메뉴 건너뛰기




Volumn 37, Issue 9, 2017, Pages 1073-1081

Diphenyl diselenide protects against methylmercury-induced inhibition of thioredoxin reductase and glutathione peroxidase in human neuroblastoma cells: a comparison with ebselen

Author keywords

diphenyl diselenide; Ebselen; glutathione peroxidase; methylmercury; neuroblastoma cells; thioredoxin reductase

Indexed keywords

DIPHENYL DISELENIDE; EBSELEN; GLUTATHIONE PEROXIDASE; GLUTATHIONE PEROXIDASE 1; METHYLMERCURY; THIOREDOXIN REDUCTASE; ANTIOXIDANT; BENZENE DERIVATIVE; METHYLMERCURY DERIVATIVE; ORGANOSELENIUM DERIVATIVE; PYRROLE DERIVATIVE;

EID: 85017334905     PISSN: 0260437X     EISSN: 10991263     Source Type: Journal    
DOI: 10.1002/jat.3458     Document Type: Article
Times cited : (31)

References (78)
  • 1
    • 0006895581 scopus 로고    scopus 로고
    • Measurement of thioredoxin and thioredoxin reductase
    • In, Costa LG, Hodgson E, Lawrence DA, Reed DJ, GreenLee WF, (eds)., Wiley, New York
    • Arnér ESJ, Holmgren A. 1999. Measurement of thioredoxin and thioredoxin reductase. In Current Protocols of Toxicology, Costa LG, Hodgson E, Lawrence DA, Reed DJ, GreenLee WF (eds). Wiley: New York; 1190–1194.
    • (1999) Current Protocols of Toxicology , pp. 1190-1194
    • Arnér, E.S.J.1    Holmgren, A.2
  • 2
    • 84984577456 scopus 로고    scopus 로고
    • Involvement of glutamate and reactive oxygen species in methylmercury neurotoxicity
    • Aschner M, Syversen T, Souza DO, Rocha JB, Farina M. 2007. Involvement of glutamate and reactive oxygen species in methylmercury neurotoxicity. Braz. J. Med. Biol. Res. 40(3): 285–291.
    • (2007) Braz. J. Med. Biol. Res. , vol.40 , Issue.3 , pp. 285-291
    • Aschner, M.1    Syversen, T.2    Souza, D.O.3    Rocha, J.B.4    Farina, M.5
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248–254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 79851508904 scopus 로고    scopus 로고
    • Inhibition of the thioredoxin system in the brain and liver of zebra-seabreams exposed to waterborne methylmercury
    • Branco V, Canário J, Holmgren A, Carvalho C. 2011. Inhibition of the thioredoxin system in the brain and liver of zebra-seabreams exposed to waterborne methylmercury. Toxicol. Appl. Pharmacol. 251: 95–103.
    • (2011) Toxicol. Appl. Pharmacol. , vol.251 , pp. 95-103
    • Branco, V.1    Canário, J.2    Holmgren, A.3    Carvalho, C.4
  • 7
    • 84856217140 scopus 로고    scopus 로고
    • Mercury and selenium interaction in vivo: effects on thioredoxin reductase and glutathione peroxidase
    • Branco V, Canário J, Lu J, Holmgren A, Carvalho C. 2012. Mercury and selenium interaction in vivo: effects on thioredoxin reductase and glutathione peroxidase. Free Radic. Biol. Med. 52(4): 781–793.
    • (2012) Free Radic. Biol. Med. , vol.52 , Issue.4 , pp. 781-793
    • Branco, V.1    Canário, J.2    Lu, J.3    Holmgren, A.4    Carvalho, C.5
  • 8
    • 84902013510 scopus 로고    scopus 로고
    • Mitochondrial thioredoxin reductase inhibition, selenium status, and Nrf-2 activation are determinant factors modulating the toxicity of mercury compounds
    • Branco V, Santos AG, Gonçalves J, Lu J, Holmgren A, Carvalho C. 2014. Mitochondrial thioredoxin reductase inhibition, selenium status, and Nrf-2 activation are determinant factors modulating the toxicity of mercury compounds. Free Radic. Biol. Med. 73: 95–105.
    • (2014) Free Radic. Biol. Med. , vol.73 , pp. 95-105
    • Branco, V.1    Santos, A.G.2    Gonçalves, J.3    Lu, J.4    Holmgren, A.5    Carvalho, C.6
  • 10
    • 84905106173 scopus 로고    scopus 로고
    • Sushi consumption rates and mercury levels in sushi: Ethnic and demographic differences in exposure
    • Burger J, Gochfeld M, Jeitner C, Donio M, Pittfield T. 2014. Sushi consumption rates and mercury levels in sushi: Ethnic and demographic differences in exposure. J. Risk Res. 17(8): 981–997.
