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  • Source: Free Radical Biology and Medicine. Unidade: IQ

    Subjects: RADICAIS LIVRES, ESTRESSE OXIDATIVO, MITOCÔNDRIAS

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      TAHARA, Erich Birelli e NAVARETE, Felipe Donizeti Teston e KOWALTOWSKI, Alicia Juliana. Tissue-, substrate-, and site-specific characteristics of mitochondrial reactive oxygen species generation. Free Radical Biology and Medicine, v. 46, n. 9, p. 1283-1297, 2009Tradução . . Disponível em: https://doi.org/10.1016/j.freeradbiomed.2009.02.008. Acesso em: 02 nov. 2024.
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      Tahara, E. B., Navarete, F. D. T., & Kowaltowski, A. J. (2009). Tissue-, substrate-, and site-specific characteristics of mitochondrial reactive oxygen species generation. Free Radical Biology and Medicine, 46( 9), 1283-1297. doi:10.1016/j.freeradbiomed.2009.02.008
    • NLM

      Tahara EB, Navarete FDT, Kowaltowski AJ. Tissue-, substrate-, and site-specific characteristics of mitochondrial reactive oxygen species generation [Internet]. Free Radical Biology and Medicine. 2009 ; 46( 9): 1283-1297.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2009.02.008
    • Vancouver

      Tahara EB, Navarete FDT, Kowaltowski AJ. Tissue-, substrate-, and site-specific characteristics of mitochondrial reactive oxygen species generation [Internet]. Free Radical Biology and Medicine. 2009 ; 46( 9): 1283-1297.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2009.02.008
  • Source: Free Radical Biology & Medicine. Unidade: IQ

    Subjects: ESTRESSE OXIDATIVO, MITOCÔNDRIAS, RADICAIS LIVRES

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      KOWALTOWSKI, Alicia Juliana et al. Mitochondria and reactive oxygen species. Free Radical Biology & Medicine, v. 47, n. 4, p. 333-343, 2009Tradução . . Disponível em: https://doi.org/10.1016/j.freeradbiomed.2009.05.004. Acesso em: 02 nov. 2024.
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      Kowaltowski, A. J., Souza-Pinto, N. C. de, Castilho, R. F., & Vercesi, A. E. (2009). Mitochondria and reactive oxygen species. Free Radical Biology & Medicine, 47( 4), 333-343. doi:10.1016/j.freeradbiomed.2009.05.004
    • NLM

      Kowaltowski AJ, Souza-Pinto NC de, Castilho RF, Vercesi AE. Mitochondria and reactive oxygen species [Internet]. Free Radical Biology & Medicine. 2009 ; 47( 4): 333-343.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2009.05.004
    • Vancouver

      Kowaltowski AJ, Souza-Pinto NC de, Castilho RF, Vercesi AE. Mitochondria and reactive oxygen species [Internet]. Free Radical Biology & Medicine. 2009 ; 47( 4): 333-343.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2009.05.004
  • Source: Free Radical Biology and Medicine. Unidade: IQ

    Subjects: ÓXIDO NÍTRICO, MACRÓFAGOS, RADICAIS LIVRES

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      LINARES, Edlaine e GIORGIO, Selma e AUGUSTO, Ohara. Inhibition of in vivo leishmanicidal mechanisms by tempol: Nitric oxide down-regulation and oxidant scavenging. Free Radical Biology and Medicine, v. 44, n. 8, p. 1668-1676, 2008Tradução . . Disponível em: https://doi.org/10.1016/j.freeradbiomed.2008.01.027. Acesso em: 02 nov. 2024.
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      Linares, E., Giorgio, S., & Augusto, O. (2008). Inhibition of in vivo leishmanicidal mechanisms by tempol: Nitric oxide down-regulation and oxidant scavenging. Free Radical Biology and Medicine, 44( 8), 1668-1676. doi:10.1016/j.freeradbiomed.2008.01.027
    • NLM

      Linares E, Giorgio S, Augusto O. Inhibition of in vivo leishmanicidal mechanisms by tempol: Nitric oxide down-regulation and oxidant scavenging [Internet]. Free Radical Biology and Medicine. 2008 ;44( 8): 1668-1676.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2008.01.027
    • Vancouver

