 26
    • 84882753352 scopus 로고    scopus 로고
    • Differential expression and glycative damage affect specific mitochondrial proteins with aging in rat liver
    • Bakala, H., Ladouce, R., Baraibar, M. A., and Friguet, B. (2013) Differential expression and glycative damage affect specific mitochondrial proteins with aging in rat liver. Biochim. Biophys. Acta 1832, 2057-2067
    • (2013) Biochim. Biophys. Acta , vol.1832 , pp. 2057-2067
    • Bakala, H.1    Ladouce, R.2    Baraibar, M.A.3    Friguet, B.4
  • 27
  • 29
    • 76749156961 scopus 로고    scopus 로고
    • The S-adenosylmethionine dependent O-methyltransferase PaMTH1: A longevity assurance factor protecting Podospora anserina against oxidative stress
    • Kunstmann, B., and Osiewacz, H. D. (2009) The S-adenosylmethionine dependent O-methyltransferase PaMTH1: a longevity assurance factor protecting Podospora anserina against oxidative stress. Aging 1, 328-334
    • (2009) Aging , vol.1 , pp. 328-334
    • Kunstmann, B.1    Osiewacz, H.D.2
  • 30
  • 32
    • 78650315984 scopus 로고    scopus 로고
    • Pinpointing oxidative modifications in proteins-recent advances in analytical methods
    • Törnvall, U. (2010) Pinpointing oxidative modifications in proteins-recent advances in analytical methods. Anal. Methods 2, 1638-1650
    • (2010) Anal. Methods , vol.2 , pp. 1638-1650
    • Törnvall, U.1
  • 33
    • 84893775972 scopus 로고    scopus 로고
    • Protein carbonylation as a major hallmark of oxidative damage: Update of analytical strategies: Protein carbonylation
    • Fedorova, M., Bollineni, R. C., and Hoffmann, R. (2014) Protein carbonylation as a major hallmark of oxidative damage: update of analytical strategies: protein carbonylation. Mass Spectrom. Rev. 33, 79-97
    • (2014) Mass Spectrom. Rev. , vol.33 , pp. 79-97
    • Fedorova, M.1    Bollineni, R.C.2    Hoffmann, R.3
  • 34
    • 42049109266 scopus 로고    scopus 로고
    • The origin and control of ex vivo oxidative peptide modifications prior to mass spectrometry analysis
    • Froelich, J. M., and Reid, G. E. (2008) The origin and control of ex vivo oxidative peptide modifications prior to mass spectrometry analysis. Proteomics 8, 1334-1345
    • (2008) Proteomics , vol.8 , pp. 1334-1345
    • Froelich, J.M.1    Reid, G.E.2
  • 35
    • 77953911347 scopus 로고    scopus 로고
    • Mass spectrometric identification of oxidative modifications of tryptophan residues in proteins: Chemical artifact or post-translational modification?
