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Volumn 38, Issue 2, 2005, Pages 175-188

Mitochondrial proteomics in free radical research

Author keywords

Alcohol; Blue native gel electrophoresis; Free radical; Mitochondria; Oxidative and nitrosative stress; Posttranslational modifications; Proteomics

Indexed keywords

SCAVENGER;

EID: 10644231017     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2004.10.011     Document Type: Review
Times cited : (62)

References (105)
  • 1
    • 2442555970 scopus 로고    scopus 로고
    • The protein import machinery of mitochondria
    • N. Wiedemann, A.E. Frazier, and N. Pfanner The protein import machinery of mitochondria J. Biol. Chem. 279 2004 14473 14476
    • (2004) J. Biol. Chem. , vol.279 , pp. 14473-14476
    • Wiedemann, N.1    Frazier, A.E.2    Pfanner, N.3
  • 2
    • 0347753801 scopus 로고    scopus 로고
    • Proteomics and mass spectrometry in nutrition research
    • H. Kim, G.P. Page, and S. Barnes Proteomics and mass spectrometry in nutrition research Nutrition 20 2004 155 165
    • (2004) Nutrition , vol.20 , pp. 155-165
    • Kim, H.1    Page, G.P.2    Barnes, S.3
  • 3
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • R. Aebersold, and M. Mann Mass spectrometry-based proteomics Nature 422 2003 198 207
    • (2003) Nature , vol.422 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 4
    • 56249089717 scopus 로고    scopus 로고
    • Mass spectrometric approaches to quantitative proteomics
    • S. Sechi Mass spectrometric approaches to quantitative proteomics Contrib. Nephrol. 141 2004 59 78
    • (2004) Contrib. Nephrol. , vol.141 , pp. 59-78
    • Sechi, S.1
  • 5
    • 0043198426 scopus 로고    scopus 로고
    • Proteomic tools for quantitation by mass spectrometry
    • J. Lill Proteomic tools for quantitation by mass spectrometry Mass Spectrom. Rev. 22 2003 182 194
    • (2003) Mass Spectrom. Rev. , vol.22 , pp. 182-194
    • Lill, J.1
  • 6
    • 0037337308 scopus 로고    scopus 로고
    • The application of mass spectrometry to membrane proteomics
    • C.C. Wu, and J.R. Yates III The application of mass spectrometry to membrane proteomics Nat. Biotechnol. 21 2003 262 267
    • (2003) Nat. Biotechnol. , vol.21 , pp. 262-267
    • Wu, C.C.1    Yates III, J.R.2
  • 8
    • 0034066471 scopus 로고    scopus 로고
    • Membrane proteins and proteomics: Un amour impossible?
    • V. Santoni, M. Molloy, and T. Rabilloud Membrane proteins and proteomics: un amour impossible? Electrophoresis 21 2000 1054 1070
    • (2000) Electrophoresis , vol.21 , pp. 1054-1070
    • Santoni, V.1    Molloy, M.2    Rabilloud, T.3
  • 9
    • 0035044161 scopus 로고    scopus 로고
    • A novel subfractionation approach for mitochondrial proteins: A three-dimensional mitochondrial proteome map
    • B.J. Hanson, B. Schulenberg, W.F. Patton, and R.A. Capaldi A novel subfractionation approach for mitochondrial proteins: a three-dimensional mitochondrial proteome map Electrophoresis 22 2001 950 959
    • (2001) Electrophoresis , vol.22 , pp. 950-959
    • Hanson, B.J.1    Schulenberg, B.2    Patton, W.F.3    Capaldi, R.A.4
  • 10
    • 0036766965 scopus 로고    scopus 로고
    • An alternative strategy to determine the mitochondrial proteome using sucrose gradient fractionation and 1D PAGE on highly purified human heart mitochondria
    • S.W. Taylor, D.E. Warnock, G.M. Glenn, B. Zhang, E. Fahy, S.P. Gaucher, R.A. Capaldi, B.W. Gibson, and S.S. Ghosh An alternative strategy to determine the mitochondrial proteome using sucrose gradient fractionation and 1D PAGE on highly purified human heart mitochondria J. Proteome Res. 1 2002 451 458
    • (2002) J. Proteome Res. , vol.1 , pp. 451-458
    • Taylor, S.W.1    Warnock, D.E.2    Glenn, G.M.3    Zhang, B.4    Fahy, E.5    Gaucher, S.P.6    Capaldi, R.A.7    Gibson, B.W.8    Ghosh, S.S.9
  • 13
    • 0026409298 scopus 로고
    • Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form
    • H. Schagger, and G. von Jagow Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form Anal. Biochem. 199 1991 223 231
    • (1991) Anal. Biochem. , vol.199 , pp. 223-231
    • Schagger, H.1    Von Jagow, G.2
  • 14
