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Volumn 31, Issue 5, 2010, Pages 454-460

Oxidative stress-mediated inhibition of brain creatine kinase activity by methylmercury

Author keywords

Creatine kinase; Methylmercury; Neurotoxicity

Indexed keywords

CARBONYL DERIVATIVE; CREATINE KINASE; METHYLMERCURY; REACTIVE OXYGEN METABOLITE; THIOL;

EID: 84984549114     PISSN: 0161813X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neuro.2010.05.012     Document Type: Article
Times cited : (56)

References (67)
  • 1
    • 28744435204 scopus 로고    scopus 로고
    • Acute cytotoxic effects of mercuric compounds in cultured astrocytes prepared from cerebral hemisphere and cerebellum of newborn rats
    • Adachi T., Kunimoto M. Acute cytotoxic effects of mercuric compounds in cultured astrocytes prepared from cerebral hemisphere and cerebellum of newborn rats. Biol Pharm Bull 2005, 28:2308-2311.
    • (2005) Biol Pharm Bull , vol.28 , pp. 2308-2311
    • Adachi, T.1    Kunimoto, M.2
  • 2
    • 0024963096 scopus 로고
    • Further characterization of contact sites from mitochondria of different tissues: topology of peripheral kinases
    • Adams V., Bosch W., Schlegel J., Wallimann T., Brdiczka D. Further characterization of contact sites from mitochondria of different tissues: topology of peripheral kinases. Biochim Biophys Acta 1989, 981:213-225.
    • (1989) Biochim Biophys Acta , vol.981 , pp. 213-225
    • Adams, V.1    Bosch, W.2    Schlegel, J.3    Wallimann, T.4    Brdiczka, D.5
  • 3
    • 0034024347 scopus 로고    scopus 로고
    • Oxidative modification of creatine kinase BB in Alzheimer's disease brain
    • Aksenov M., Aksenova M., Butterfield D.A., Markesbery W.R. Oxidative modification of creatine kinase BB in Alzheimer's disease brain. J Neurochem 2000, 74:2520-2527.
    • (2000) J Neurochem , vol.74 , pp. 2520-2527
    • Aksenov, M.1    Aksenova, M.2    Butterfield, D.A.3    Markesbery, W.R.4
  • 4
    • 0035909948 scopus 로고    scopus 로고
    • Different responses of astrocytes and neurons to nitric oxide: the role of glycolytically generated ATP in astrocyte protection
    • Almeida A., Almeida J., Bolanos J.P., Moncada S. Different responses of astrocytes and neurons to nitric oxide: the role of glycolytically generated ATP in astrocyte protection. Proc Natl Acad Sci USA 2001, 98:15294-15299.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 15294-15299
    • Almeida, A.1    Almeida, J.2    Bolanos, J.P.3    Moncada, S.4
  • 5
    • 0038608272 scopus 로고    scopus 로고
    • Metabolic consequences of functional complexes of mitochondria, myofibrils and sarcoplasmic reticulum in muscle cells
    • Andrienko T., Kuznetsov A.V., Kaambre T., Usson Y., Orosco A., Appaix F., et al. Metabolic consequences of functional complexes of mitochondria, myofibrils and sarcoplasmic reticulum in muscle cells. J Exp Biol 2003, 206:2059-2072.
    • (2003) J Exp Biol , vol.206 , pp. 2059-2072
    • Andrienko, T.1    Kuznetsov, A.V.2    Kaambre, T.3    Usson, Y.4    Orosco, A.5    Appaix, F.6
  • 6
    • 0023748960 scopus 로고
    • Uptake of methylmercury in the rat brain: effects of amino acids
    • Aschner M., Clarkson T.W. Uptake of methylmercury in the rat brain: effects of amino acids. Brain Res 1988, 462:31-39.