      Linares E, Giorgio S, Augusto O. Inhibition of in vivo leishmanicidal mechanisms by tempol: Nitric oxide down-regulation and oxidant scavenging [Internet]. Free Radical Biology and Medicine. 2008 ;44( 8): 1668-1676.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2008.01.027
  • Source: Toxicology and Applied Pharmacology. Unidade: IQ

    Subjects: ÓXIDO NÍTRICO, EXPRESSÃO GÊNICA, TRANSDUÇÃO DE SINAL CELULAR

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      ARAI, Roberto J. et al. Thioredoxin-1 promotes survival in cells exposed to S-nitrosoglutathione: correlation with reduction of intracellular levels of nitrosothiols and up-regulation of the ERK1/2 MAP Kinases. Toxicology and Applied Pharmacology, v. 233, n. 2, p. 227-237, 2008Tradução . . Disponível em: https://doi.org/10.1016/j.taap.2008.07.023. Acesso em: 02 nov. 2024.
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      Arai, R. J., Ogata, F. T., Batista, W. L., Masutami, H., Yodoi, J., Debbas, V., et al. (2008). Thioredoxin-1 promotes survival in cells exposed to S-nitrosoglutathione: correlation with reduction of intracellular levels of nitrosothiols and up-regulation of the ERK1/2 MAP Kinases. Toxicology and Applied Pharmacology, 233( 2), 227-237. doi:10.1016/j.taap.2008.07.023
    • NLM

      Arai RJ, Ogata FT, Batista WL, Masutami H, Yodoi J, Debbas V, Augusto O, Stern A, Monteiro HP. Thioredoxin-1 promotes survival in cells exposed to S-nitrosoglutathione: correlation with reduction of intracellular levels of nitrosothiols and up-regulation of the ERK1/2 MAP Kinases [Internet]. Toxicology and Applied Pharmacology. 2008 ; 233( 2): 227-237.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.taap.2008.07.023
    • Vancouver

      Arai RJ, Ogata FT, Batista WL, Masutami H, Yodoi J, Debbas V, Augusto O, Stern A, Monteiro HP. Thioredoxin-1 promotes survival in cells exposed to S-nitrosoglutathione: correlation with reduction of intracellular levels of nitrosothiols and up-regulation of the ERK1/2 MAP Kinases [Internet]. Toxicology and Applied Pharmacology. 2008 ; 233( 2): 227-237.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.taap.2008.07.023
  • Source: Food and Chemical Toxicology. Unidade: IQ

    Subjects: CHLORELLA, ANTIOXIDANTES, BIOQUÍMICA

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      QUEIROZ, Mary Luci de Souza et al. Chlorella vulgaris up-modulation of myelossupression induced by lead: the role of stromal cells. Food and Chemical Toxicology, v. 46, n. 9, p. 3147-3154, 2008Tradução . . Disponível em: https://doi.org/10.1016/j.fct.2008.07.005. Acesso em: 02 nov. 2024.
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      Queiroz, M. L. de S., Torello, C. O., Perhs, S. M. C., Rocha, M. C., Bechara, E. J. H., Morgano, M. A., et al. (2008). Chlorella vulgaris up-modulation of myelossupression induced by lead: the role of stromal cells. Food and Chemical Toxicology, 46( 9), 3147-3154. doi:10.1016/j.fct.2008.07.005
    • NLM

      Queiroz ML de S, Torello CO, Perhs SMC, Rocha MC, Bechara EJH, Morgano MA, Valadares MC, Rodrigues APO, Ramos AL, Soares CO. Chlorella vulgaris up-modulation of myelossupression induced by lead: the role of stromal cells [Internet]. Food and Chemical Toxicology. 2008 ; 46( 9): 3147-3154.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.fct.2008.07.005
    • Vancouver

      Queiroz ML de S, Torello CO, Perhs SMC, Rocha MC, Bechara EJH, Morgano MA, Valadares MC, Rodrigues APO, Ramos AL, Soares CO. Chlorella vulgaris up-modulation of myelossupression induced by lead: the role of stromal cells [Internet]. Food and Chemical Toxicology. 2008 ; 46( 9): 3147-3154.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.fct.2008.07.005
  • Source: Free Radical Biology and Medicine. Unidade: IQ