    • 0029924286 scopus 로고    scopus 로고
    • Electrophoretic techniques for isolation and quantification of oxidative phosphorylation complexes from human tissues
    • H. Schagger Electrophoretic techniques for isolation and quantification of oxidative phosphorylation complexes from human tissues Methods Enzymol. 264 1996 555 566
    • (1996) Methods Enzymol. , vol.264 , pp. 555-566
    • Schagger, H.1
  • 15
    • 0036668515 scopus 로고    scopus 로고
    • High throughput two-dimensional blue-native electrophoresis: A tool for functional proteomics of mitochondria and signaling complexes
    • P.S. Brookes, A. Pinner, A. Ramachandran, L. Coward, S. Barnes, H. Kim, and V.M. Darley-Usmar High throughput two-dimensional blue-native electrophoresis: a tool for functional proteomics of mitochondria and signaling complexes Proteomics 2 2002 969 977
    • (2002) Proteomics , vol.2 , pp. 969-977
    • Brookes, P.S.1    Pinner, A.2    Ramachandran, A.3    Coward, L.4    Barnes, S.5    Kim, H.6    Darley-Usmar, V.M.7
  • 17
    • 0037072739 scopus 로고    scopus 로고
    • A functionally active human F1F0 ATPase can be purified by immunocapture from heart tissue and fibroblast cell lines: Subunit structure and activity studies
    • R. Aggeler, J. Coons, S.W. Taylor, S.S. Ghosh, J.J. Garcia, R.A. Capaldi, and M.F. Marusich A functionally active human F1F0 ATPase can be purified by immunocapture from heart tissue and fibroblast cell lines: subunit structure and activity studies J. Biol. Chem. 277 2002 33906 33912
    • (2002) J. Biol. Chem. , vol.277 , pp. 33906-33912
    • Aggeler, R.1    Coons, J.2    Taylor, S.W.3    Ghosh, S.S.4    Garcia, J.J.5    Capaldi, R.A.6    Marusich, M.F.7
  • 18
    • 0037333309 scopus 로고    scopus 로고
    • Immunocapture and microplate-based activity measurement of mammalian pyruvate dehydrogenase complex
    • M. Lib, A. Rodriguez-Mari, M.F. Marusich, and R.A. Capaldi Immunocapture and microplate-based activity measurement of mammalian pyruvate dehydrogenase complex Anal. Biochem. 314 2003 121 127
    • (2003) Anal. Biochem. , vol.314 , pp. 121-127
    • Lib, M.1    Rodriguez-Mari, A.2    Marusich, M.F.3    Capaldi, R.A.4
  • 20
    • 0036138947 scopus 로고    scopus 로고
    • A subset of newly synthesized polypeptides in mitochondria from human endothelial cells exposed to hydroperoxide stress
    • A. Mitsumoto, A. Takeuchi, K. Okawa, and Y. Nakagawa A subset of newly synthesized polypeptides in mitochondria from human endothelial cells exposed to hydroperoxide stress Free Radic. Biol. Med. 32 2002 22 37
    • (2002) Free Radic. Biol. Med. , vol.32 , pp. 22-37
    • Mitsumoto, A.1    Takeuchi, A.2    Okawa, K.3    Nakagawa, Y.4
  • 21
    • 0346458616 scopus 로고    scopus 로고
    • Chronic exposure to nitric oxide alters the free iron pool in endothelial cells: Role of mitochondrial respiratory complexes and heat shock proteins
    • A. Ramachandran, E. Ceaser, and V.M. Darley-Usmar Chronic exposure to nitric oxide alters the free iron pool in endothelial cells: role of mitochondrial respiratory complexes and heat shock proteins Proc. Natl. Acad. Sci. USA 101 2004 384 389
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 384-389
    • Ramachandran, A.1    Ceaser, E.2    Darley-Usmar, V.M.3
  • 22
    • 0031757931 scopus 로고    scopus 로고
    • Acute and chronic ethanol increases reactive oxygen species generation and decreases viability in fresh, isolated rat hepatocytes
    • S.M. Bailey, and C.C. Cunningham Acute and chronic ethanol increases reactive oxygen species generation and decreases viability in fresh, isolated rat hepatocytes Hepatology 28 1998 1318 1326
    • (1998) Hepatology , vol.28 , pp. 1318-1326
    • Bailey, S.M.1    Cunningham, C.C.2
  • 23
    • 0032815325 scopus 로고    scopus 로고
    • Effect of dietary fat on chronic ethanol-induced oxidative stress in hepatocytes
    • S.M. Bailey, and C.C. Cunningham Effect of dietary fat on chronic ethanol-induced oxidative stress in hepatocytes Alcohol. Clin. Exp. Res. 23 1999 1210 1218
    • (1999) Alcohol. Clin. Exp. Res. , vol.23 , pp. 1210-1218
    • Bailey, S.M.1    Cunningham, C.C.2
  • 24
    • 0025312660 scopus 로고