    • (1988) Brain Res , vol.462 , pp. 31-39
    • Aschner, M.1    Clarkson, T.W.2
  • 7
    • 84984577456 scopus 로고    scopus 로고
    • Involvement of glutamate and reactive oxygen species in methylmercury neurotoxicity
    • Aschner M., Syversen T., Souza D.O., Rocha J.B., Farina M. Involvement of glutamate and reactive oxygen species in methylmercury neurotoxicity. Braz J Med Biol Res 2007, 40:285-291.
    • (2007) Braz J Med Biol Res , vol.40 , pp. 285-291
    • Aschner, M.1    Syversen, T.2    Souza, D.O.3    Rocha, J.B.4    Farina, M.5
  • 8
    • 0028206137 scopus 로고
    • Mechanisms of methylmercury-induced neurotoxicity
    • Atchison W.D., Hare M.F. Mechanisms of methylmercury-induced neurotoxicity. FASEB J 1994, 8:622-629.
    • (1994) FASEB J , vol.8 , pp. 622-629
    • Atchison, W.D.1    Hare, M.F.2
  • 10
    • 0034237719 scopus 로고    scopus 로고
    • Energetics in the pathogenesis of neurodegenerative diseases
    • Beal M.F. Energetics in the pathogenesis of neurodegenerative diseases. Trends Neurosci 2000, 23:298-304.
    • (2000) Trends Neurosci , vol.23 , pp. 298-304
    • Beal, M.F.1
  • 11
    • 0036525567 scopus 로고    scopus 로고
    • Coenzyme Q10 as a possible treatment for neurodegenerative diseases
    • Beal M.F. Coenzyme Q10 as a possible treatment for neurodegenerative diseases. Free Radical Res 2002, 36:455-460.
    • (2002) Free Radical Res , vol.36 , pp. 455-460
    • Beal, M.F.1
  • 12
    • 0344653616 scopus 로고    scopus 로고
    • Complexes between porin, hexokinase, mitochondrial creatine kinase and adenylate translocator display properties of the permeability transition pore. Implication for regulation of permeability transition by the kinases
    • Beutner G., Ruck A., Riede B., Brdiczka D. Complexes between porin, hexokinase, mitochondrial creatine kinase and adenylate translocator display properties of the permeability transition pore. Implication for regulation of permeability transition by the kinases. Biochim Biophys Acta 1998, 1368:7-18.
    • (1998) Biochim Biophys Acta , vol.1368 , pp. 7-18
    • Beutner, G.1    Ruck, A.2    Riede, B.3    Brdiczka, D.4
  • 13
    • 84984537116 scopus 로고    scopus 로고
    • Effects of 2,3-dimercapto-1-propanesulfonic acid (DMPS) on methylmercury-induced locomotor deficits and cerebellar toxicity in mice
    • Carvalho M.C., Franco J.L., Ghizoni H., Kobus K., Nazari E.M., Rocha J.B., et al. Effects of 2,3-dimercapto-1-propanesulfonic acid (DMPS) on methylmercury-induced locomotor deficits and cerebellar toxicity in mice. Toxicology 2007, 239:195-203.
    • (2007) Toxicology , vol.239 , pp. 195-203
    • Carvalho, M.C.1    Franco, J.L.2    Ghizoni, H.3    Kobus, K.4    Nazari, E.M.5    Rocha, J.B.6
  • 14
    • 0024540448 scopus 로고
    • The effects of methylmercury on the developing brain
    • Choi B.H. The effects of methylmercury on the developing brain. Prog Neurobiol 1989, 32:447-470.
    • (1989) Prog Neurobiol , vol.32 , pp. 447-470
    • Choi, B.H.1
  • 15
    • 33745915895 scopus 로고    scopus 로고
    • The toxicology of mercury and its chemical compounds
    • Clarkson T.W., Magos L. The toxicology of mercury and its chemical compounds. Crit Rev Toxicol 2006, 36:609-662.