    • (2014) J. Risk Res. , vol.17 , Issue.8 , pp. 981-997
    • Burger, J.1    Gochfeld, M.2    Jeitner, C.3    Donio, M.4    Pittfield, T.5
  • 11
    • 45549099735 scopus 로고    scopus 로고
    • Inhibition of human thioredoxin system: a molecular mechanism of mercury toxicity
    • Carvalho CML, Chew E, Hashemy SI, Lu J, Holmgren A. 2008. Inhibition of human thioredoxin system: a molecular mechanism of mercury toxicity. J. Biol. Chem. 283: 11913–11923.
    • (2008) J. Biol. Chem. , vol.283 , pp. 11913-11923
    • Carvalho, C.M.L.1    Chew, E.2    Hashemy, S.I.3    Lu, J.4    Holmgren, A.5
  • 12
    • 79251546408 scopus 로고    scopus 로고
    • Effects of selenite and chelating agents on mammalian thioredoxin reductase inhibited by mercury: implications for treatment of mercury poisoning
    • Carvalho CML, Lu J, Zhang X, Arnér ESJ, Holmgren A. 2011. Effects of selenite and chelating agents on mammalian thioredoxin reductase inhibited by mercury: implications for treatment of mercury poisoning. FASEB J. 25: 370–381.
    • (2011) FASEB J. , vol.25 , pp. 370-381
    • Carvalho, C.M.L.1    Lu, J.2    Zhang, X.3    Arnér, E.S.J.4    Holmgren, A.5
  • 13
    • 33745915895 scopus 로고    scopus 로고
    • The toxicology of mercury and its chemical compounds
    • Clarkson TW, Magos L. 2006. The toxicology of mercury and its chemical compounds. Crit. Rev. Toxicol. 36(8): 609–662.
    • (2006) Crit. Rev. Toxicol. , vol.36 , Issue.8 , pp. 609-662
    • Clarkson, T.W.1    Magos, L.2
  • 14
    • 84881017025 scopus 로고    scopus 로고
    • Molecular mechanisms involved in the protective effect of selenocystine against methylmercury-induced cell death in human HepG2 cells
    • Cordero-Herrera I, Cuello S, Goya L, Madrid Y, Bravo L, Cámara C, Ramos S. 2013. Molecular mechanisms involved in the protective effect of selenocystine against methylmercury-induced cell death in human HepG2 cells. Food Chem. Toxicol. 59: 554–563.
    • (2013) Food Chem. Toxicol. , vol.59 , pp. 554-563
    • Cordero-Herrera, I.1    Cuello, S.2    Goya, L.3    Madrid, Y.4    Bravo, L.5    Cámara, C.6    Ramos, S.7
  • 16
    • 36649023534 scopus 로고    scopus 로고
    • Selenium methylselenocysteine protects human hepatoma HepG2 cells against oxidative stress induced by tert-butylhydroperoxide
    • Cuello S, Ramos S, Mateos R, Martin MA, Madrid Y, Camara C, Bravo L, Goy L. 2007. Selenium methylselenocysteine protects human hepatoma HepG2 cells against oxidative stress induced by tert-butylhydroperoxide. Anal. Bioanal. Chem. 389: 2167–2178.
    • (2007) Anal. Bioanal. Chem. , vol.389 , pp. 2167-2178
    • Cuello, S.1    Ramos, S.2    Mateos, R.3    Martin, M.A.4    Madrid, Y.5    Camara, C.6    Bravo, L.7    Goy, L.8
  • 17
    • 84984585621 scopus 로고    scopus 로고
    • The combination of organoselenium compounds and guanosine prevents glutamate-induced oxidative stress in different regions of rat brains
    • Dalla Corte CL, Bastos LL, Dobrachinski F, Rocha JB, Soares FA. 2012. The combination of organoselenium compounds and guanosine prevents glutamate-induced oxidative stress in different regions of rat brains. Brain Res. 1430: 101–111.