    Subjects: MITOCÔNDRIAS, BIOQUÍMICA, PEROXIDASE

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      FACUNDO, Heberty Di Tarso Fernandes e PAULA, Juliana Gabriela de e KOWALTOWSKI, Alicia Juliana. Mitochondrial ATP-sensitive 'K POT. +' channels are redox-sensitive pathways that control reactive oxygen species production. Free Radical Biology and Medicine, v. 42, n. 7, p. 1039-1048, 2007Tradução . . Disponível em: https://doi.org/10.1016/j.freeradbiomed.2007.01.001. Acesso em: 02 nov. 2024.
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      Facundo, H. D. T. F., Paula, J. G. de, & Kowaltowski, A. J. (2007). Mitochondrial ATP-sensitive 'K POT. +' channels are redox-sensitive pathways that control reactive oxygen species production. Free Radical Biology and Medicine, 42( 7), 1039-1048. doi:10.1016/j.freeradbiomed.2007.01.001
    • NLM

      Facundo HDTF, Paula JG de, Kowaltowski AJ. Mitochondrial ATP-sensitive 'K POT. +' channels are redox-sensitive pathways that control reactive oxygen species production [Internet]. Free Radical Biology and Medicine. 2007 ; 42( 7): 1039-1048.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2007.01.001
    • Vancouver

      Facundo HDTF, Paula JG de, Kowaltowski AJ. Mitochondrial ATP-sensitive 'K POT. +' channels are redox-sensitive pathways that control reactive oxygen species production [Internet]. Free Radical Biology and Medicine. 2007 ; 42( 7): 1039-1048.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2007.01.001
  • Source: Free Radical Biology and Medicine. Unidade: IQ

    Subjects: RADICAIS LIVRES, BIOQUÍMICA

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      FACUNDO, Heberty Di Tarso Fernandes et al. Ischemic preconditioning requires increases in reactive oxygen release independent of mitochondrial 'K POT.+' channel activity. Free Radical Biology and Medicine, v. 40, n. 3, p. 469-479, 2006Tradução . . Disponível em: https://doi.org/10.1016/j.freeradbiomed.2005.08.041. Acesso em: 02 nov. 2024.
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      Facundo, H. D. T. F., Carreira, R. S., Paula, J. G. de, Santos, C. X. da C. dos, Ferranti, R., Laurindo, F. R. M., & Kowaltowski, A. J. (2006). Ischemic preconditioning requires increases in reactive oxygen release independent of mitochondrial 'K POT.+' channel activity. Free Radical Biology and Medicine, 40( 3), 469-479. doi:10.1016/j.freeradbiomed.2005.08.041
    • NLM

      Facundo HDTF, Carreira RS, Paula JG de, Santos CX da C dos, Ferranti R, Laurindo FRM, Kowaltowski AJ. Ischemic preconditioning requires increases in reactive oxygen release independent of mitochondrial 'K POT.+' channel activity [Internet]. Free Radical Biology and Medicine. 2006 ; 40( 3): 469-479.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2005.08.041
    • Vancouver

      Facundo HDTF, Carreira RS, Paula JG de, Santos CX da C dos, Ferranti R, Laurindo FRM, Kowaltowski AJ. Ischemic preconditioning requires increases in reactive oxygen release independent of mitochondrial 'K POT.+' channel activity [Internet]. Free Radical Biology and Medicine. 2006 ; 40( 3): 469-479.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2005.08.041
  • Source: Free Radical Biology and Medicine. Unidade: IQ

    Subjects: DANO AO DNA, ESPECTROMETRIA DE MASSAS, RADICAIS LIVRES

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      MARTINEZ, Glaucia Regina et al. Identification of the main oxidation products of 8-methoxy-2'-deoxyguanosine by singlet molecular oxygen. Free Radical Biology and Medicine, v. 38, n. 11, p. 1491-1500, 2005Tradução . . Disponível em: https://doi.org/10.1016/j.freeradbiomed.2005.02.008. Acesso em: 02 nov. 2024.
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      Martinez, G. R., Gasparutto, D., Ravanat, J. -L., Cadet, J., Medeiros, M. H. G. de, & Di Mascio, P. (2005). Identification of the main oxidation products of 8-methoxy-2'-deoxyguanosine by singlet molecular oxygen. Free Radical Biology and Medicine, 38( 11), 1491-1500. doi:10.1016/j.freeradbiomed.2005.02.008
    • NLM