    • The effects of chronic ethanol consumption on hepatic mitochondrial energy metabolism
    • C.C. Cunningham, W.B. Coleman, and P.I. Spach The effects of chronic ethanol consumption on hepatic mitochondrial energy metabolism Alcohol Alcohol. 25 1990 127 136
    • (1990) Alcohol Alcohol. , vol.25 , pp. 127-136
    • Cunningham, C.C.1    Coleman, W.B.2    Spach, P.I.3
  • 25
    • 0028190518 scopus 로고
    • Mitochondrial energy metabolism in chronic alcoholism
    • J.B. Hoek Mitochondrial energy metabolism in chronic alcoholism Curr. Top. Bioenerg. 17 1994 197 241
    • (1994) Curr. Top. Bioenerg. , vol.17 , pp. 197-241
    • Hoek, J.B.1
  • 29
    • 0038121968 scopus 로고    scopus 로고
    • Chronic alcohol consumption increases the senstivity of rat liver mitochondrial respiration to inhibition by nitric oxide
    • A. Venkatraman, S. Shiva, A.J. Davis, S.M. Bailey, P.S. Brookes, and V. Darley-Usmar Chronic alcohol consumption increases the senstivity of rat liver mitochondrial respiration to inhibition by nitric oxide Hepatology 38 2003 141 147
    • (2003) Hepatology , vol.38 , pp. 141-147
    • Venkatraman, A.1    Shiva, S.2    Davis, A.J.3    Bailey, S.M.4    Brookes, P.S.5    Darley-Usmar, V.6
  • 30
    • 0025002623 scopus 로고
    • Effects of chronic ethanol consumption on the synthesis of polypeptides encoded by the hepatic mitochondrial genome
    • W.B. Coleman, and C.C. Cunningham Effects of chronic ethanol consumption on the synthesis of polypeptides encoded by the hepatic mitochondrial genome Biochim. Biophys. Acta 1019 1990 142 150
    • (1990) Biochim. Biophys. Acta , vol.1019 , pp. 142-150
    • Coleman, W.B.1    Cunningham, C.C.2
  • 31
    • 0025909968 scopus 로고
    • Effect of chronic ethanol consumption on hepatic mitochondrial transcription and translation
    • W.B. Coleman, and C.C. Cunningham Effect of chronic ethanol consumption on hepatic mitochondrial transcription and translation Biochim. Biophys. Acta 1058 1991 178 186
    • (1991) Biochim. Biophys. Acta , vol.1058 , pp. 178-186
    • Coleman, W.B.1    Cunningham, C.C.2
  • 33
    • 0033769441 scopus 로고    scopus 로고
    • Effects of chronic ethanol feeding on the protein composition of mitochondrial ribosomes
    • A. Cahill, and C.C. Cunningham Effects of chronic ethanol feeding on the protein composition of mitochondrial ribosomes Electrophoresis 21 2000 3420 3426
    • (2000) Electrophoresis , vol.21 , pp. 3420-3426
    • Cahill, A.1    Cunningham, C.C.2
  • 34
    • 0029826618 scopus 로고    scopus 로고
    • Differential effects of chronic ethanol consumption on hepatic mitochondrial and cytoplasmic ribosomes
    • A. Cahill, D.L. Baio, P.I. Ivester, and C.C. Cunningham Differential effects of chronic ethanol consumption on hepatic mitochondrial and cytoplasmic ribosomes Alcohol. Clin. Exp. Res. 20 1996 1362 1367
    • (1996) Alcohol. Clin. Exp. Res. , vol.20 , pp. 1362-1367
    • Cahill, A.1    Baio, D.L.2    Ivester, P.I.3    Cunningham, C.C.4
  • 35
    • 0036478824 scopus 로고    scopus 로고
    • Altered hepatic mitochondrial ribosome structure following chronic ethanol consumption
    • V.B. Patel, and C.C. Cunningham Altered hepatic mitochondrial ribosome structure following chronic ethanol consumption Arch. Biochem. Biophys. 398 2002 41 50
    • (2002) Arch. Biochem. Biophys. , vol.398 , pp. 41-50
    • Patel, V.B.1    Cunningham, C.C.2
  • 36
    • 0042316795 scopus 로고    scopus 로고
    • Quantitative protein profiling in heart mitochondria from diabetic rats
    • I.V. Turko, and F. Murad Quantitative protein profiling in heart mitochondria from diabetic rats J. Biol. Chem. 278 2003 35844 35849
    • (2003) J. Biol. Chem. , vol.278 , pp. 35844-35849
    • Turko, I.V.1    Murad, F.2
  • 37
    • 0035503501 scopus 로고    scopus 로고
    • Lifespan extension and rescue of spongiform encephalopathy in superoxide dismutase 2 nullizygous mice treated with superoxide dismutase-catalase mimetics
    • S. Melov, S.R. Doctrow, J.A. Schneider, J. Haberson, M. Patel, P.E. Coskun, K. Huffman, D.C. Wallace, and B. Malfroy Lifespan extension and rescue of spongiform encephalopathy in superoxide dismutase 2 nullizygous mice treated with superoxide dismutase-catalase mimetics J. Neurosci. 21 2001 8348 8353