    • (2012) Brain Res. , vol.1430 , pp. 101-111
    • Dalla Corte, C.L.1    Bastos, L.L.2    Dobrachinski, F.3    Rocha, J.B.4    Soares, F.A.5
  • 21
    • 84856229200 scopus 로고    scopus 로고
    • Analysis of glutathione-related enzymes
    • In, Costa LG, Hodgson E, Lawrence DA, Reed DJ, GreenLee WF, (eds)., Wiley, New York
    • Esworthy RS, Chu FF, Doroshow JH. 1999. Analysis of glutathione-related enzymes. In Current Protocols of Toxicololy, Costa LG, Hodgson E, Lawrence DA, Reed DJ, GreenLee WF (eds). Wiley: New York; 1142–1146.
    • (1999) Current Protocols of Toxicololy , pp. 1142-1146
    • Esworthy, R.S.1    Chu, F.F.2    Doroshow, J.H.3
  • 22
    • 36049034249 scopus 로고    scopus 로고
    • Selenium-mercury interactions in man and animals
    • Falnoga I, Tusek-Znidaric M. 2007. Selenium-mercury interactions in man and animals. Biol. Trace Elem. Res. 119: 212–220.
    • (2007) Biol. Trace Elem. Res. , vol.119 , pp. 212-220
    • Falnoga, I.1    Tusek-Znidaric, M.2
  • 24
    • 84984538861 scopus 로고    scopus 로고
    • Methylmercury increases glutamate release from brain synaptosomes and glutamate uptake by cortical slices from suckling rat pups: modulatory effect of ebselen
    • Farina M, Dahm KC, Schwalm FD, Brusque AM, Frizzo ME, Zeni G, Souza DO, Rocha JB. 2003b. Methylmercury increases glutamate release from brain synaptosomes and glutamate uptake by cortical slices from suckling rat pups: modulatory effect of ebselen. Toxicol. Sci. 73: 135–140.
    • (2003) Toxicol. Sci. , vol.73 , pp. 135-140
    • Farina, M.1    Dahm, K.C.2    Schwalm, F.D.3    Brusque, A.M.4    Frizzo, M.E.5    Zeni, G.6    Souza, D.O.7    Rocha, J.B.8
  • 25
    • 84984539021 scopus 로고    scopus 로고
    • Additive pro-oxidative effects of methylmercury and ebselen in liver from suckling rat pups
    • Farina M, Soares FA, Zeni G, Souza DO, Rocha JB. 2004. Additive pro-oxidative effects of methylmercury and ebselen in liver from suckling rat pups. Toxicol. Lett. 146(3): 227–235.
    • (2004) Toxicol. Lett. , vol.146 , Issue.3 , pp. 227-235
    • Farina, M.1    Soares, F.A.2    Zeni, G.3    Souza, D.O.4    Rocha, J.B.5
  • 26
    • 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, Suñol C. 2009. Probucol increases glutathione peroxidase-1 activity and displays long-lasting protection against methylmercury toxicity in cerebellar granule cells. Toxicol. Sci. 112(2): 419–426.
    • (2009) Toxicol. Sci. , vol.112 , Issue.2 , pp. 419-426
    • Farina, M.1    Campos, F.2    Vendrell, I.3    Berenguer, J.4    Barzi, M.5    Pons, S.6    Suñol, C.7
  • 28
    • 38149107696 scopus 로고    scopus 로고
    • Mercurial-induced hydrogen peroxide generation in mouse brain mitochondria: protective effects of quercetin
    • Franco JL, Braga HC, Stringari J, Missau FC, Posser T, Mendes BG. 2007. Mercurial-induced hydrogen peroxide generation in mouse brain mitochondria: protective effects of quercetin. Chem. Res. Toxicol. 20: 1919–1926.
    • (2007) Chem. Res. Toxicol. , vol.20 , pp. 1919-1926
    • Franco, J.L.1    Braga, H.C.2    Stringari, J.3    Missau, F.C.4    Posser, T.5    Mendes, B.G.6
  • 30
    • 84984550859 scopus 로고    scopus 로고
    • Diphenyl diselenide and analogs are substrates of cerebral rat thioredoxin reductase: a pathway for their neuroprotective effects
    • Freitas AS, Rocha JB. 2011. Diphenyl diselenide and analogs are substrates of cerebral rat thioredoxin reductase: a pathway for their neuroprotective effects. Neurosci. Lett. 503: 1–5.
    • (2011) Neurosci. Lett. , vol.503 , pp. 1-5
    • Freitas, A.S.1    Rocha, J.B.2
  • 32
    • 84984535996 scopus 로고    scopus 로고
    • reduction of diphenyl diselenide and analogs by mammalian thioredoxin reductase is independent of their gluthathione peroxidase-like activity: A possible novel pathway for their antioxidant activity
    • Freitas AS, Prestes AS, Wagner C, Sudati JH, Alves D, Porciúncula LO, Kade IJ, Rocha JBT. 2010. reduction of diphenyl diselenide and analogs by mammalian thioredoxin reductase is independent of their gluthathione peroxidase-like activity: A possible novel pathway for their antioxidant activity. Molecules 15(11): 7699–7714.