    • Perdivara, I., Deterding, L. J., Przybylski, M., and Tomer, K. B. (2010) Mass spectrometric identification of oxidative modifications of tryptophan residues in proteins: chemical artifact or post-translational modification? J. Am. Soc. Mass Spectrom. 21, 1114-1117
    • (2010) J. Am. Soc. Mass Spectrom. , vol.21 , pp. 1114-1117
    • Perdivara, I.1    Deterding, L.J.2    Przybylski, M.3    Tomer, K.B.4
  • 36
    • 80053041158 scopus 로고    scopus 로고
    • Protein carbonylation and metal-catalyzed protein oxidation in a cellular perspective
    • Møller, I. M., Rogowska-Wrzesinska, A., and Rao, R. S. P. (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.P.3
  • 37
    • 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, D. L., Xie, H., Thompson, L. V., Arriaga, E. A., and Griffin, T. J. (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
  • 38
    • 0037338365 scopus 로고    scopus 로고
    • Proteomic analysis of post-translational modifications
    • Mann, M., and Jensen, O. N. (2003) Proteomic analysis of post-translational modifications. Nat. Biotechnol. 21, 255-261
    • (2003) Nat. Biotechnol. , vol.21 , pp. 255-261
    • Mann, M.1    Jensen, O.N.2
  • 39
    • 84886952015 scopus 로고    scopus 로고
    • Proteomic quantification and identification of carbonylated proteins upon oxidative stress and during cellular aging
    • Baraibar, M. A., Ladouce, R., and Friguet, B. (2013) Proteomic quantification and identification of carbonylated proteins upon oxidative stress and during cellular aging. J. Proteomics 92, 63-70
    • (2013) J. Proteomics , vol.92 , pp. 63-70
    • Baraibar, M.A.1    Ladouce, R.2    Friguet, B.3
  • 40
    • 19944432197 scopus 로고    scopus 로고
    • Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents
    • Ross, P. L. (2004) Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents. Mol. Cell. Proteomics 3, 1154-1169
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 1154-1169
    • Ross, P.L.1
  • 43
    • 67349266694 scopus 로고    scopus 로고
    • Universal sample preparation method for proteome analysis
    • Wiśniewski, J. R., Zougman, A., Nagaraj, N., and Mann, M. (2009) Universal sample preparation method for proteome analysis. Nat. Methods 6, 359-362
    • (2009) Nat. Methods , vol.6 , pp. 359-362
    • Wiśniewski, J.R.1    Zougman, A.2    Nagaraj, N.3    Mann, M.4
  • 45
    • 38649129079 scopus 로고    scopus 로고
    • Posterior error probabilities and false discovery rates: Two sides of the same coin
    • Käll, L., Storey, J. D., MacCoss, M. J., and Noble, W. S. (2008) Posterior error probabilities and false discovery rates: two sides of the same coin. J. Proteome Res. 7, 40-44
    • (2008) J. Proteome Res. , vol.7 , pp. 40-44
    • Käll, L.1    Storey, J.D.2    MacCoss, M.J.3    Noble, W.S.4
  • 47
    • 4544367274 scopus 로고    scopus 로고
    • Evaluating Kolmogorov's distribution
    • Marsaglia, G., Tsang, W. W., and Wang, J. (2003) Evaluating Kolmogorov's Distribution. J. Stat Softw 8, 1-4
    • (2003) J. Stat Softw , vol.8 , pp. 1-4
    • Marsaglia, G.1    Tsang, W.W.2    Wang, J.3
  • 49
    • 0001677717 scopus 로고
    • Controlling the false discovery rate: A practical and powerful approach to multiple testing
    • Benjamini, Y., and Hochberg, Y. (1995) Controlling the False Discovery Rate: A Practical and Powerful Approach to Multiple Testing. J. R. Statist. Soc. B 57, 289-300