    • (2001) J. Neurosci. , vol.21 , pp. 8348-8353
    • Melov, S.1    Doctrow, S.R.2    Schneider, J.A.3    Haberson, J.4    Patel, M.5    Coskun, P.E.6    Huffman, K.7    Wallace, D.C.8    Malfroy, B.9
  • 38
    • 0942298545 scopus 로고    scopus 로고
    • Endogenous mitochondrial oxidative stress: Neurodegeneration, proteomic analysis, specific respiratory chain defects, and efficacious antioxidant therapy in superoxide dismutase 2 null mice
    • D. Hinerfeld, M.D. Traini, R.P. Weinberger, B. Cochran, S.R. Doctrow, J. Harry, and S. Melov Endogenous mitochondrial oxidative stress: neurodegeneration, proteomic analysis, specific respiratory chain defects, and efficacious antioxidant therapy in superoxide dismutase 2 null mice J. Neurochem. 88 2004 657 667
    • (2004) J. Neurochem. , vol.88 , pp. 657-667
    • Hinerfeld, D.1    Traini, M.D.2    Weinberger, R.P.3    Cochran, B.4    Doctrow, S.R.5    Harry, J.6    Melov, S.7
  • 40
    • 0032506040 scopus 로고    scopus 로고
    • Selective inactivation of alpha-ketoglutarate dehydrogenase and pyruvate dehydrogenase: Reaction of lipoic acid with 4-hydroxy-2-nonenal
    • K.M. Humphries, and L.I. Szweda Selective inactivation of alpha-ketoglutarate dehydrogenase and pyruvate dehydrogenase: reaction of lipoic acid with 4-hydroxy-2-nonenal Biochemistry 37 1998 15835 15841
    • (1998) Biochemistry , vol.37 , pp. 15835-15841
    • Humphries, K.M.1    Szweda, L.I.2
  • 46
    • 0035826898 scopus 로고    scopus 로고
    • Methionine adenosyltransferase 1A knockout mice are predisposed to liver injury and exhibit increased expression of genes involved in proliferation
    • S.C. Lu, L. Alvarez, Z.Z. Huang, L. Chen, W. An, F.J. Corrales, M.A. Avila, G. Kanel, and J.M. Mato Methionine adenosyltransferase 1A knockout mice are predisposed to liver injury and exhibit increased expression of genes involved in proliferation Proc. Natl. Acad. Sci. USA 98 2001 5560 5565
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 5560-5565
    • Lu, S.C.1    Alvarez, L.2    Huang, Z.Z.3    Chen, L.4    An, W.5    Corrales, F.J.6    Avila, M.A.7    Kanel, G.8    Mato, J.M.9
  • 50
    • 0034255470 scopus 로고    scopus 로고
    • Identification of proteins containing cysteine residues that are sensitive to oxidation by hydrogen peroxide at neutral pH
    • J.R. Kim, H.W. Yoon, K.S. Kwon, S.R. Lee, and S.G. Rhee Identification of proteins containing cysteine residues that are sensitive to oxidation by hydrogen peroxide at neutral pH Anal. Biochem. 283 2000 214 221
    • (2000) Anal. Biochem. , vol.283 , pp. 214-221
    • Kim, J.R.1    Yoon, H.W.2    Kwon, K.S.3    Lee, S.R.4    Rhee, S.G.5
  • 51
    • 3843125309 scopus 로고    scopus 로고
    • The biotin switch method for the detection of S-nitrosylated proteins
    • S.R. Jaffrey, and S.H. Snyder The biotin switch method for the detection of S-nitrosylated proteins Sci. STKE PL1 2001 2001
    • (2001) Sci. STKE , vol.1 , pp. 2001
    • Jaffrey, S.R.1    Snyder, S.H.2
  • 53
    • 2942558370 scopus 로고    scopus 로고
    • New insights into protein S-nitrosylation: Mitochondria as a model system
    • M.W. Foster, and J.S. Stamler New insights into protein S-nitrosylation: mitochondria as a model system J. Biol. Chem. 279 2004 25891 25897
    • (2004) J. Biol. Chem. , vol.279 , pp. 25891-25897
    • Foster, M.W.1    Stamler, J.S.2
  • 56
    • 0035477926 scopus 로고    scopus 로고
    • Nitric oxide inhibits mitochondrial NADH:ubiquinone reductase activity through peroxynitrite formation
    • N.A. Riobo, E. Clementi, M. Melani, A. Boveris, E. Cadenas, S. Moncada, and J.J. Poderoso Nitric oxide inhibits mitochondrial NADH:ubiquinone reductase activity through peroxynitrite formation Biochem. J. 359 2001 139 145
    • (2001) Biochem. J. , vol.359 , pp. 139-145
    • Riobo, N.A.1    Clementi, E.2    Melani, M.3    Boveris, A.4    Cadenas, E.5    Moncada, S.6    Poderoso, J.J.7
  • 57
    • 0033621429 scopus 로고    scopus 로고
    • The regulation of mitochondrial oxygen uptake by redox reactions involving nitric oxide and ubiquinol