    • (2006) Crit Rev Toxicol , vol.36 , pp. 609-662
    • Clarkson, T.W.1    Magos, L.2
  • 16
    • 0142213730 scopus 로고    scopus 로고
    • The toxicology of mercury-current exposures and clinical manifestations
    • Clarkson T.W., Magos L., Myers G.J. The toxicology of mercury-current exposures and clinical manifestations. N Engl J Med 2003, 349:1731-1737.
    • (2003) N Engl J Med , vol.349 , pp. 1731-1737
    • Clarkson, T.W.1    Magos, L.2    Myers, G.J.3
  • 17
    • 0030792637 scopus 로고    scopus 로고
    • Multiple roles of glutathione in the central nervous system
    • Cooper A.J., Kristal B.S. Multiple roles of glutathione in the central nervous system. Biol Chem 1997, 378:793-802.
    • (1997) Biol Chem , vol.378 , pp. 793-802
    • Cooper, A.J.1    Kristal, B.S.2
  • 18
    • 0036235795 scopus 로고    scopus 로고
    • Role of creatine kinase in cardiac excitation-contraction coupling: studies in creatine kinase-deficient mice
    • Crozatier B., Badoual T., Boehm E., Ennezat P.V., Guenoun T., Su J., et al. Role of creatine kinase in cardiac excitation-contraction coupling: studies in creatine kinase-deficient mice. FASEB J 2002, 16:653-660.
    • (2002) FASEB J , vol.16 , pp. 653-660
    • Crozatier, B.1    Badoual, T.2    Boehm, E.3    Ennezat, P.V.4    Guenoun, T.5    Su, J.6
  • 19
    • 0028606987 scopus 로고
    • Astrocytes as mediators of methylmercury neurotoxicity: effects on d-aspartate and serotonin uptake
    • Dave V., Mullaney K.J., Goderie S., Kimelberg H.K., Aschner M. Astrocytes as mediators of methylmercury neurotoxicity: effects on d-aspartate and serotonin uptake. Dev Neurosci 1994, 16:222-231.
    • (1994) Dev Neurosci , vol.16 , pp. 222-231
    • Dave, V.1    Mullaney, K.J.2    Goderie, S.3    Kimelberg, H.K.4    Aschner, M.5
  • 22
    • 0038381490 scopus 로고    scopus 로고
    • Inhibition of the mitochondrial permeability transition by creatine kinase substrates. Requirement for microcompartmentation
    • Dolder M., Walzel B., Speer O., Schlattner U., Wallimann T. Inhibition of the mitochondrial permeability transition by creatine kinase substrates. Requirement for microcompartmentation. J Biol Chem 2003, 278:17760-17766.
    • (2003) J Biol Chem , vol.278 , pp. 17760-17766
    • Dolder, M.1    Walzel, B.2    Speer, O.3    Schlattner, U.4    Wallimann, T.5
  • 24
    • 0038636003 scopus 로고    scopus 로고
    • Glutathione pathways in the brain
    • Dringen R., Hirrlinger J. Glutathione pathways in the brain. Biol Chem 2003, 384:505-516.
    • (2003) Biol Chem , vol.384 , pp. 505-516
    • Dringen, R.1    Hirrlinger, J.2
  • 25
    • 3042934967 scopus 로고
    • Tissue sulfhydryl groups
    • Ellman G.L. Tissue sulfhydryl groups. Arch Biochem Biophys 1959, 82:70-77.
    • (1959) Arch Biochem Biophys , vol.82 , pp. 70-77
    • Ellman, G.L.1
  • 26
    • 35348993447 scopus 로고    scopus 로고
    • Protective effects of Polygala paniculata extract against methylmercury-induced neurotoxicity in mice
    • Farina M., Franco J.L., Ribas C.M., Meotti F.C., Missau F.C., Pizzolatti M.G., et al. Protective effects of Polygala paniculata extract against methylmercury-induced neurotoxicity in mice. J Pharm Pharmacol 2005, 57:1503-1508.