    • (2010) Molecules , vol.15 , Issue.11 , pp. 7699-7714
    • Freitas, A.S.1    Prestes, A.S.2    Wagner, C.3    Sudati, J.H.4    Alves, D.5    Porciúncula, L.O.6    Kade, I.J.7    Rocha, J.B.T.8
  • 33
    • 84922616366 scopus 로고    scopus 로고
    • Methylmercury causes neuronal cell death through the suppression of the TrkA pathway: In vitro and in vivo effects of TrkA pathway activators
    • Fujimura M, Usuki F. 2015. Methylmercury causes neuronal cell death through the suppression of the TrkA pathway: In vitro and in vivo effects of TrkA pathway activators. Toxicol. Appl. Pharmacol. 282(3): 259–266.
    • (2015) Toxicol. Appl. Pharmacol. , vol.282 , Issue.3 , pp. 259-266
    • Fujimura, M.1    Usuki, F.2
  • 36
    • 84874470858 scopus 로고    scopus 로고
    • Mercuric chloride-induced testicular toxicity in rats and the protective role of sodium selenite and vitamin E
    • Kalender S, Uzun FG, Demir F, Uzunhisarcıklı M, Aslanturk A. 2013. Mercuric chloride-induced testicular toxicity in rats and the protective role of sodium selenite and vitamin E. Food Chem. Toxicol. 55: 456–462.
    • (2013) Food Chem. Toxicol. , vol.55 , pp. 456-462
    • Kalender, S.1    Uzun, F.G.2    Demir, F.3    Uzunhisarcıklı, M.4    Aslanturk, A.5
  • 37
    • 84870044559 scopus 로고    scopus 로고
    • Organic selenium supplementation increases mercury excretion and decreases oxidative damage in long-term mercury-exposed residents from Wanshan, China
    • Li YF, Dong Z, Chen C, Li B, Gao Y, Qu L, Wang T, Fu X, Zhao Y, Chai Z. 2012. Organic selenium supplementation increases mercury excretion and decreases oxidative damage in long-term mercury-exposed residents from Wanshan, China. Environ. Sci. Technol. 46: 11313–11318.
    • (2012) Environ. Sci. Technol. , vol.46 , pp. 11313-11318
    • Li, Y.F.1    Dong, Z.2    Chen, C.3    Li, B.4    Gao, Y.5    Qu, L.6    Wang, T.7    Fu, X.8    Zhao, Y.9    Chai, Z.10
  • 38
    • 84903949065 scopus 로고    scopus 로고
    • The protective role of tea polyphenols against methylmercury-induced neurotoxic effects in rat cerebral cortex via inhibition of oxidative stress
    • Liu W, Xu Z, Yang T, Deng Y, Xu B, Feng S, Li Y. 2014. The protective role of tea polyphenols against methylmercury-induced neurotoxic effects in rat cerebral cortex via inhibition of oxidative stress. Free Radic. Res. 48(8): 849–863.
    • (2014) Free Radic. Res. , vol.48 , Issue.8 , pp. 849-863
    • Liu, W.1    Xu, Z.2    Yang, T.3    Deng, Y.4    Xu, B.5    Feng, S.6    Li, Y.7
  • 41
    • 84892366219 scopus 로고    scopus 로고
    • The thioredoxin antioxidant system
    • Lu J, Holmgren A. 2014. The thioredoxin antioxidant system. Free Radic. Biol. Med. 66: 75–87.
    • (2014) Free Radic. Biol. Med. , vol.66 , pp. 75-87
    • Lu, J.1    Holmgren, A.2
  • 42
    • 79957847259 scopus 로고    scopus 로고
    • Involvement of oxidative stress-mediated ERK1/2 and p38 activation regulated mitochondria-dependent apoptotic signals in methylmercury-induced neuronal cell injury
    • Lu TH, Hsieh SY, Yen CC, Wu HC, Chen KL, Hung DZ, Chen CH, Wu CC, Su YC, Chen YW, Liu SH, Huang CF. 2011. Involvement of oxidative stress-mediated ERK1/2 and p38 activation regulated mitochondria-dependent apoptotic signals in methylmercury-induced neuronal cell injury. Toxicol. Lett. 204: 71–80.