    • J.J. Poderoso, C. Lisdero, F. Schopfer, N. Riobo, M.C. Carreras, E. Cadenas, and A. Boveris The regulation of mitochondrial oxygen uptake by redox reactions involving nitric oxide and ubiquinol J. Biol. Chem. 274 1999 37709 37716
    • (1999) J. Biol. Chem. , vol.274 , pp. 37709-37716
    • Poderoso, J.J.1    Lisdero, C.2    Schopfer, F.3    Riobo, N.4    Carreras, M.C.5    Cadenas, E.6    Boveris, A.7
  • 58
    • 0028885796 scopus 로고
    • Inhibition of cytochrome c oxidase in turnover by nitric oxide: Mechanism and implications for control of respiration
    • J. Torres, V. Darley-Usmar, and M.T. Wilson Inhibition of cytochrome c oxidase in turnover by nitric oxide: mechanism and implications for control of respiration Biochem. J. 312 Pt. 1 1995 169 173
    • (1995) Biochem. J. , vol.312 , Issue.1 , pp. 169-173
    • Torres, J.1    Darley-Usmar, V.2    Wilson, M.T.3
  • 59
    • 0030821015 scopus 로고    scopus 로고
    • Nitric oxide inhibition of cytochrome oxidase and mitochondrial respiration: Implications for inflammatory, neurodegenerative and ischaemic pathologies
    • G.C. Brown Nitric oxide inhibition of cytochrome oxidase and mitochondrial respiration: implications for inflammatory, neurodegenerative and ischaemic pathologies Mol. Cell. Biochem. 174 1997 189 192
    • (1997) Mol. Cell. Biochem. , vol.174 , pp. 189-192
    • Brown, G.C.1
  • 60
    • 0026453418 scopus 로고
    • Peroxynitrite formation from macrophage-derived nitric oxide
    • H. Ischiropoulos, L. Zhu, and J.S. Beckman Peroxynitrite formation from macrophage-derived nitric oxide Arch. Biochem. Biophys. 298 1992 446 451
    • (1992) Arch. Biochem. Biophys. , vol.298 , pp. 446-451
    • Ischiropoulos, H.1    Zhu, L.2    Beckman, J.S.3
  • 62
    • 0035853685 scopus 로고    scopus 로고
    • Reaction of peroxynitrite with Mn-superoxide dismutase. Role of the metal center in decomposition kinetics and nitration
    • C. Quijano, D. Hernandez-Saavedra, L. Castro, J.M. McCord, B.A. Freeman, and R. Radi Reaction of peroxynitrite with Mn-superoxide dismutase. Role of the metal center in decomposition kinetics and nitration J. Biol. Chem. 276 2001 11631 11638
    • (2001) J. Biol. Chem. , vol.276 , pp. 11631-11638
    • Quijano, C.1    Hernandez-Saavedra, D.2    Castro, L.3    McCord, J.M.4    Freeman, B.A.5    Radi, R.6
  • 63
    • 0032486405 scopus 로고    scopus 로고
    • Inactivation of human manganese-superoxide dismutase by peroxynitrite is caused by exclusive nitration of tyrosine 34 to 3-nitrotyrosine
    • F. Yamakura, H. Taka, T. Fujimura, and K. Murayama Inactivation of human manganese-superoxide dismutase by peroxynitrite is caused by exclusive nitration of tyrosine 34 to 3-nitrotyrosine J. Biol. Chem. 273 1998 14085 14089
    • (1998) J. Biol. Chem. , vol.273 , pp. 14085-14089
    • Yamakura, F.1    Taka, H.2    Fujimura, T.3    Murayama, K.4
  • 64
    • 0029862502 scopus 로고    scopus 로고
    • Nitration and inactivation of manganese superoxide dismutase in chronic rejection of human renal allografts
    • L.A. MacMillan-Crow, J.P. Crow, J.D. Kerby, J.S. Beckman, and J.A. Thompson Nitration and inactivation of manganese superoxide dismutase in chronic rejection of human renal allografts Proc. Natl. Acad. Sci. USA 93 1996 11853 11858
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 11853-11858
    • MacMillan-Crow, L.A.1    Crow, J.P.2    Kerby, J.D.3    Beckman, J.S.4    Thompson, J.A.5
  • 66
    • 0029998238 scopus 로고    scopus 로고
    • Differential inhibitory action of nitric oxide and peroxynitrite on mitochondrial electron transport
    • A. Cassina, and R. Radi Differential inhibitory action of nitric oxide and peroxynitrite on mitochondrial electron transport Arch. Biochem. Biophys. 328 1996 309 316
    • (1996) Arch. Biochem. Biophys. , vol.328 , pp. 309-316
    • Cassina, A.1    Radi, R.2
  • 68
    • 0032808057 scopus 로고    scopus 로고
    • Nitric oxide induces tyrosine nitration and release of cytochrome c preceding an increase of mitochondrial transmembrane potential in macrophages
    • S. Hortelano, A.M. Alvarez, and L. Bosca Nitric oxide induces tyrosine nitration and release of cytochrome c preceding an increase of mitochondrial transmembrane potential in macrophages FASEB J. 13 1999 2311 2317