    • (2005) J Pharm Pharmacol , vol.57 , pp. 1503-1508
    • Farina, M.1    Franco, J.L.2    Ribas, C.M.3    Meotti, F.C.4    Missau, F.C.5    Pizzolatti, M.G.6
  • 27
    • 74949138312 scopus 로고    scopus 로고
    • Probucol increases glutathione peroxidase-1 activity and displays long-lasting protection against methylmercury toxicity in cerebellar granule cells
    • Farina M., Campos F., Vendrell I., Berenguer J., Barzi M., Pons S., et al. Probucol increases glutathione peroxidase-1 activity and displays long-lasting protection against methylmercury toxicity in cerebellar granule cells. Toxicol Sci 2009, 112:416-426.
    • (2009) Toxicol Sci , vol.112 , pp. 416-426
    • Farina, M.1    Campos, F.2    Vendrell, I.3    Berenguer, J.4    Barzi, M.5    Pons, S.6
  • 30
    • 67649998477 scopus 로고    scopus 로고
    • Methylmercury neurotoxicity is associated with inhibition of the antioxidant enzyme glutathione peroxidase
    • Franco J.L., Posser T., Dunkley P.R., Dickson P.W., Mattos J.J., Martins R., et al. Methylmercury neurotoxicity is associated with inhibition of the antioxidant enzyme glutathione peroxidase. Free Radical Biol Med 2009, 47:449-457.
    • (2009) Free Radical Biol Med , vol.47 , pp. 449-457
    • Franco, J.L.1    Posser, T.2    Dunkley, P.R.3    Dickson, P.W.4    Mattos, J.J.5    Martins, R.6
  • 32
    • 0000380025 scopus 로고    scopus 로고
    • Minamata disease and other mercury syndromes
    • CRC Press, Boca Raton, L.W. Chang (Ed.)
    • Hamada R., Osame M. Minamata disease and other mercury syndromes. Toxicology of metals 1996, 337-351. CRC Press, Boca Raton. L.W. Chang (Ed.).
    • (1996) Toxicology of metals , pp. 337-351
    • Hamada, R.1    Osame, M.2
  • 33
    • 0027724925 scopus 로고
    • Functional aspects of creatine kinase in brain
    • Hemmer W., Wallimann T. Functional aspects of creatine kinase in brain. Dev Neurosci 1993, 15:249-260.
    • (1993) Dev Neurosci , vol.15 , pp. 249-260
    • Hemmer, W.1    Wallimann, T.2
  • 34
    • 50549160763 scopus 로고
    • A method for the estimation of serum creatine kinase and its use in comparing creatine kinase and aldolase activity in normal and pathological sera
    • Hughes B.P. A method for the estimation of serum creatine kinase and its use in comparing creatine kinase and aldolase activity in normal and pathological sera. Clin Chim Acta 1962, 7:597-603.
    • (1962) Clin Chim Acta , vol.7 , pp. 597-603
    • Hughes, B.P.1
  • 35
    • 78651053970 scopus 로고
    • Focal cerebellar and cerebellar atrophy in a human subject due to organic mercury compounds
    • Hunter D., Russell D.S. Focal cerebellar and cerebellar atrophy in a human subject due to organic mercury compounds. J Neurol Neurosurg Psychiatry 1954, 17:235-241.
    • (1954) J Neurol Neurosurg Psychiatry , vol.17 , pp. 235-241
    • Hunter, D.1    Russell, D.S.2
  • 36
    • 0042734413 scopus 로고    scopus 로고
    • Impaired intracellular energetic communication in muscles from creatine kinase and adenylate kinase (M-CK/AK1) double knock-out mice
    • Janssen E., Terzic A., Wieringa B., Dzeja P.P. Impaired intracellular energetic communication in muscles from creatine kinase and adenylate kinase (M-CK/AK1) double knock-out mice. J Biol Chem 2003, 278:30441-30449.