    • (1995) J. R. Statist. Soc. B , vol.57 , pp. 289-300
    • Benjamini, Y.1    Hochberg, Y.2
  • 51
    • 84875841478 scopus 로고    scopus 로고
    • Combined application of targeted and untargeted proteomics identifies distinct metabolic alterations in the tetraacetylphytosphingosine (TAPS) producing yeast Wickerhamomyces ciferrii
    • Wolff, D., ter Veld, F., Kohler, T., and Poetsch, A. (2013) Combined application of targeted and untargeted proteomics identifies distinct metabolic alterations in the tetraacetylphytosphingosine (TAPS) producing yeast Wickerhamomyces ciferrii. J. Proteomics 82, 274-287
    • (2013) J. Proteomics , vol.82 , pp. 274-287
    • Wolff, D.1    Ter Veld, F.2    Kohler, T.3    Poetsch, A.4
  • 55
    • 80155124832 scopus 로고    scopus 로고
    • MS3 eliminates ratio distortion in isobaric multiplexed quantitative proteomics
    • Ting, L., Rad, R., Gygi, S. P., and Haas, W. (2011) MS3 eliminates ratio distortion in isobaric multiplexed quantitative proteomics. Nat. Methods 8, 937-940
    • (2011) Nat. Methods , vol.8 , pp. 937-940
    • Ting, L.1    Rad, R.2    Gygi, S.P.3    Haas, W.4
  • 57
    • 0030660581 scopus 로고    scopus 로고
    • A genomic perspective on protein families
    • Tatusov, R. L., Koonin, E. V., and Lipman, D. J. (1997) A genomic perspective on protein families. Science 278, 631-637
    • (1997) Science , vol.278 , pp. 631-637
    • Tatusov, R.L.1    Koonin, E.V.2    Lipman, D.J.3
  • 58
    • 0034442070 scopus 로고    scopus 로고
    • The nature and mechanism of superoxide production by the electron transport chain: Its relevance to aging
    • Muller, F. (2000) The nature and mechanism of superoxide production by the electron transport chain: Its relevance to aging. AGE 23, 227-253
    • (2000) AGE , vol.23 , pp. 227-253
    • Muller, F.1
  • 59
    • 19444387198 scopus 로고    scopus 로고
    • Free radicals and antioxidants in human health: Current status and future prospects
    • Devasagayam, T., Tilak, J. C., Boloor, K. K., Sane, K., Ghaskadbi, S., and Lele, R. (2004) Free radicals and antioxidants in human health: current status and future prospects. Japi 52, 794-804
    • (2004) Japi , vol.52 , pp. 794-804
    • Devasagayam, T.1    Tilak, J.C.2    Boloor, K.K.3    Sane, K.4    Ghaskadbi, S.5    Lele, R.6
  • 61
    • 84886952989 scopus 로고    scopus 로고
    • Reporter ion-based mass spectrometry approaches for the detection of non-enzymatic protein modifications in biological samples
    • Tveen-Jensen, K., Reis, A., Mouls, L., Pitt, A. R., and Spickett, C. M. (2013) Reporter ion-based mass spectrometry approaches for the detection of non-enzymatic protein modifications in biological samples. J. Proteomics 92, 71-79
    • (2013) J. Proteomics , vol.92 , pp. 71-79
    • Tveen-Jensen, K.1    Reis, A.2    Mouls, L.3    Pitt, A.R.4    Spickett, C.M.5
  • 62
    • 84879970303 scopus 로고    scopus 로고
    • Comparative informatics analysis to evaluate sitespecific protein oxidation in multidimensional LC-MS/MS data
    • McClintock, C. S., Parks, J. M., Bern, M., GhattyVenkataKrishna, P. K., and Hettich, R. L. (2013) Comparative informatics analysis to evaluate sitespecific protein oxidation in multidimensional LC-MS/MS data. J. Proteome Res. 12, 3307-3316
    • (2013) J. Proteome Res. , vol.12 , pp. 3307-3316
    • McClintock, C.S.1    Parks, J.M.2    Bern, M.3    GhattyVenkataKrishna, P.K.4    Hettich, R.L.5