      Martinez GR, Gasparutto D, Ravanat J-L, Cadet J, Medeiros MHG de, Di Mascio P. Identification of the main oxidation products of 8-methoxy-2'-deoxyguanosine by singlet molecular oxygen [Internet]. Free Radical Biology and Medicine. 2005 ; 38( 11): 1491-1500.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2005.02.008
    • Vancouver

      Martinez GR, Gasparutto D, Ravanat J-L, Cadet J, Medeiros MHG de, Di Mascio P. Identification of the main oxidation products of 8-methoxy-2'-deoxyguanosine by singlet molecular oxygen [Internet]. Free Radical Biology and Medicine. 2005 ; 38( 11): 1491-1500.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2005.02.008
  • Source: Free Radical Biology and Medicine. Unidades: IQ, FM, FCF

    Subjects: ÓXIDO NÍTRICO, VASODILATAÇÃO, RESSONÂNCIA PARAMAGNÉTICA DE SPIN

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      LIMA, Emersom Silva et al. Nitrated lipids decompose to nitric oxide and lipid radicals and cause vasorelaxation. Free Radical Biology and Medicine, v. 39, n. 4, p. 532-539, 2005Tradução . . Disponível em: https://doi.org/10.1016/j.freeradbiomed.2005.04.005. Acesso em: 02 nov. 2024.
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      Lima, E. S., Bonini, M. G., Augusto, O., Barbeiro, H. V., Souza, H. P. de, & Abdalla, D. S. P. (2005). Nitrated lipids decompose to nitric oxide and lipid radicals and cause vasorelaxation. Free Radical Biology and Medicine, 39( 4), 532-539. doi:10.1016/j.freeradbiomed.2005.04.005
    • NLM

      Lima ES, Bonini MG, Augusto O, Barbeiro HV, Souza HP de, Abdalla DSP. Nitrated lipids decompose to nitric oxide and lipid radicals and cause vasorelaxation [Internet]. Free Radical Biology and Medicine. 2005 ; 39( 4): 532-539.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2005.04.005
    • Vancouver

      Lima ES, Bonini MG, Augusto O, Barbeiro HV, Souza HP de, Abdalla DSP. Nitrated lipids decompose to nitric oxide and lipid radicals and cause vasorelaxation [Internet]. Free Radical Biology and Medicine. 2005 ; 39( 4): 532-539.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2005.04.005
  • Source: Free Radical Biology and Medicine. Unidade: IQ

    Subjects: ÓXIDO NÍTRICO, RADICAIS LIVRES

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      FERNANDES, Denise C. et al. Tempol diverts peroxynitrite/carbon dioxide reactivity toward albumin and cells from protein-tyrosine nitration to protein-cysteine nitrosation. Free Radical Biology and Medicine, v. 38, n. 2, p. 189-200, 2005Tradução . . Disponível em: https://doi.org/10.1016/j.freeradbiomed.2004.09.027. Acesso em: 02 nov. 2024.
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      Fernandes, D. C., Medinas, D. B., Alves, M. J. M., & Augusto, O. (2005). Tempol diverts peroxynitrite/carbon dioxide reactivity toward albumin and cells from protein-tyrosine nitration to protein-cysteine nitrosation. Free Radical Biology and Medicine, 38( 2), 189-200. doi:10.1016/j.freeradbiomed.2004.09.027
    • NLM

      Fernandes DC, Medinas DB, Alves MJM, Augusto O. Tempol diverts peroxynitrite/carbon dioxide reactivity toward albumin and cells from protein-tyrosine nitration to protein-cysteine nitrosation [Internet]. Free Radical Biology and Medicine. 2005 ; 38( 2): 189-200.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2004.09.027
    • Vancouver

      Fernandes DC, Medinas DB, Alves MJM, Augusto O. Tempol diverts peroxynitrite/carbon dioxide reactivity toward albumin and cells from protein-tyrosine nitration to protein-cysteine nitrosation [Internet]. Free Radical Biology and Medicine. 2005 ; 38( 2): 189-200.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2004.09.027
  • Source: Free Radical Biology and Medicine. Unidade: IQ