    • (2011) Toxicol. Lett. , vol.204 , pp. 71-80
    • Lu, T.H.1    Hsieh, S.Y.2    Yen, C.C.3    Wu, H.C.4    Chen, K.L.5    Hung, D.Z.6    Chen, C.H.7    Wu, C.C.8    Su, Y.C.9    Chen, Y.W.10    Liu, S.H.11    Huang, C.F.12
  • 44
    • 84905642683 scopus 로고    scopus 로고
    • An unsolved puzzle: The complex interplay between methylmercury and fish oil-derived fatty acids within the cardiovascular system
    • Moreira ELG, Farina M. 2014. An unsolved puzzle: The complex interplay between methylmercury and fish oil-derived fatty acids within the cardiovascular system. Toxicol. Res. 3(5): 300–310.
    • (2014) Toxicol. Res. , vol.3 , Issue.5 , pp. 300-310
    • Moreira, E.L.G.1    Farina, M.2
  • 46
    • 84984586927 scopus 로고    scopus 로고
    • Selenium compounds prevent the effects of methylmercury on the in vitro phosphorylation of cytoskeletal proteins in cerebral cortex of young rats
    • Moretto MB, Funchal C, Zeni G, Pessoa-Pureur R, Rocha JB. 2005. Selenium compounds prevent the effects of methylmercury on the in vitro phosphorylation of cytoskeletal proteins in cerebral cortex of young rats. Toxicol. Sci. 85: 639–646.
    • (2005) Toxicol. Sci. , vol.85 , pp. 639-646
    • Moretto, M.B.1    Funchal, C.2    Zeni, G.3    Pessoa-Pureur, R.4    Rocha, J.B.5
  • 48
    • 35748959328 scopus 로고    scopus 로고
    • Mercurial-induced hydrogen peroxide generation in mouse brain mitochondria: protective effects of quercetin
    • Mori N, Yasutake A, Hirayama K. 2007. Mercurial-induced hydrogen peroxide generation in mouse brain mitochondria: protective effects of quercetin. Arch. Toxicol. 81: 769–776.
    • (2007) Arch. Toxicol. , vol.81 , pp. 769-776
    • Mori, N.1    Yasutake, A.2    Hirayama, K.3
  • 49
    • 0031983885 scopus 로고    scopus 로고
    • Immunological effects of occupational exposure to metallic mercury in the population of T-cells and NK-cells
    • Moszczynski P, Rutowski J, Słowinski S, Bem S. 2008. Immunological effects of occupational exposure to metallic mercury in the population of T-cells and NK-cells. Analyst 123: 99–103.
    • (2008) Analyst , vol.123 , pp. 99-103
    • Moszczynski, P.1    Rutowski, J.2    Słowinski, S.3    Bem, S.4
  • 50
    • 0035385139 scopus 로고    scopus 로고
    • Chemistry of biologically important synthetic organoselenium compounds
    • Mugesh G, Dumont WW, Sies H. 2001. Chemistry of biologically important synthetic organoselenium compounds. Chem. Rev. 101: 2125–2179.
    • (2001) Chem. Rev. , vol.101 , pp. 2125-2179
    • Mugesh, G.1    Dumont, W.W.2    Sies, H.3
  • 51
    • 0021185122 scopus 로고
    • A novel biologically active seleno-organic compound-I. Glutathione peroxidase-like activity in vitro and antioxidant capacity of PZ 51 (Ebselen)
    • Muller A, Cadenas E, Graf P, Sies H. 1984. A novel biologically active seleno-organic compound-I. Glutathione peroxidase-like activity in vitro and antioxidant capacity of PZ 51 (Ebselen). Biochem. Pharmacol. 33(20): 3235–3239.
    • (1984) Biochem. Pharmacol. , vol.33 , Issue.20 , pp. 3235-3239
    • Muller, A.1    Cadenas, E.2    Graf, P.3    Sies, H.4
  • 52
    • 84984580672 scopus 로고    scopus 로고
    • Toxicology and pharmacology of selenium: emphasis on synthetic organoselenium compounds
    • Nogueira CW, Rocha JB. 2011. Toxicology and pharmacology of selenium: emphasis on synthetic organoselenium compounds. Arch. Toxicol. 85(11): 1313–1359.
    • (2011) Arch. Toxicol. , vol.85 , Issue.11 , pp. 1313-1359
    • Nogueira, C.W.1    Rocha, J.B.2
  • 53
    • 84984583119 scopus 로고    scopus 로고
    • Organoselenium and organotellurium compounds: pharmacology and toxicology
    • Nogueira CW, Zeni G, Rocha JB. 2004. Organoselenium and organotellurium compounds: pharmacology and toxicology. Chem. Rev. 104: 6255–6286.