    • (1999) FASEB J. , vol.13 , pp. 2311-2317
    • Hortelano, S.1    Alvarez, A.M.2    Bosca, L.3
  • 69
    • 0028977904 scopus 로고
    • Kinetics of cytochrome c 2+oxidation by peroxynitrite: Implications for superoxide measurements in nitric oxide-producing biological systems
    • L. Thomson, M. Trujillo, R. Telleri, and R. Radi Kinetics of cytochrome c 2+oxidation by peroxynitrite: implications for superoxide measurements in nitric oxide-producing biological systems Arch. Biochem. Biophys. 319 1995 491 497
    • (1995) Arch. Biochem. Biophys. , vol.319 , pp. 491-497
    • Thomson, L.1    Trujillo, M.2    Telleri, R.3    Radi, R.4
  • 72
    • 0346218261 scopus 로고    scopus 로고
    • Cytochrome c: A catalyst and target of nitrite-hydrogen peroxide-dependent protein nitration
    • L. Castro, J.P. Eiserich, S. Sweeney, R. Radi, and B.A. Freeman Cytochrome c: a catalyst and target of nitrite-hydrogen peroxide-dependent protein nitration Arch. Biochem. Biophys. 421 2004 99 107
    • (2004) Arch. Biochem. Biophys. , vol.421 , pp. 99-107
    • Castro, L.1    Eiserich, J.P.2    Sweeney, S.3    Radi, R.4    Freeman, B.A.5
  • 74
    • 0141706702 scopus 로고    scopus 로고
    • Protein tyrosine nitration in the mitochondria from diabetic mouse heart. Implications to dysfunctional mitochondria in diabetes
    • I.V. Turko, L. Li, K.S. Aulak, D.J. Stuehr, J.Y. Chang, and F. Murad Protein tyrosine nitration in the mitochondria from diabetic mouse heart. Implications to dysfunctional mitochondria in diabetes J. Biol. Chem. 278 2003 33972 33977
    • (2003) J. Biol. Chem. , vol.278 , pp. 33972-33977
    • Turko, I.V.1    Li, L.2    Aulak, K.S.3    Stuehr, D.J.4    Chang, J.Y.5    Murad, F.6
  • 75
    • 0345683544 scopus 로고    scopus 로고
    • The assumption that nitric oxide inhibits mitochondrial ATP synthesis is correct
    • P.S. Brookes, J.P. Bolanos, and S.J. Heales The assumption that nitric oxide inhibits mitochondrial ATP synthesis is correct FEBS Lett. 446 1999 261 263
    • (1999) FEBS Lett. , vol.446 , pp. 261-263
    • Brookes, P.S.1    Bolanos, J.P.2    Heales, S.J.3
  • 76
    • 3042646339 scopus 로고    scopus 로고
    • Rapid and selective oxygen-regulated protein tyrosine denitration and nitration in mitochondria
    • T. Koeck, X. Fu, S.L. Hazen, J.W. Crabb, D.J. Stuehr, and K.S. Aulak Rapid and selective oxygen-regulated protein tyrosine denitration and nitration in mitochondria J. Biol. Chem. 279 2004 27257 27262
    • (2004) J. Biol. Chem. , vol.279 , pp. 27257-27262
    • Koeck, T.1    Fu, X.2    Hazen, S.L.3    Crabb, J.W.4    Stuehr, D.J.5    Aulak, K.S.6
  • 78
    • 0141510019 scopus 로고    scopus 로고
    • Oxidative damage to mitochondrial complex I due to peroxynitrite: Identification of reactive tyrosines by mass spectrometry
    • J. Murray, S.W. Taylor, B. Zhang, S.S. Ghosh, and R.A. Capaldi Oxidative damage to mitochondrial complex I due to peroxynitrite: identification of reactive tyrosines by mass spectrometry J. Biol. Chem. 278 2003 37223 37230
    • (2003) J. Biol. Chem. , vol.278 , pp. 37223-37230
    • Murray, J.1    Taylor, S.W.2    Zhang, B.3    Ghosh, S.S.4    Capaldi, R.A.5
  • 79
    • 0038820056 scopus 로고    scopus 로고
    • Oxidative post-translational modification of tryptophan residues in cardiac mitochondrial proteins
    • S.W. Taylor, E. Fahy, J. Murray, R.A. Capaldi, and S.S. Ghosh Oxidative post-translational modification of tryptophan residues in cardiac mitochondrial proteins J. Biol. Chem. 278 2003 19587 19590
    • (2003) J. Biol. Chem. , vol.278 , pp. 19587-19590
    • Taylor, S.W.1    Fahy, E.2    Murray, J.3    Capaldi, R.A.4    Ghosh, S.S.5
  • 80
    • 0027326559 scopus 로고
    • Immunochemical detection of 4-hydroxynonenal protein adducts in oxidized hepatocytes
    • K. Uchida, L.I. Szweda, H.Z. Chae, and E.R. Stadtman Immunochemical detection of 4-hydroxynonenal protein adducts in oxidized hepatocytes Proc. Natl. Acad. Sci. USA 90 1993 8742 8746
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8742-8746