    Subjects: RADICAIS LIVRES, APOPTOSE, ANTIOXIDANTES, NECROSE, BIOQUÍMICA

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      KOWALTOWSKI, Alicia Juliana e FENTON, Robert G. e FISKUM, Gary. Bcl-2 family proteins regulate mitochondrial reactive oxygen production and protect against oxidative stress. Free Radical Biology and Medicine, v. 37, n. 11, p. 1845-1853, 2004Tradução . . Disponível em: https://doi.org/10.1016/j.freeradbiomed.2004.09.005. Acesso em: 02 nov. 2024.
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      Kowaltowski, A. J., Fenton, R. G., & Fiskum, G. (2004). Bcl-2 family proteins regulate mitochondrial reactive oxygen production and protect against oxidative stress. Free Radical Biology and Medicine, 37( 11), 1845-1853. doi:10.1016/j.freeradbiomed.2004.09.005
    • NLM

      Kowaltowski AJ, Fenton RG, Fiskum G. Bcl-2 family proteins regulate mitochondrial reactive oxygen production and protect against oxidative stress [Internet]. Free Radical Biology and Medicine. 2004 ; 37( 11): 1845-1853.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2004.09.005
    • Vancouver

      Kowaltowski AJ, Fenton RG, Fiskum G. Bcl-2 family proteins regulate mitochondrial reactive oxygen production and protect against oxidative stress [Internet]. Free Radical Biology and Medicine. 2004 ; 37( 11): 1845-1853.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2004.09.005
  • Source: Free Radical Biology and Medicine. Unidade: IQ

    Subjects: BIOQUÍMICA, ÓXIDO NÍTRICO, RADICAIS LIVRES

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      AUGUSTO, Ohara e BONINI, Marcelo Gialluisi e TRINDADE, Daniel F. Spin trapping of glutathiyl and protein radicals produced from nitric oxide-derived oxidants. Free Radical Biology and Medicine, v. 36, n. 10, p. 1224-1232, 2004Tradução . . Disponível em: https://doi.org/10.1016/j.freeradbiomed.2004.02.076. Acesso em: 02 nov. 2024.
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      Augusto, O., Bonini, M. G., & Trindade, D. F. (2004). Spin trapping of glutathiyl and protein radicals produced from nitric oxide-derived oxidants. Free Radical Biology and Medicine, 36( 10), 1224-1232. doi:10.1016/j.freeradbiomed.2004.02.076
    • NLM

      Augusto O, Bonini MG, Trindade DF. Spin trapping of glutathiyl and protein radicals produced from nitric oxide-derived oxidants [Internet]. Free Radical Biology and Medicine. 2004 ; 36( 10): 1224-1232.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2004.02.076
    • Vancouver

      Augusto O, Bonini MG, Trindade DF. Spin trapping of glutathiyl and protein radicals produced from nitric oxide-derived oxidants [Internet]. Free Radical Biology and Medicine. 2004 ; 36( 10): 1224-1232.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2004.02.076
  • Source: Free Radical Biology and Medicine. Unidades: IQ, IFSC

    Subjects: RADICAIS LIVRES, ESPECTROMETRIA DE MASSAS, RESSONÂNCIA PARAMAGNÉTICA DE SPIN, BIOQUÍMICA

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      RINALDI, Tatiana Alvarez et al. Protonation of two adjacent tyrosine residues influences the reduction of cytochrome 'c' by diphenylacetaldehyde: a possible mechanism to select the reducer agent of heme iron. Free Radical Biology and Medicine, v. 36, n. 6, p. 802-810, 2004Tradução . . Disponível em: https://doi.org/10.1016/j.freeradbiomed.2003.12.002. Acesso em: 02 nov. 2024.
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      Rinaldi, T. A., Tersariol, I. L. dos S., Dyszy, F. H., Prado, F. M., Nascimento, O. R., Di Mascio, P., & Nantes, I. L. (2004). Protonation of two adjacent tyrosine residues influences the reduction of cytochrome 'c' by diphenylacetaldehyde: a possible mechanism to select the reducer agent of heme iron. Free Radical Biology and Medicine, 36( 6), 802-810. doi:10.1016/j.freeradbiomed.2003.12.002
    • NLM

      Rinaldi TA, Tersariol IL dos S, Dyszy FH, Prado FM, Nascimento OR, Di Mascio P, Nantes IL. Protonation of two adjacent tyrosine residues influences the reduction of cytochrome 'c' by diphenylacetaldehyde: a possible mechanism to select the reducer agent of heme iron [Internet]. Free Radical Biology and Medicine. 2004 ; 36( 6): 802-810.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2003.12.002
    • Vancouver