    • (2003) J Biol Chem , vol.278 , pp. 30441-30449
    • Janssen, E.1    Terzic, A.2    Wieringa, B.3    Dzeja, P.P.4
  • 37
    • 33846249322 scopus 로고    scopus 로고
    • Role of glutathione in determining the differential sensitivity between the cortical and cerebellar regions towards mercury-induced oxidative stress
    • Kaur P., Aschner M., Syversen T. Role of glutathione in determining the differential sensitivity between the cortical and cerebellar regions towards mercury-induced oxidative stress. Toxicology 2007, 230:164-177.
    • (2007) Toxicology , vol.230 , pp. 164-177
    • Kaur, P.1    Aschner, M.2    Syversen, T.3
  • 38
    • 0030598591 scopus 로고    scopus 로고
    • Energy metabolism. Creatine kinase shapes up
    • Kenyon G.L. Energy metabolism. Creatine kinase shapes up. Nature 1996, 381:281-282.
    • (1996) Nature , vol.381 , pp. 281-282
    • Kenyon, G.L.1
  • 39
    • 0032496422 scopus 로고    scopus 로고
    • Rapid and irreversible inhibition of creatine kinase by peroxynitrite
    • Konorev E.A., Hogg N., Kalyanaraman B. Rapid and irreversible inhibition of creatine kinase by peroxynitrite. FEBS Lett 1998, 427:171-174.
    • (1998) FEBS Lett , vol.427 , pp. 171-174
    • Konorev, E.A.1    Hogg, N.2    Kalyanaraman, B.3
  • 40
    • 0034655508 scopus 로고    scopus 로고
    • Free radical induced inactivation of creatine kinase: sites of interaction, protection, and recovery
    • Koufen P., Stark G. Free radical induced inactivation of creatine kinase: sites of interaction, protection, and recovery. Biochim Biophys Acta 2000, 1501:44-50.
    • (2000) Biochim Biophys Acta , vol.1501 , pp. 44-50
    • Koufen, P.1    Stark, G.2
  • 41
    • 26244435816 scopus 로고    scopus 로고
    • Mitochondrial energy metabolism is markedly impaired by d-2-hydroxyglutaric acid in rat tissues
    • Latini A., da Silva C.G., Ferreira G.C., Schuck P.F., Scussiato K., Sarkis J.J., et al. Mitochondrial energy metabolism is markedly impaired by d-2-hydroxyglutaric acid in rat tissues. Mol Genet Metab 2005, 86:188-199.
    • (2005) Mol Genet Metab , vol.86 , pp. 188-199
    • Latini, A.1    da Silva, C.G.2    Ferreira, G.C.3    Schuck, P.F.4    Scussiato, K.5    Sarkis, J.J.6
  • 42
    • 17044455914 scopus 로고    scopus 로고
    • Inborn errors of creatine metabolism and epilepsy: clinical features, diagnosis, and treatment
    • 3S89-97, discussion 83S97
    • Leuzzi V. Inborn errors of creatine metabolism and epilepsy: clinical features, diagnosis, and treatment. J Child Neurol 2002, 17. 3S89-97, discussion 83S97.
    • (2002) J Child Neurol , vol.17
    • Leuzzi, V.1
  • 44
    • 84984573432 scopus 로고    scopus 로고
    • Maternal milk as methylmercury source for suckling mice: neurotoxic effects involved with the cerebellar glutamatergic system
    • Manfroi C.B., Schwalm F.D., Cereser V., Abreu F., Oliveira A., Bizarro L., et al. Maternal milk as methylmercury source for suckling mice: neurotoxic effects involved with the cerebellar glutamatergic system. Toxicol Sci 2004, 81:172-178.
    • (2004) Toxicol Sci , vol.81 , pp. 172-178
    • Manfroi, C.B.1    Schwalm, F.D.2    Cereser, V.3    Abreu, F.4    Oliveira, A.5    Bizarro, L.6
  • 45
    • 35748959328 scopus 로고    scopus 로고
    • Comparative study of activities in reactive oxygen species production/defense system in mitochondria of rat brain and liver, and their susceptibility to methylmercury toxicity
    • Mori N., Yasutake A., Hirayama K. Comparative study of activities in reactive oxygen species production/defense system in mitochondria of rat brain and liver, and their susceptibility to methylmercury toxicity. Arch Toxicol 2007, 81:769-776.