    • Uchida, K.1    Szweda, L.I.2    Chae, H.Z.3    Stadtman, E.R.4
  • 81
    • 0037082350 scopus 로고    scopus 로고
    • Role of malondialdehyde-acetaldehyde adducts in liver injury
    • D.J. Tuma Role of malondialdehyde-acetaldehyde adducts in liver injury Free Radic. Biol. Med. 32 2002 303 308
    • (2002) Free Radic. Biol. Med. , vol.32 , pp. 303-308
    • Tuma, D.J.1
  • 82
    • 0030751667 scopus 로고    scopus 로고
    • Prooxidant-initiated lipid peroxidation in isolated rat hepatocytes: Detection of 4-hydroxynonenal- and malondialdehyde-protein adducts
    • D.P. Hartley, D.J. Kroll, and D.R. Petersen Prooxidant-initiated lipid peroxidation in isolated rat hepatocytes: detection of 4-hydroxynonenal- and malondialdehyde-protein adducts Chem. Res. Toxicol. 10 1997 895 905
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 895-905
    • Hartley, D.P.1    Kroll, D.J.2    Petersen, D.R.3
  • 83
    • 0025814980 scopus 로고
    • Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes
    • H. Esterbauer, R.J. Schaur, and H. Zollner Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes Free Radic. Biol. Med. 11 1991 81 128
    • (1991) Free Radic. Biol. Med. , vol.11 , pp. 81-128
    • Esterbauer, H.1    Schaur, R.J.2    Zollner, H.3
  • 86
    • 0037411282 scopus 로고    scopus 로고
    • 4-Hydroxy-2-nonenal: A product and mediator of oxidative stress
    • K. Uchida 4-Hydroxy-2-nonenal: a product and mediator of oxidative stress Prog. Lipid Res. 42 2003 318 343
    • (2003) Prog. Lipid Res. , vol.42 , pp. 318-343
    • Uchida, K.1
  • 88
    • 0029986692 scopus 로고    scopus 로고
    • Chemical characterization of a protein-4-hydroxy-2-nonenal cross-link: Immunochemical detection in mitochondria exposed to oxidative stress
    • J.A. Cohn, L. Tsai, B. Friguet, and L.I. Szweda Chemical characterization of a protein-4-hydroxy-2-nonenal cross-link: immunochemical detection in mitochondria exposed to oxidative stress Arch. Biochem. Biophys. 328 1996 158 164
    • (1996) Arch. Biochem. Biophys. , vol.328 , pp. 158-164
    • Cohn, J.A.1    Tsai, L.2    Friguet, B.3    Szweda, L.I.4
  • 89
    • 0036401499 scopus 로고    scopus 로고
    • Selective inactivation of redox-sensitive mitochondrial enzymes during cardiac reperfusion
    • H.A. Sadek, K.M. Humphries, P.A. Szweda, and L.I. Szweda Selective inactivation of redox-sensitive mitochondrial enzymes during cardiac reperfusion Arch. Biochem. Biophys. 406 2002 222 228
    • (2002) Arch. Biochem. Biophys. , vol.406 , pp. 222-228
    • Sadek, H.A.1    Humphries, K.M.2    Szweda, P.A.3    Szweda, L.I.4
  • 90
    • 0345146921 scopus 로고    scopus 로고
    • Reversible inactivation of alpha-ketoglutarate dehydrogenase in response to alterations in the mitochondrial glutathione status
    • A.C. Nulton-Persson, D.W. Starke, J.J. Mieyal, and L.I. Szweda Reversible inactivation of alpha-ketoglutarate dehydrogenase in response to alterations in the mitochondrial glutathione status Biochemistry 42 2003 4235 4242
    • (2003) Biochemistry , vol.42 , pp. 4235-4242
    • Nulton-Persson, A.C.1    Starke, D.W.2    Mieyal, J.J.3    Szweda, L.I.4
  • 91
    • 0142213541 scopus 로고    scopus 로고
    • Age-related increase in 4-hydroxynonenal adduction to rat heart alpha-ketoglutarate dehydrogenase does not cause loss of its catalytic activity
    • R. Moreau, S.H. Heath, C.E. Doneanu, J.G. Lindsay, and T.M. Hagen Age-related increase in 4-hydroxynonenal adduction to rat heart alpha-ketoglutarate dehydrogenase does not cause loss of its catalytic activity Antioxid. Redox Signal. 5 2003 517 527
    • (2003) Antioxid. Redox Signal. , vol.5 , pp. 517-527
    • Moreau, R.1    Heath, S.H.2    Doneanu, C.E.3    Lindsay, J.G.4    Hagen, T.M.5
  • 92
    • 0034060591 scopus 로고    scopus 로고
    • Formation of malondialdehyde adducts in livers of rats exposed to ethanol: Role in ethanol-mediated inhibition of cytochrome c oxidase
    • J.J. Chen, D.R. Petersen, S. Schenker, and G.I. Henderson Formation of malondialdehyde adducts in livers of rats exposed to ethanol: role in ethanol-mediated inhibition of cytochrome c oxidase Alcohol. Clin. Exp. Res. 24 2000 544 552
    • (2000) Alcohol. Clin. Exp. Res. , vol.24 , pp. 544-552
