Filtros : "Indexado no BIOSIS" "RADICAIS LIVRES" "IQ" Removido: "MEDEIROS, MARISA HELENA GENNARI DE" Limpar

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  • Source: Free Radical Biology & Medicine. Unidades: IQ, FM

    Subjects: INFLAMAÇÃO, ANTIOXIDANTES, RADICAIS LIVRES, ÓXIDO NÍTRICO

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      TSUHAKO, Maria Heloisa et al. Tempol ameliorates murine viral encephalomyelitis by preserving the blood–brain barrier, reducing viral load, and lessening inflammation. Free Radical Biology & Medicine, v. 48, n. 5, p. 704-712, 2010Tradução . . Disponível em: https://doi.org/10.1016/j.freeradbiomed.2009.12.013. Acesso em: 06 jun. 2024.
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      Tsuhako, M. H., Agusto, O., Linares, E., Chadi, G., Giorgio, S., & Pereira, C. A. (2010). Tempol ameliorates murine viral encephalomyelitis by preserving the blood–brain barrier, reducing viral load, and lessening inflammation. Free Radical Biology & Medicine, 48( 5), 704-712. doi:10.1016/j.freeradbiomed.2009.12.013
    • NLM

      Tsuhako MH, Agusto O, Linares E, Chadi G, Giorgio S, Pereira CA. Tempol ameliorates murine viral encephalomyelitis by preserving the blood–brain barrier, reducing viral load, and lessening inflammation [Internet]. Free Radical Biology & Medicine. 2010 ; 48( 5): 704-712.[citado 2024 jun. 06 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2009.12.013
    • Vancouver

      Tsuhako MH, Agusto O, Linares E, Chadi G, Giorgio S, Pereira CA. Tempol ameliorates murine viral encephalomyelitis by preserving the blood–brain barrier, reducing viral load, and lessening inflammation [Internet]. Free Radical Biology & Medicine. 2010 ; 48( 5): 704-712.[citado 2024 jun. 06 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2009.12.013
  • 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: 06 jun. 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
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      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 jun. 06 ] 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 jun. 06 ] 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: 06 jun. 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 jun. 06 ] 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 jun. 06 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2009.05.004
  • Source: Food Chemistry. Unidade: IQ

    Subjects: ACEROLA, RADICAIS LIVRES, FRUTAS TROPICAIS

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      OLIVEIRA, Alane Cabral de et al. Total phenolic content and free radical scavenging activities of methanolic extract powders of tropical fruit residues. Food Chemistry, v. 115, n. 2, p. 469-475, 2009Tradução . . Disponível em: https://doi.org/10.1016/j.foodchem.2008.12.045. Acesso em: 06 jun. 2024.
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      Oliveira, A. C. de, Valentim, I. B., Silva, C. A., Bechara, E. J. H., Barros, M. P. de, Mano, C. M., & Goulart, M. O. F. (2009). Total phenolic content and free radical scavenging activities of methanolic extract powders of tropical fruit residues. Food Chemistry, 115( 2), 469-475. doi:10.1016/j.foodchem.2008.12.045
    • NLM

      Oliveira AC de, Valentim IB, Silva CA, Bechara EJH, Barros MP de, Mano CM, Goulart MOF. Total phenolic content and free radical scavenging activities of methanolic extract powders of tropical fruit residues [Internet]. Food Chemistry. 2009 ; 115( 2): 469-475.[citado 2024 jun. 06 ] Available from: https://doi.org/10.1016/j.foodchem.2008.12.045
    • Vancouver

      Oliveira AC de, Valentim IB, Silva CA, Bechara EJH, Barros MP de, Mano CM, Goulart MOF. Total phenolic content and free radical scavenging activities of methanolic extract powders of tropical fruit residues [Internet]. Food Chemistry. 2009 ; 115( 2): 469-475.[citado 2024 jun. 06 ] Available from: https://doi.org/10.1016/j.foodchem.2008.12.045
  • Source: Free Radical Biology & Medicine. Unidade: IQ