  • 63
    • 82355181555 scopus 로고    scopus 로고
    • Using quantitative redox proteomics to dissect the yeast redoxome
    • Brandes, N., Reichmann, D., Tienson, H., Leichert, L. I., and Jakob, U. (2011) Using quantitative redox proteomics to dissect the yeast redoxome. J. Biol. Chem. 286, 41893-41903
    • (2011) J. Biol. Chem. , vol.286 , pp. 41893-41903
    • Brandes, N.1    Reichmann, D.2    Tienson, H.3    Leichert, L.I.4    Jakob, U.5
  • 64
    • 79951896245 scopus 로고    scopus 로고
    • Effects of oxidative stress on behavior, physiology, and the redox thiol proteome of Caenorhabditis elegans
    • Kumsta, C., Thamsen, M., and Jakob, U. (2011) Effects of oxidative stress on behavior, physiology, and the redox thiol proteome of Caenorhabditis elegans. Antioxid Redox Signal 14, 1023-1037
    • (2011) Antioxid Redox Signal , vol.14 , pp. 1023-1037
    • Kumsta, C.1    Thamsen, M.2    Jakob, U.3
  • 65
    • 84866272849 scopus 로고    scopus 로고
    • Quantitative in vivo redox sensors uncover oxidative stress as an early event in life
    • Knoefler, D., Thamsen, M., Koniczek, M., Niemuth, Nicholas J., Diederich, A.-K., and Jakob, U. (2012) Quantitative in vivo redox sensors uncover oxidative stress as an early event in life. Mol. Cell 47, 767-776
    • (2012) Mol. Cell , vol.47 , pp. 767-776
    • Knoefler, D.1    Thamsen, M.2    Koniczek, M.3    Niemuth, N.J.4    Diederich, A.-K.5    Jakob, U.6
  • 67
    • 70449412362 scopus 로고    scopus 로고
    • ITRAQ underestimation in simple and complex mixtures: "The good, the bad and the ugly"
    • Ow, S. Y., Salim, M., Noirel, J., Evans, C., Rehman, I., and Wright, P. C. (2009) iTRAQ underestimation in simple and complex mixtures: "The good, the bad and the ugly". J. Proteome Res. 8, 5347-5355
    • (2009) J. Proteome Res. , vol.8 , pp. 5347-5355
    • Ow, S.Y.1    Salim, M.2    Noirel, J.3    Evans, C.4    Rehman, I.5    Wright, P.C.6
  • 68
    • 84883348438 scopus 로고    scopus 로고
    • Age-related changes in the mitochondrial proteome of the fungus Podospora anserina analyzed by 2D-DIGE and LC-MS/MS
    • Chimi, M. A., Dröse, S., Wittig, I., Heide, H., Steger, M., Werner, A., Hamann, A., Osiewacz, H. D., and Brandt, U. (2013) Age-related changes in the mitochondrial proteome of the fungus Podospora anserina analyzed by 2D-DIGE and LC-MS/MS. J. Proteomics 91, 358-374
    • (2013) J. Proteomics , vol.91 , pp. 358-374
    • Chimi, M.A.1    Dröse, S.2    Wittig, I.3    Heide, H.4    Steger, M.5    Werner, A.6    Hamann, A.7    Osiewacz, H.D.8    Brandt, U.9
  • 69
    • 84893364380 scopus 로고    scopus 로고
    • A genome-wide longitudinal transcriptome analysis of the aging model podospora anserina
    • Philipp, O., Hamann, A., Servos, J., Werner, A., Koch, I., and Osiewacz, H. D. (2013) A Genome-Wide Longitudinal Transcriptome Analysis of the Aging Model Podospora anserina. PLoS ONE 8, e83109
    • (2013) PLoS ONE , vol.8 , pp. e83109
    • Philipp, O.1    Hamann, A.2    Servos, J.3    Werner, A.4    Koch, I.5    Osiewacz, H.D.6
  • 70
    • 84901845193 scopus 로고    scopus 로고
    • Proteomic analysis of mitochondria from senescent Podospora anserina casts new light on ROS dependent aging mechanisms
    • Plohnke, N., Hamann, A., Poetsch, A., Osiewacz, H. D., Rögner, M., and Rexroth, S. (2014) Proteomic analysis of mitochondria from senescent Podospora anserina casts new light on ROS dependent aging mechanisms. Exp. Gerontol. 56, 13-25