      Rinaldi TA, Tersariol IL dos S, Dyszy FH, Prado FM, Nascimento OR, Di Mascio P, Nantes IL. Protonation of two adjacent tyrosine residues influences the reduction of cytochrome 'c' by diphenylacetaldehyde: a possible mechanism to select the reducer agent of heme iron [Internet]. Free Radical Biology and Medicine. 2004 ; 36( 6): 802-810.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2003.12.002
  • Source: Free Radical Biology and Medicine. Unidade: IQ

    Subjects: RADICAIS LIVRES, BIOQUÍMICA, RESSONÂNCIA PARAMAGNÉTICA DE SPIN

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      LINARES, Edlaine et al. EPR studies of in vivo radical production by lipopolysaccharide: potential role of iron mobilized from iron-nitrosyl complexes. Free Radical Biology and Medicine, v. 34, n. 6, p. 766-773, 2003Tradução . . Disponível em: https://doi.org/10.1016/s0891-5849(02)01424-7. Acesso em: 02 nov. 2024.
    • APA

      Linares, E., Nakao, L. S., Augusto, O., & Kadiiska, M. B. (2003). EPR studies of in vivo radical production by lipopolysaccharide: potential role of iron mobilized from iron-nitrosyl complexes. Free Radical Biology and Medicine, 34( 6), 766-773. doi:10.1016/s0891-5849(02)01424-7
    • NLM

      Linares E, Nakao LS, Augusto O, Kadiiska MB. EPR studies of in vivo radical production by lipopolysaccharide: potential role of iron mobilized from iron-nitrosyl complexes [Internet]. Free Radical Biology and Medicine. 2003 ; 34( 6): 766-773.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/s0891-5849(02)01424-7
    • Vancouver

      Linares E, Nakao LS, Augusto O, Kadiiska MB. EPR studies of in vivo radical production by lipopolysaccharide: potential role of iron mobilized from iron-nitrosyl complexes [Internet]. Free Radical Biology and Medicine. 2003 ; 34( 6): 766-773.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/s0891-5849(02)01424-7
  • Source: Free Radical Biology and Medicine. Unidade: IQ

    Subjects: BIOQUÍMICA, COMPOSTOS INORGÂNICOS, ÓXIDO NÍTRICO, RADICAIS LIVRES, OXIDAÇÃO, BIOLOGIA MOLECULAR

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      AUGUSTO, Ohara et al. Nitrogen dioxide and carbonate radical anion: Two emerging radicals in biology. Free Radical Biology and Medicine, v. 32, n. 9, p. 841-859, 2002Tradução . . Disponível em: https://doi.org/10.1016/s0891-5849(02)00786-4. Acesso em: 02 nov. 2024.
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      Augusto, O., Bonini, M. G., Amanso, A. M., Linares, E., Santos, C. X. C., & Menezes, S. L. de. (2002). Nitrogen dioxide and carbonate radical anion: Two emerging radicals in biology. Free Radical Biology and Medicine, 32( 9), 841-859. doi:10.1016/s0891-5849(02)00786-4
    • NLM

      Augusto O, Bonini MG, Amanso AM, Linares E, Santos CXC, Menezes SL de. Nitrogen dioxide and carbonate radical anion: Two emerging radicals in biology [Internet]. Free Radical Biology and Medicine. 2002 ; 32( 9): 841-859.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/s0891-5849(02)00786-4
    • Vancouver

      Augusto O, Bonini MG, Amanso AM, Linares E, Santos CXC, Menezes SL de. Nitrogen dioxide and carbonate radical anion: Two emerging radicals in biology [Internet]. Free Radical Biology and Medicine. 2002 ; 32( 9): 841-859.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/s0891-5849(02)00786-4
  • Source: Journal of Protein Chemistry. Unidade: IQ

    Subjects: BIOQUÍMICA, TOXINAS, SURFACTANTES, ALBUMINAS

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      LANIO, Maria E. et al. Effect of a zwitterionic surfactant (HPS) on the conformation and hemolytic activity of St I and St II, two isotoxins purified from Stichodactyla helianthus. Journal of Protein Chemistry, v. 21, n. 6, p. 401-405, 2002Tradução . . Acesso em: 02 nov. 2024.
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      Lanio, M. E., Alvarez, C., Martinez, F. D., Casallanovo, F., Schreier, S., Campos, A. M., et al. (2002). Effect of a zwitterionic surfactant (HPS) on the conformation and hemolytic activity of St I and St II, two isotoxins purified from Stichodactyla helianthus. Journal of Protein Chemistry, 21( 6), 401-405.
    • NLM