    Subjects: MITOCÔNDRIAS, RADICAIS LIVRES

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      ALBERICI, Luciane Carla et al. Mitochondrial ATP-sensitive 'K POT. +' channels as redox signals to liver mitochondria in response to hypertriglyceridemia. Free Radical Biology & Medicine, v. 47, n. 10, p. 1432-1439, 2009Tradução . . Disponível em: https://doi.org/10.1016/j.freeradbiomed.2009.08.013. Acesso em: 06 jun. 2024.
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      Alberici, L. C., Oliveira, H. C. F. de, Paim, B. A., Mantello, C. C., Augusto, A. C., Zecchin, K. G., et al. (2009). Mitochondrial ATP-sensitive 'K POT. +' channels as redox signals to liver mitochondria in response to hypertriglyceridemia. Free Radical Biology & Medicine, 47( 10), 1432-1439. doi:10.1016/j.freeradbiomed.2009.08.013
    • NLM

      Alberici LC, Oliveira HCF de, Paim BA, Mantello CC, Augusto AC, Zecchin KG, Gurgueira SA, Kowaltowski AJ, Vercesi AE. Mitochondrial ATP-sensitive 'K POT. +' channels as redox signals to liver mitochondria in response to hypertriglyceridemia [Internet]. Free Radical Biology & Medicine. 2009 ; 47( 10): 1432-1439.[citado 2024 jun. 06 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2009.08.013
    • Vancouver

      Alberici LC, Oliveira HCF de, Paim BA, Mantello CC, Augusto AC, Zecchin KG, Gurgueira SA, Kowaltowski AJ, Vercesi AE. Mitochondrial ATP-sensitive 'K POT. +' channels as redox signals to liver mitochondria in response to hypertriglyceridemia [Internet]. Free Radical Biology & Medicine. 2009 ; 47( 10): 1432-1439.[citado 2024 jun. 06 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2009.08.013
  • Source: Free Radical Biology & Medicine. Unidade: IQ

    Subjects: RADICAIS LIVRES, MITOCÔNDRIAS, APOPTOSE

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      PANDURI, V. et al. Role of mitochondrial hOGG1 and aconitase in oxidant-induced lung epithelial cell apoptosis. Free Radical Biology & Medicine, v. 47, n. 6, p. 750-759, 2009Tradução . . Disponível em: https://doi.org/10.1016/j.freeradbiomed.2009.06.010. Acesso em: 06 jun. 2024.
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      Panduri, V., Liu, G., Surapureddi, S., Kondapalli, J., Soberanes, S., Souza-Pinto, N. C. de, et al. (2009). Role of mitochondrial hOGG1 and aconitase in oxidant-induced lung epithelial cell apoptosis. Free Radical Biology & Medicine, 47( 6), 750-759. doi:10.1016/j.freeradbiomed.2009.06.010
    • NLM

      Panduri V, Liu G, Surapureddi S, Kondapalli J, Soberanes S, Souza-Pinto NC de, Bohr VA, Budinger GRS, Schumacker PT, Weitzman SA, Kamp DW. Role of mitochondrial hOGG1 and aconitase in oxidant-induced lung epithelial cell apoptosis [Internet]. Free Radical Biology & Medicine. 2009 ; 47( 6): 750-759.[citado 2024 jun. 06 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2009.06.010
    • Vancouver

      Panduri V, Liu G, Surapureddi S, Kondapalli J, Soberanes S, Souza-Pinto NC de, Bohr VA, Budinger GRS, Schumacker PT, Weitzman SA, Kamp DW. Role of mitochondrial hOGG1 and aconitase in oxidant-induced lung epithelial cell apoptosis [Internet]. Free Radical Biology & Medicine. 2009 ; 47( 6): 750-759.[citado 2024 jun. 06 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2009.06.010
  • Source: Proceedings of the National Academy of Sciences of the United States of America - PNAS. Unidade: IQ