    • (2014) Exp. Gerontol. , vol.56 , pp. 13-25
    • Plohnke, N.1    Hamann, A.2    Poetsch, A.3    Osiewacz, H.D.4    Rögner, M.5    Rexroth, S.6
  • 71
    • 0034626735 scopus 로고    scopus 로고
    • Oxidants, oxidative stress and the biology of ageing
    • Finkel, T., and Holbrook, N. J. (2000) Oxidants, oxidative stress and the biology of ageing. Nature 408, 239-247
    • (2000) Nature , vol.408 , pp. 239-247
    • Finkel, T.1    Holbrook, N.J.2
  • 72
    • 0036570159 scopus 로고    scopus 로고
    • Oxidatively modified proteins in aging and disease
    • Beal, M. F. (2002) Oxidatively modified proteins in aging and disease. Free Radic. Biol. Med. 32, 797-803
    • (2002) Free Radic. Biol. Med. , vol.32 , pp. 797-803
    • Beal, M.F.1
  • 73
    • 84887022165 scopus 로고    scopus 로고
    • Oxidative stress and mitochondrial protein quality control in aging
    • Lionaki, E., and Tavernarakis, N. (2013) Oxidative stress and mitochondrial protein quality control in aging. J. Proteomics 92, 181-194
    • (2013) J. Proteomics , vol.92 , pp. 181-194
    • Lionaki, E.1    Tavernarakis, N.2
  • 74
    • 8344282655 scopus 로고    scopus 로고
    • The role of oxidative damage and stress in aging
    • Bokov, A., Chaudhuri, A., and Richardson, A. (2004) The role of oxidative damage and stress in aging. Mech. Ageing Dev. 125, 811-826
    • (2004) Mech. Ageing Dev. , vol.125 , pp. 811-826
    • Bokov, A.1    Chaudhuri, A.2    Richardson, A.3
  • 76
    • 73749085674 scopus 로고    scopus 로고
    • When a theory of aging ages badly
    • Lapointe, J., and Hekimi, S. (2010) When a theory of aging ages badly. Cell. Mol. Life Sci. 67, 1-8
    • (2010) Cell. Mol. Life Sci. , vol.67 , pp. 1-8
    • Lapointe, J.1    Hekimi, S.2
  • 77
    • 57749095081 scopus 로고    scopus 로고
    • Against the oxidative damage theory of aging: Superoxide dismutases protect against oxidative stress but have little or no effect on life span in Caenorhabditis elegans
    • Doonan, R., McElwee, J. J., Matthijssens, F., Walker, G. A., Houthoofd, K., Back, P., Matscheski, A., Vanfleteren, J. R., and Gems, D. (2008) Against the oxidative damage theory of aging: superoxide dismutases protect against oxidative stress but have little or no effect on life span in Caenorhabditis elegans. Genes Dev. 22, 3236-3241
    • (2008) Genes Dev. , vol.22 , pp. 3236-3241
    • Doonan, R.1    McElwee, J.J.2    Matthijssens, F.3    Walker, G.A.4    Houthoofd, K.5    Back, P.6    Matscheski, A.7    Vanfleteren, J.R.8    Gems, D.9
  • 78
    • 79953231670 scopus 로고    scopus 로고
    • Accurate quantification of more than 4000 mouse tissue proteins reveals minimal proteome changes during aging
    • M110 004523
    • Walther, D. M., and Mann, M. (2011) Accurate quantification of more than 4000 mouse tissue proteins reveals minimal proteome changes during aging. Mol. Cell. Proteomics 10, M110 004523
    • (2011) Mol. Cell. Proteomics , vol.10
    • Walther, D.M.1    Mann, M.2
  • 79
    • 33745631769 scopus 로고    scopus 로고
    • 2, a necessary evil for cell signaling
    • 2, a necessary evil for cell signaling. Science 312, 1882-1883
    • (2006) Science , vol.312 , pp. 1882-1883
    • Rhee, S.G.1
  • 80
    • 84859822386 scopus 로고    scopus 로고
    • Regulatory control or oxidative damage? Proteomic approaches to interrogate the role of cysteine oxidation status in biological processes