    • (2007) Arch Toxicol , vol.81 , pp. 769-776
    • Mori, N.1    Yasutake, A.2    Hirayama, K.3
  • 46
    • 24044527481 scopus 로고    scopus 로고
    • Effects of methylmercury on primary brain cells in mono- and co-culture
    • Morken T.S., Sonnewald U., Aschner M., Syversen T. Effects of methylmercury on primary brain cells in mono- and co-culture. Toxicol Sci 2005, 87:169-175.
    • (2005) Toxicol Sci , vol.87 , pp. 169-175
    • Morken, T.S.1    Sonnewald, U.2    Aschner, M.3    Syversen, T.4
  • 47
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays
    • Mosmann T. Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J Immunol Methods 1983, 65:55-63.
    • (1983) J Immunol Methods , vol.65 , pp. 55-63
    • Mosmann, T.1
  • 48
    • 11144250046 scopus 로고    scopus 로고
    • Biomolecule-mercury interactions: modalities of DNA base-mercury binding mechanisms. Remediation strategies
    • Onyido I., Norris A.R., Buncel E. Biomolecule-mercury interactions: modalities of DNA base-mercury binding mechanisms. Remediation strategies. Chem Rev 2004, 104:5911-5929.
    • (2004) Chem Rev , vol.104 , pp. 5911-5929
    • Onyido, I.1    Norris, A.R.2    Buncel, E.3
  • 49
    • 0034306267 scopus 로고    scopus 로고
    • Mitochondria, oxygen free radicals, disease and ageing
    • Raha S, Robinson B.H. Mitochondria, oxygen free radicals, disease and ageing. Trends Biochem Sci 2000, 25:502-508.
    • (2000) Trends Biochem Sci , vol.25 , pp. 502-508
    • Raha, S.1    Robinson, B.H.2
  • 50
    • 0028239163 scopus 로고
    • Oxidative damage to proteins: spectrophotometric method for carbonyl assay
    • Reznick A.Z., Packer L. Oxidative damage to proteins: spectrophotometric method for carbonyl assay. Methods Enzymol 1994, 233:357-363.
    • (1994) Methods Enzymol , vol.233 , pp. 357-363
    • Reznick, A.Z.1    Packer, L.2
  • 51
    • 0842345401 scopus 로고    scopus 로고
    • Functional coupling as a basic mechanism of feedback regulation of cardiac energy metabolism
    • Saks V.A., Kuznetsov A.V., Vendelin M., Guerrero K., Kay L., Seppet E.K. Functional coupling as a basic mechanism of feedback regulation of cardiac energy metabolism. Mol Cell Biochem 2004, 256/257:185-199.
    • (2004) Mol Cell Biochem , pp. 185-199
    • Saks, V.A.1    Kuznetsov, A.V.2    Vendelin, M.3    Guerrero, K.4    Kay, L.5    Seppet, E.K.6
  • 53
    • 4344644501 scopus 로고    scopus 로고
    • Free radical formation in cerebral cortical astrocytes in culture induced by methylmercury
    • Shanker G., Aschner J.L., Syversen T., Aschner M. Free radical formation in cerebral cortical astrocytes in culture induced by methylmercury. Brain Res Mol Brain Res 2004, 128:48-57.
    • (2004) Brain Res Mol Brain Res , vol.128 , pp. 48-57
    • Shanker, G.1    Aschner, J.L.2    Syversen, T.3    Aschner, M.4
  • 54
    • 0033562940 scopus 로고    scopus 로고
    • Induction of apoptosis in human T-cells by methyl mercury: temporal relationship between mitochondrial dysfunction and loss of reductive reserve
    • Shenker B.J., Guo T.L., Onyido I., Shapiro I.M. Induction of apoptosis in human T-cells by methyl mercury: temporal relationship between mitochondrial dysfunction and loss of reductive reserve. Toxicol Appl Pharmacol 1999, 157:23-35.