    • (2004) Chem. Rev. , vol.104 , pp. 6255-6286
    • Nogueira, C.W.1    Zeni, G.2    Rocha, J.B.3
  • 54
    • 0035584857 scopus 로고    scopus 로고
    • Reactive oxygen species, antioxidants, and the mammalian thioredoxin system
    • Nordberg J, Arnér ES. 2001. Reactive oxygen species, antioxidants, and the mammalian thioredoxin system. Free Radic. Biol. Med. 31(11): 1287–1312.
    • (2001) Free Radic. Biol. Med. , vol.31 , Issue.11 , pp. 1287-1312
    • Nordberg, J.1    Arnér, E.S.2
  • 55
    • 34250318625 scopus 로고    scopus 로고
    • From selenium to selenoproteins: synthesis, identity and their role in human health
    • Papp LV, Lu J, Holmgren A, Khanna KK. 2007. From selenium to selenoproteins: synthesis, identity and their role in human health. Antioxid. Redox Sign. 9: 775–806.
    • (2007) Antioxid. Redox Sign. , vol.9 , pp. 775-806
    • Papp, L.V.1    Lu, J.2    Holmgren, A.3    Khanna, K.K.4
  • 56
    • 84984538763 scopus 로고    scopus 로고
    • Antioxidant effect of diphenyl diselenide against sodium nitroprusside (SNP) induced lipid peroxidation in human platelets and erythrocyte membranes: An in vitro evaluation
    • Posser T, Moretto MB, Dafre AL, Farina M, Rocha JBT, Nogueira CW, Zeni G, Ferreira JS, Leal RB, Franco JL. 2006. Antioxidant effect of diphenyl diselenide against sodium nitroprusside (SNP) induced lipid peroxidation in human platelets and erythrocyte membranes: An in vitro evaluation. Chem. Biol. Interact. 164: 126–135.
    • (2006) Chem. Biol. Interact. , vol.164 , pp. 126-135
    • Posser, T.1    Moretto, M.B.2    Dafre, A.L.3    Farina, M.4    Rocha, J.B.T.5    Nogueira, C.W.6    Zeni, G.7    Ferreira, J.S.8    Leal, R.B.9    Franco, J.L.10
  • 57
    • 84984568135 scopus 로고    scopus 로고
    • Diphenyl diselenide induces apoptotic cell death and modulates ERK1/2 phosphorylation in human neuroblastoma SH-SY5Y cells
    • Posser T, de Paula MT, Franco JL, Leal RB, Rocha JBT. 2011. Diphenyl diselenide induces apoptotic cell death and modulates ERK1/2 phosphorylation in human neuroblastoma SH-SY5Y cells. Arch. Toxicol. 85: 645–651.
    • (2011) Arch. Toxicol. , vol.85 , pp. 645-651
    • Posser, T.1    de Paula, M.T.2    Franco, J.L.3    Leal, R.B.4    Rocha, J.B.T.5
  • 58
    • 84909613176 scopus 로고    scopus 로고
    • Potential role of selenoenzymes and antioxidant metabolism in relation to autism etiology and pathology
    • Raymond LJ, Deth RC, Ralston NVC. 2014. Potential role of selenoenzymes and antioxidant metabolism in relation to autism etiology and pathology. Autism Res Treat. 2014: 1–15.
    • (2014) Autism Res Treat. , vol.2014 , pp. 1-15
    • Raymond, L.J.1    Deth, R.C.2    Ralston, N.V.C.3
  • 59
    • 84984550577 scopus 로고    scopus 로고
    • Guanosine and synthetic organoselenium compounds modulate methylmercury-induced oxidative stress in rat brain cortical slices: involvement of oxidative stress and glutamatergic system
    • Roos DH, Puntel RL, Santos MM, Souza DO, Farina M, Nogueira CW, Aschner M, Burger ME, Barbosa NB, Rocha JB. 2009. Guanosine and synthetic organoselenium compounds modulate methylmercury-induced oxidative stress in rat brain cortical slices: involvement of oxidative stress and glutamatergic system. Toxicol. in Vitro 23(2): 302–307.