    • 013037
    • Held, J. M., and Gibson, B. W. (2012) Regulatory control or oxidative damage? Proteomic approaches to interrogate the role of cysteine oxidation status in biological processes. Mol. Cell. Proteomics 11, R111 013037
    • (2012) Mol. Cell. Proteomics , vol.11 , pp. R111
    • Held, J.M.1    Gibson, B.W.2
  • 82
    • 12844264123 scopus 로고    scopus 로고
    • Methionine sulfoxide reductases: History and cellular role in protecting against oxidative damage
    • Weissbach, H., Resnick, L., and Brot, N. (2005) Methionine sulfoxide reductases: history and cellular role in protecting against oxidative damage. Biochim. Biophys. Acta 1703, 203-212
    • (2005) Biochim. Biophys. Acta , vol.1703 , pp. 203-212
    • Weissbach, H.1    Resnick, L.2    Brot, N.3
  • 83
    • 0034456721 scopus 로고    scopus 로고
    • Oxidation of methionine in proteins: Roles in antioxidant defense and cellular regulation
    • Levine, R. L., Moskovitz, J., and Stadtman, E. R. (2000) Oxidation of methionine in proteins: roles in antioxidant defense and cellular regulation. IUBMB Life 50, 301-307
    • (2000) IUBMB Life , vol.50 , pp. 301-307
    • Levine, R.L.1    Moskovitz, J.2    Stadtman, E.R.3
  • 84
    • 48949119155 scopus 로고    scopus 로고
    • Mitochondrial protein quality control: Implications in ageing
    • Friguet, B., Bulteau, A.-L., and Petropoulos, I. (2008) Mitochondrial protein quality control: implications in ageing. Biotechnol J. 3, 757-764
    • (2008) Biotechnol J. , vol.3 , pp. 757-764
    • Friguet, B.1    Bulteau, A.-L.2    Petropoulos, I.3
  • 86
    • 22344456832 scopus 로고    scopus 로고
    • Mitochondrial DNA mutations, oxidative stress, and apoptosis in mammalian aging
    • Kujoth, G. C. (2005) Mitochondrial DNA mutations, oxidative stress, and apoptosis in mammalian aging. Science 309, 481-484
    • (2005) Science , vol.309 , pp. 481-484
    • Kujoth, G.C.1
  • 87
    • 77953507107 scopus 로고    scopus 로고
    • Mitochondrial DNA mutations in disease and aging
    • Wallace, D. C. (2010) Mitochondrial DNA mutations in disease and aging. Environ. Mol. Mutagen. 51, 440-450
    • (2010) Environ. Mol. Mutagen. , vol.51 , pp. 440-450
    • Wallace, D.C.1
  • 88
    • 0027082452 scopus 로고
    • The role of mitochondrial DNA rearrangements in aging and human diseases
    • Osiewacz, H. D., and Hermanns, J. (1992) The role of mitochondrial DNA rearrangements in aging and human diseases. Aging 4, 273-286
    • (1992) Aging , vol.4 , pp. 273-286
    • Osiewacz, H.D.1    Hermanns, J.2
  • 89
    • 0030826910 scopus 로고    scopus 로고
    • Genetic regulation of aging
    • Osiewacz, H. D. (1997) Genetic regulation of aging. J. Mol. Med. 75, 715-727
    • (1997) J. Mol. Med. , vol.75 , pp. 715-727
    • Osiewacz, H.D.1
  • 90
    • 84899766412 scopus 로고    scopus 로고
    • Identification of autophagy as a longevity-assurance mechanism in the aging model Podospora anserina
    • Knuppertz, L., Hamann, A., Pampaloni, F., Stelzer, E., and Osiewacz, H. D. (2014) Identification of autophagy as a longevity-assurance mechanism in the aging model Podospora anserina. Autophagy 10, 822-834
    • (2014) Autophagy , vol.10 , pp. 822-834
    • Knuppertz, L.1    Hamann, A.2    Pampaloni, F.3    Stelzer, E.4    Osiewacz, H.D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.