    • (1999) Toxicol Appl Pharmacol , vol.157 , pp. 23-35
    • Shenker, B.J.1    Guo, T.L.2    Onyido, I.3    Shapiro, I.M.4
  • 55
    • 0034663064 scopus 로고    scopus 로고
    • Methylmercury affects multiple subtypes of calcium channels in rat cerebellar granule cells
    • Sirois J.E., Atchison W.D. Methylmercury affects multiple subtypes of calcium channels in rat cerebellar granule cells. Toxicol Appl Pharmacol 2000, 167:1-11.
    • (2000) Toxicol Appl Pharmacol , vol.167 , pp. 1-11
    • Sirois, J.E.1    Atchison, W.D.2
  • 56
    • 0031000775 scopus 로고    scopus 로고
    • PH profiles indicative of rate-limiting nucleophilic displacement in thioltransferase catalysis
    • Srinivasan U., Mieyal P.A., Mieyal J.J. pH profiles indicative of rate-limiting nucleophilic displacement in thioltransferase catalysis. Biochemistry 1997, 36:3199-3206.
    • (1997) Biochemistry , vol.36 , pp. 3199-3206
    • Srinivasan, U.1    Mieyal, P.A.2    Mieyal, J.J.3
  • 57
    • 0030611177 scopus 로고    scopus 로고
    • Altered Ca2+ responses in muscles with combined mitochondrial and cytosolic creatine kinase deficiencies
    • Steeghs K., Benders A., Oerlemans F., de Haan A., Heerschap A., Ruitenbeek W., et al. Altered Ca2+ responses in muscles with combined mitochondrial and cytosolic creatine kinase deficiencies. Cell 1997, 89:93-103.
    • (1997) Cell , vol.89 , pp. 93-103
    • Steeghs, K.1    Benders, A.2    Oerlemans, F.3    de Haan, A.4    Heerschap, A.5    Ruitenbeek, W.6
  • 58
    • 84984577771 scopus 로고    scopus 로고
    • Prenatal methylmercury exposure hampers glutathione antioxidant system ontogenesis and causes long-lasting oxidative stress in the mouse brain
    • Stringari J., Nunes A.K., Franco J.L., Bohrer D., Garcia S.C., Dafre A.L., et al. Prenatal methylmercury exposure hampers glutathione antioxidant system ontogenesis and causes long-lasting oxidative stress in the mouse brain. Toxicol Appl Pharmacol 2008, 227:147-154.
    • (2008) Toxicol Appl Pharmacol , vol.227 , pp. 147-154
    • Stringari, J.1    Nunes, A.K.2    Franco, J.L.3    Bohrer, D.4    Garcia, S.C.5    Dafre, A.L.6
  • 59
    • 0027454486 scopus 로고
    • Immunoelectron microscopic investigation of creatine kinase BB-isoenzyme after cerebral ischemia in gerbils
    • Tomimoto H., Yamamoto K., Homburger H.A., Yanagihara T. Immunoelectron microscopic investigation of creatine kinase BB-isoenzyme after cerebral ischemia in gerbils. Acta Neuropathol 1993, 86:447-455.
    • (1993) Acta Neuropathol , vol.86 , pp. 447-455
    • Tomimoto, H.1    Yamamoto, K.2    Homburger, H.A.3    Yanagihara, T.4
  • 60
    • 36948998989 scopus 로고    scopus 로고
    • Protective effects of resveratrol on hydrogen peroxide induced toxicity in primary cortical astrocyte cultures
    • Vieira de Almeida L.M., Pineiro C.C., Leite M.C., Brolese G., Leal R.B., Gottfried C., et al. Protective effects of resveratrol on hydrogen peroxide induced toxicity in primary cortical astrocyte cultures. Neurochem Res 2008, 33:8-15.