    • (2009) Toxicol. in Vitro , vol.23 , Issue.2 , pp. 302-307
    • Roos, D.H.1    Puntel, R.L.2    Santos, M.M.3    Souza, D.O.4    Farina, M.5    Nogueira, C.W.6    Aschner, M.7    Burger, M.E.8    Barbosa, N.B.9    Rocha, J.B.10
  • 60
    • 17744418644 scopus 로고    scopus 로고
    • Efficacy of urine determination of early renal damage markers for nephrotoxicity monitoring during occupational exposure to mercury vapours
    • Rutowski J, Moszczynski P, Bem S, Szewczyk A. 1998. Efficacy of urine determination of early renal damage markers for nephrotoxicity monitoring during occupational exposure to mercury vapours. Med. Pr. 49: 129–135.
    • (1998) Med. Pr. , vol.49 , pp. 129-135
    • Rutowski, J.1    Moszczynski, P.2    Bem, S.3    Szewczyk, A.4
  • 61
    • 84971635984 scopus 로고    scopus 로고
    • Potentiation of methylmercury-induced death in rat cerebellar granular neurons occurs by further decrease of total intracellular GSH with BDNF via TrkB in vitro
    • Sakaue M, Maki T, Kaneko T, Hemmi N, Sekiguchi H, Horio T, Kadowaki E, Ozawa A, Yamamoto M. 2016. Potentiation of methylmercury-induced death in rat cerebellar granular neurons occurs by further decrease of total intracellular GSH with BDNF via TrkB in vitro. Biol. Pharm. Bull. 39(6): 1047–1054.
    • (2016) Biol. Pharm. Bull. , vol.39 , Issue.6 , pp. 1047-1054
    • Sakaue, M.1    Maki, T.2    Kaneko, T.3    Hemmi, N.4    Sekiguchi, H.5    Horio, T.6    Kadowaki, E.7    Ozawa, A.8    Yamamoto, M.9
  • 63
    • 0032603820 scopus 로고    scopus 로고
    • Methylmercury-induced generation of free radicals: biological implications
    • Sarafian TA. 1999. Methylmercury-induced generation of free radicals: biological implications. Met. Ions Biol. Syst. 36: 415–444.
    • (1999) Met. Ions Biol. Syst. , vol.36 , pp. 415-444
    • Sarafian, T.A.1
  • 64
    • 77649256856 scopus 로고    scopus 로고
    • Structure-function relations, physiological roles, and evolution of mammalian ER-resident selenoproteins
    • Shchedrina VA, Zhang Y, Labunskyy VM, Hatfield DL, Gladyshev VN. 2010. Structure-function relations, physiological roles, and evolution of mammalian ER-resident selenoproteins. Antioxid. Redox Sign. 12(7): 839–849.
    • (2010) Antioxid. Redox Sign. , vol.12 , Issue.7 , pp. 839-849
    • Shchedrina, V.A.1    Zhang, Y.2    Labunskyy, V.M.3    Hatfield, D.L.4    Gladyshev, V.N.5
  • 65
    • 33644956003 scopus 로고    scopus 로고
    • High susceptibility of neural stem cells to methylmercury toxicity: effects on cell survival and neuronal differentiation
    • Tamm C, Duckworth J, Hermanson O, Ceccatelli S. 2006. High susceptibility of neural stem cells to methylmercury toxicity: effects on cell survival and neuronal differentiation. J. Neurochem. 97: 69–78.
    • (2006) J. Neurochem. , vol.97 , pp. 69-78
    • Tamm, C.1    Duckworth, J.2    Hermanson, O.3    Ceccatelli, S.4
  • 66
    • 84960129247 scopus 로고    scopus 로고
    • In vitro evaluation of inorganic and methyl mercury mediated cytotoxic effect on neural cells derived from different animal species
    • Tong J, Wang Y, Lu Y. 2016. In vitro evaluation of inorganic and methyl mercury mediated cytotoxic effect on neural cells derived from different animal species. J. Environ. Sci. 41: 138–145.
    • (2016) J. Environ. Sci. , vol.41 , pp. 138-145
    • Tong, J.1    Wang, Y.2    Lu, Y.3
  • 68
    • 72649102227 scopus 로고    scopus 로고
    • Catalytic mechanisms and specificities of glutathione peroxidases: variations of a basic scheme
    • Toppo S, Flohé L, Ursini F, Vanin S, Maiorino M. 2009. Catalytic mechanisms and specificities of glutathione peroxidases: variations of a basic scheme. Biochim. Biophys. Acta 1790: 1486–1500.
    • (2009) Biochim. Biophys. Acta , vol.1790 , pp. 1486-1500
    • Toppo, S.1    Flohé, L.2    Ursini, F.3    Vanin, S.4    Maiorino, M.5
  • 70
    • 84984563931 scopus 로고    scopus 로고
    • In vivo and in vitro inhibition of mice thioredoxin reductase by methylmercury
    • Wagner C, Sudati JH, Nogueira CW, Rocha JB. 2010. In vivo and in vitro inhibition of mice thioredoxin reductase by methylmercury. Biometals 23(6): 1171–1177.