      Lanio ME, Alvarez C, Martinez FD, Casallanovo F, Schreier S, Campos AM, Abuin E, Lissi E. Effect of a zwitterionic surfactant (HPS) on the conformation and hemolytic activity of St I and St II, two isotoxins purified from Stichodactyla helianthus. Journal of Protein Chemistry. 2002 ; 21( 6): 401-405.[citado 2024 nov. 02 ]
    • Vancouver

      Lanio ME, Alvarez C, Martinez FD, Casallanovo F, Schreier S, Campos AM, Abuin E, Lissi E. Effect of a zwitterionic surfactant (HPS) on the conformation and hemolytic activity of St I and St II, two isotoxins purified from Stichodactyla helianthus. Journal of Protein Chemistry. 2002 ; 21( 6): 401-405.[citado 2024 nov. 02 ]
  • Source: Free Radical Biology & Medicine. Unidade: IQ

    Subjects: BIOQUÍMICA, ÓXIDO NÍTRICO, RADICAIS LIVRES

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      LINARES, Edlaine et al. Role of peroxynitrite in macrophage microbicidal mechanisms in vivo revealed by protein nitration and hydroxylation. Free Radical Biology & Medicine, v. 30, n. 11, p. 1234-1242, 2001Tradução . . Disponível em: https://doi.org/10.1016/s0891-5849(01)00516-0. Acesso em: 02 nov. 2024.
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      Linares, E., Giorgio, S., Mortara, R. A., Santos, C. X. C., Yamada, Á. T., & Augusto, O. (2001). Role of peroxynitrite in macrophage microbicidal mechanisms in vivo revealed by protein nitration and hydroxylation. Free Radical Biology & Medicine, 30( 11), 1234-1242. doi:10.1016/s0891-5849(01)00516-0
    • NLM

      Linares E, Giorgio S, Mortara RA, Santos CXC, Yamada ÁT, Augusto O. Role of peroxynitrite in macrophage microbicidal mechanisms in vivo revealed by protein nitration and hydroxylation [Internet]. Free Radical Biology & Medicine. 2001 ; 30( 11): 1234-1242.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/s0891-5849(01)00516-0
    • Vancouver

      Linares E, Giorgio S, Mortara RA, Santos CXC, Yamada ÁT, Augusto O. Role of peroxynitrite in macrophage microbicidal mechanisms in vivo revealed by protein nitration and hydroxylation [Internet]. Free Radical Biology & Medicine. 2001 ; 30( 11): 1234-1242.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/s0891-5849(01)00516-0
  • Source: Free Radical Biology & Medicine. Unidade: IQ

    Subjects: BIOQUÍMICA, RADICAIS LIVRES

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      JANISZEWSKI, Mariano et al. Inhibition of vascular NADH/NADPH oxidase activity by thiol reagents: lack of correlation with cellular glutathione redox status. Free Radical Biology & Medicine, v. 29, n. 9, p. 889-899, 2000Tradução . . Disponível em: http://probe.usp.br/cgi-bin/sciserv.pl?collection=journals&journal=08915849&issue=v29i0009&article=889_iovnoacwcgrs&form=pdf&file=file.pdf. Acesso em: 02 nov. 2024.
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      Janiszewski, M., Pedro, M. de A., Scheffer, R. C. H., Asseldonk, J. -T. H. van, Souza, L. C., Luz, P. L. da, et al. (2000). Inhibition of vascular NADH/NADPH oxidase activity by thiol reagents: lack of correlation with cellular glutathione redox status. Free Radical Biology & Medicine, 29( 9), 889-899. Recuperado de http://probe.usp.br/cgi-bin/sciserv.pl?collection=journals&journal=08915849&issue=v29i0009&article=889_iovnoacwcgrs&form=pdf&file=file.pdf
    • NLM

      Janiszewski M, Pedro M de A, Scheffer RCH, Asseldonk J-TH van, Souza LC, Luz PL da, Augusto O, Laurindo FRM. Inhibition of vascular NADH/NADPH oxidase activity by thiol reagents: lack of correlation with cellular glutathione redox status [Internet]. Free Radical Biology & Medicine. 2000 ; 29( 9): 889-899.[citado 2024 nov. 02 ] Available from: http://probe.usp.br/cgi-bin/sciserv.pl?collection=journals&journal=08915849&issue=v29i0009&article=889_iovnoacwcgrs&form=pdf&file=file.pdf
    • Vancouver