    • Chen, J.J.1    Petersen, D.R.2    Schenker, S.3    Henderson, G.I.4
  • 93
    • 0032996250 scopus 로고    scopus 로고
    • Formation of 4-hydroxynonenal adducts with cytochrome c oxidase in rats following short-term ethanol intake
    • J.J. Chen, N.C. Robinson, S. Schenker, T.A. Frosto, and G.I. Henderson Formation of 4-hydroxynonenal adducts with cytochrome c oxidase in rats following short-term ethanol intake Hepatology 29 1999 1792 1798
    • (1999) Hepatology , vol.29 , pp. 1792-1798
    • Chen, J.J.1    Robinson, N.C.2    Schenker, S.3    Frosto, T.A.4    Henderson, G.I.5
  • 94
    • 0035196175 scopus 로고    scopus 로고
    • Role of 4-hydroxynonenal in modification of cytochrome c oxidase in ischemia/reperfused rat heart
    • J. Chen, G.I. Henderson, and G.L. Freeman Role of 4-hydroxynonenal in modification of cytochrome c oxidase in ischemia/reperfused rat heart J. Mol. Cell. Cardiol. 33 2001 1919 1927
    • (2001) J. Mol. Cell. Cardiol. , vol.33 , pp. 1919-1927
    • Chen, J.1    Henderson, G.I.2    Freeman, G.L.3
  • 96
    • 0242665322 scopus 로고    scopus 로고
    • +-isocitrate dehydrogenase is inactivated through 4-hydroxynonenal adduct formation: An event that precedes hypertrophy development
    • +-isocitrate dehydrogenase is inactivated through 4-hydroxynonenal adduct formation: an event that precedes hypertrophy development J. Biol. Chem. 278 2003 45154 45159
    • (2003) J. Biol. Chem. , vol.278 , pp. 45154-45159
    • Benderdour, M.1    Charron, G.2    Deblois, D.3    Comte, B.4    Des, C.5
  • 97
    • 0025674536 scopus 로고
    • Metal ion-catalyzed oxidation of proteins: Biochemical mechanism and biological consequences
    • E.R. Stadtman Metal ion-catalyzed oxidation of proteins: biochemical mechanism and biological consequences Free Radic. Biol. Med. 9 1990 315 325
    • (1990) Free Radic. Biol. Med. , vol.9 , pp. 315-325
    • Stadtman, E.R.1
  • 98
    • 0031831270 scopus 로고    scopus 로고
    • Reactive oxygen-mediated protein oxidation in aging and disease
    • E.R. Stadtman, and B.S. Berlett Reactive oxygen-mediated protein oxidation in aging and disease Drug Metab. Rev. 30 1998 225 243
    • (1998) Drug Metab. Rev. , vol.30 , pp. 225-243
    • Stadtman, E.R.1    Berlett, B.S.2
  • 99
    • 0030841350 scopus 로고    scopus 로고
    • Protein oxidation in aging, disease, and oxidative stress
    • B.S. Berlett, and E.R. Stadtman Protein oxidation in aging, disease, and oxidative stress J. Biol. Chem. 272 1997 20313 20316
    • (1997) J. Biol. Chem. , vol.272 , pp. 20313-20316
    • Berlett, B.S.1    Stadtman, E.R.2
  • 100
    • 0028291974 scopus 로고
    • Carbonyl assays for determination of oxidatively modified proteins
    • R.L. Levine, J.A. Williams, E.R. Stadtman, and E. Shacter Carbonyl assays for determination of oxidatively modified proteins Methods Enzymol. 233 1994 346 357
    • (1994) Methods Enzymol. , vol.233 , pp. 346-357
    • Levine, R.L.1    Williams, J.A.2    Stadtman, E.R.3    Shacter, E.4
  • 103
    • 3042523891 scopus 로고    scopus 로고
    • Proteomic analysis of carbonylated proteins in two-dimensional gel electrophoresis using avidin-fluorescein affinity staining
    • B.S. Yoo, and F.E. Regnier Proteomic analysis of carbonylated proteins in two-dimensional gel electrophoresis using avidin-fluorescein affinity staining Electrophoresis 25 2004 1334 1341
    • (2004) Electrophoresis , vol.25 , pp. 1334-1341
    • Yoo, B.S.1    Regnier, F.E.2
  • 104
    • 0343294288 scopus 로고    scopus 로고
    • Adaptation of protein carbonyl detection to the requirements of proteome analysis demonstrated for hypoxia/reoxygenation in isolated rat liver mitochondria
    • T. Reinheckel, S. Korn, S. Mohring, W. Augustin, W. Halangk, and L. Schild Adaptation of protein carbonyl detection to the requirements of proteome analysis demonstrated for hypoxia/reoxygenation in isolated rat liver mitochondria Arch. Biochem. Biophys. 376 2000 59 65
    • (2000) Arch. Biochem. Biophys. , vol.376 , pp. 59-65
    • Reinheckel, T.1    Korn, S.2    Mohring, S.3    Augustin, W.4    Halangk, W.5    Schild, L.6


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