    • (2010) Biometals , vol.23 , Issue.6 , pp. 1171-1177
    • Wagner, C.1    Sudati, J.H.2    Nogueira, C.W.3    Rocha, J.B.4
  • 71
    • 33845182896 scopus 로고
    • Development of synthetic compounds with glutathione peroxidase activity
    • Wilson SR, Zucker PA, Huang RRC, Spector A. 1989. Development of synthetic compounds with glutathione peroxidase activity. J. Am. Chem. Soc. 111: 5936–5939.
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 5936-5939
    • Wilson, S.R.1    Zucker, P.A.2    Huang, R.R.C.3    Spector, A.4
  • 74
    • 84875134553 scopus 로고    scopus 로고
    • Organoselenium compounds modulate extracellular redox by induction of extracellular cysteine and cell surface thioredoxin reductase
    • Zhang G, Nitteranon V, Guo S, Qiu P, Wu X, Li F, Xiao H, Hu Q, Parkin KL. 2013. Organoselenium compounds modulate extracellular redox by induction of extracellular cysteine and cell surface thioredoxin reductase. Chem. Res. Toxicol. 26: 456–464.
    • (2013) Chem. Res. Toxicol. , vol.26 , pp. 456-464
    • Zhang, G.1    Nitteranon, V.2    Guo, S.3    Qiu, P.4    Wu, X.5    Li, F.6    Xiao, H.7    Hu, Q.8    Parkin, K.L.9
  • 75
    • 0037131424 scopus 로고    scopus 로고
    • A novel antioxidant mechanism of ebselen involving ebselen diselenide, a substrate of mammalian thioredoxin and thioredoxin reductase
    • Zhao R, Holmgren A. 2002. A novel antioxidant mechanism of ebselen involving ebselen diselenide, a substrate of mammalian thioredoxin and thioredoxin reductase. J. Biol. Chem. 277(42): 39456–39462.
    • (2002) J. Biol. Chem. , vol.277 , Issue.42 , pp. 39456-39462
    • Zhao, R.1    Holmgren, A.2
  • 76
    • 0037172997 scopus 로고    scopus 로고
    • Ebselen: a substrate for human thioredoxin reductase strongly stimulating its hydroperoxide reductase activity and a superfast thioredoxin oxidant
    • Zhao R, Masayasu H, Holmgren A. 2002. Ebselen: a substrate for human thioredoxin reductase strongly stimulating its hydroperoxide reductase activity and a superfast thioredoxin oxidant. Proc. Natl. Acad. Sci. U. S. A. 99(13): 8579–8584.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , Issue.13 , pp. 8579-8584
    • Zhao, R.1    Masayasu, H.2    Holmgren, A.3
  • 77
    • 0034705133 scopus 로고    scopus 로고
    • Structure and mechanism of mammalian thioredoxin reductase: the active site is a redox-active selenothiol/selenenylsulfide Formed from the conserved cysteine-selenocysteine sequence
    • Zhong L, Arnér ESJ, Holmgren A. 2000. Structure and mechanism of mammalian thioredoxin reductase: the active site is a redox-active selenothiol/selenenylsulfide Formed from the conserved cysteine-selenocysteine sequence. Proc. Natl. Acad. Sci. U. S. A. 97: 5854–5859.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 5854-5859
    • Zhong, L.1    Arnér, E.S.J.2    Holmgren, A.3
  • 78
    • 84879594818 scopus 로고    scopus 로고
    • Comparative study on methyl- and ethylmercury-induced toxicity in C6 glioma cells and the potential role of LAT-1 in mediating mercurial-thiol complexes uptake
    • Zimmermann LT, Santos DB, Naime AA, Leal RB, Dórea JG, Barbosa F, Aschner M, Rocha JBT, Farina M. 2013. Comparative study on methyl- and ethylmercury-induced toxicity in C6 glioma cells and the potential role of LAT-1 in mediating mercurial-thiol complexes uptake. Neurotoxicology 38: 1–8.
    • (2013) Neurotoxicology , vol.38 , pp. 1-8
    • Zimmermann, L.T.1    Santos, D.B.2    Naime, A.A.3    Leal, R.B.4    Dórea, J.G.5    Barbosa, F.6    Aschner, M.7    Rocha, J.B.T.8    Farina, M.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.