      Janiszewski M, Pedro M de A, Scheffer RCH, Asseldonk J-TH van, Souza LC, Luz PL da, Augusto O, Laurindo FRM. Inhibition of vascular NADH/NADPH oxidase activity by thiol reagents: lack of correlation with cellular glutathione redox status [Internet]. Free Radical Biology & Medicine. 2000 ; 29( 9): 889-899.[citado 2024 nov. 02 ] Available from: http://probe.usp.br/cgi-bin/sciserv.pl?collection=journals&journal=08915849&issue=v29i0009&article=889_iovnoacwcgrs&form=pdf&file=file.pdf
  • Source: Free Radical Biology & Medicine. Unidades: FM, IQ

    Subjects: BIOQUÍMICA, SUPERÓXIDO DISMUTASE, RADICAIS LIVRES

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      SOUZA, Heraldo Possolo de et al. Vascular oxidant stress early after balloon injury: evidence for increased NAD(P)H oxidoreductase activity. Free Radical Biology & Medicine, v. 28, n. 8, p. 1232-1242, 2000Tradução . . Disponível em: https://doi.org/10.1016/s0891-5849(00)00240-9. Acesso em: 02 nov. 2024.
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      Souza, H. P. de, Souza, L. C., Anastácio, V. M., Pereira, A. C., Junqueira, M. de L., Krieger, J. E., et al. (2000). Vascular oxidant stress early after balloon injury: evidence for increased NAD(P)H oxidoreductase activity. Free Radical Biology & Medicine, 28( 8), 1232-1242. doi:10.1016/s0891-5849(00)00240-9
    • NLM

      Souza HP de, Souza LC, Anastácio VM, Pereira AC, Junqueira M de L, Krieger JE, Luz PL da, Augusto O, Laurindo FRM. Vascular oxidant stress early after balloon injury: evidence for increased NAD(P)H oxidoreductase activity [Internet]. Free Radical Biology & Medicine. 2000 ; 28( 8): 1232-1242.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/s0891-5849(00)00240-9
    • Vancouver

      Souza HP de, Souza LC, Anastácio VM, Pereira AC, Junqueira M de L, Krieger JE, Luz PL da, Augusto O, Laurindo FRM. Vascular oxidant stress early after balloon injury: evidence for increased NAD(P)H oxidoreductase activity [Internet]. Free Radical Biology & Medicine. 2000 ; 28( 8): 1232-1242.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/s0891-5849(00)00240-9
  • Source: Free Radical Biology & Medicine. Unidade: IQ

    Subjects: BIOQUÍMICA, RADICAIS LIVRES, TRYPANOSOMA CRUZI

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      LOPEZ, Jorge A et al. Evidence for a trypanothione-dependent peroxidase system in Trypanosoma cruzi. Free Radical Biology & Medicine, v. 28, n. 5, p. 767-772, 2000Tradução . . Disponível em: https://doi.org/10.1016/s0891-5849(00)00159-3. Acesso em: 02 nov. 2024.
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      Lopez, J. A., Carvalho, T. U., Souza, W. de, Flohé, L., Montemartini, M., Kalisz, H. M., et al. (2000). Evidence for a trypanothione-dependent peroxidase system in Trypanosoma cruzi. Free Radical Biology & Medicine, 28( 5), 767-772. doi:10.1016/s0891-5849(00)00159-3
    • NLM

      Lopez JA, Carvalho TU, Souza W de, Flohé L, Montemartini M, Kalisz HM, Nogoceke E, Singh M, Alves MJM, Colli W. Evidence for a trypanothione-dependent peroxidase system in Trypanosoma cruzi [Internet]. Free Radical Biology & Medicine. 2000 ; 28( 5): 767-772.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/s0891-5849(00)00159-3
    • Vancouver

      Lopez JA, Carvalho TU, Souza W de, Flohé L, Montemartini M, Kalisz HM, Nogoceke E, Singh M, Alves MJM, Colli W. Evidence for a trypanothione-dependent peroxidase system in Trypanosoma cruzi [Internet]. Free Radical Biology & Medicine. 2000 ; 28( 5): 767-772.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/s0891-5849(00)00159-3

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