    • (2008) Neurochem Res , vol.33 , pp. 8-15
    • Vieira de Almeida, L.M.1    Pineiro, C.C.2    Leite, M.C.3    Brolese, G.4    Leal, R.B.5    Gottfried, C.6
  • 61
    • 0042381676 scopus 로고    scopus 로고
    • The function of complexes between the outer mitochondrial membrane pore (VDAC) and the adenine nucleotide translocase in regulation of energy metabolism and apoptosis
    • Vyssokikh M.Y., Brdiczka D. The function of complexes between the outer mitochondrial membrane pore (VDAC) and the adenine nucleotide translocase in regulation of energy metabolism and apoptosis. Acta Biochim Pol 2003, 50:389-404.
    • (2003) Acta Biochim Pol , vol.50 , pp. 389-404
    • Vyssokikh, M.Y.1    Brdiczka, D.2
  • 62
    • 84984566469 scopus 로고    scopus 로고
    • Comparative study of quercetin and its two glycoside derivatives quercitrin and rutin against methylmercury (MeHg)-induced ROS production in rat brain slices
    • Wagner C., Vargas A.P., Roos D.H., Morel A.F., Farina M., Nogueira C.W., et al. Comparative study of quercetin and its two glycoside derivatives quercitrin and rutin against methylmercury (MeHg)-induced ROS production in rat brain slices. Arch Toxicol 2009.
    • (2009) Arch Toxicol
    • Wagner, C.1    Vargas, A.P.2    Roos, D.H.3    Morel, A.F.4    Farina, M.5    Nogueira, C.W.6
  • 63
    • 0028017704 scopus 로고
    • Creatine kinase in non-muscle tissues and cells
    • Wallimann T., Hemmer W. Creatine kinase in non-muscle tissues and cells. Mol Cell Biochem 1994, 133/134:193-220.
    • (1994) Mol Cell Biochem , pp. 193-220
    • Wallimann, T.1    Hemmer, W.2
  • 64
    • 0026585611 scopus 로고
    • Intracellular compartmentation, structure and function of creatine kinase isoenzymes in tissues with high and fluctuating energy demands: the 'phosphocreatine circuit' for cellular energy homeostasis
    • Wallimann T., Wyss M., Brdiczka D., Nicolay K., Eppenberger H.M. Intracellular compartmentation, structure and function of creatine kinase isoenzymes in tissues with high and fluctuating energy demands: the 'phosphocreatine circuit' for cellular energy homeostasis. Biochem J 1992, 281:21-40.
    • (1992) Biochem J , vol.281 , pp. 21-40
    • Wallimann, T.1    Wyss, M.2    Brdiczka, D.3    Nicolay, K.4    Eppenberger, H.M.5
  • 65
    • 0035797915 scopus 로고    scopus 로고
    • An unusually low pK(a) for Cys282 in the active site of human muscle creatine kinase
    • Wang P.F., McLeish M.J., Kneen M.M., Lee G., Kenyon G.L. An unusually low pK(a) for Cys282 in the active site of human muscle creatine kinase. Biochemistry 2001, 40:11698-11705.
    • (2001) Biochemistry , vol.40 , pp. 11698-11705
    • Wang, P.F.1    McLeish, M.J.2    Kneen, M.M.3    Lee, G.4    Kenyon, G.L.5
  • 66
    • 0026778172 scopus 로고
    • In situ compartmentation of creatine kinase in intact sarcomeric muscle: the acto-myosin overlap zone as a molecular sieve
    • Wegmann G., Zanolla E., Eppenberger H.M., Wallimann T. In situ compartmentation of creatine kinase in intact sarcomeric muscle: the acto-myosin overlap zone as a molecular sieve. J Muscle Res Cell Motil 1992, 13:420-435.
    • (1992) J Muscle Res Cell Motil , vol.13 , pp. 420-435
    • Wegmann, G.1    Zanolla, E.2    Eppenberger, H.M.3    Wallimann, T.4


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