    Subjects: ÓXIDO NÍTRICO, RADICAIS LIVRES

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      VAZ, Sandra Muntz e AUGUSTO, Ohara. Inhibition of myeloperoxidase-mediated protein nitration by tempol: kinetics, mechanism, and implications. Proceedings of the National Academy of Sciences of the United States of America - PNAS, v. 105, n. 24, p. 8194-8196, 2008Tradução . . Disponível em: https://doi.org/10.1073/pnas.0708211105. Acesso em: 06 jun. 2024.
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      Vaz, S. M., & Augusto, O. (2008). Inhibition of myeloperoxidase-mediated protein nitration by tempol: kinetics, mechanism, and implications. Proceedings of the National Academy of Sciences of the United States of America - PNAS, 105( 24), 8194-8196. doi:10.1073/pnas.0708211105
    • NLM

      Vaz SM, Augusto O. Inhibition of myeloperoxidase-mediated protein nitration by tempol: kinetics, mechanism, and implications [Internet]. Proceedings of the National Academy of Sciences of the United States of America - PNAS. 2008 ;105( 24): 8194-8196.[citado 2024 jun. 06 ] Available from: https://doi.org/10.1073/pnas.0708211105
    • Vancouver

      Vaz SM, Augusto O. Inhibition of myeloperoxidase-mediated protein nitration by tempol: kinetics, mechanism, and implications [Internet]. Proceedings of the National Academy of Sciences of the United States of America - PNAS. 2008 ;105( 24): 8194-8196.[citado 2024 jun. 06 ] Available from: https://doi.org/10.1073/pnas.0708211105
  • 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: 06 jun. 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 jun. 06 ] 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 jun. 06 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2008.01.027
  • 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: 06 jun. 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 jun. 06 ] 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 jun. 06 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2005.08.041
  • 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: 06 jun. 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 jun. 06 ] 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 jun. 06 ] 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: 06 jun. 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 jun. 06 ] 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 jun. 06 ] 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: 06 jun. 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 jun. 06 ] 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 jun. 06 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2004.02.076
  • Source: Biopolymers. Unidade: IQ

    Subjects: BIOQUÍMICA, ANGIOTENSINA II, RADICAIS LIVRES, SOLUÇÕES AQUOSAS

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      SCHREIER, Shirley et al. Conformational basis for the biological activity of TOAC-labeled angiotensin II and Bradykinin: Electron paramagnetic resonance, circular dichroism, and fluorescence studies. Biopolymers, v. 74, n. 5, p. 389-402, 2004Tradução . . Disponível em: https://doi.org/10.1002/bip.20092. Acesso em: 06 jun. 2024.
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      Schreier, S., Barbosa, S. R., Casallanovo, F., Vieira, R. de F. F., Cilli, E. M., Paiva, A. C. de M., & Nakaie, C. R. (2004). Conformational basis for the biological activity of TOAC-labeled angiotensin II and Bradykinin: Electron paramagnetic resonance, circular dichroism, and fluorescence studies. Biopolymers, 74( 5), 389-402. doi:10.1002/bip.20092
    • NLM

      Schreier S, Barbosa SR, Casallanovo F, Vieira R de FF, Cilli EM, Paiva AC de M, Nakaie CR. Conformational basis for the biological activity of TOAC-labeled angiotensin II and Bradykinin: Electron paramagnetic resonance, circular dichroism, and fluorescence studies [Internet]. Biopolymers. 2004 ; 74( 5): 389-402.[citado 2024 jun. 06 ] Available from: https://doi.org/10.1002/bip.20092
    • Vancouver

      Schreier S, Barbosa SR, Casallanovo F, Vieira R de FF, Cilli EM, Paiva AC de M, Nakaie CR. Conformational basis for the biological activity of TOAC-labeled angiotensin II and Bradykinin: Electron paramagnetic resonance, circular dichroism, and fluorescence studies [Internet]. Biopolymers. 2004 ; 74( 5): 389-402.[citado 2024 jun. 06 ] Available from: https://doi.org/10.1002/bip.20092
  • 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: 06 jun. 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 jun. 06 ] 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 jun. 06 ] 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: 06 jun. 2024.
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      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 jun. 06 ] 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 jun. 06 ] Available from: https://doi.org/10.1016/s0891-5849(02)01424-7
  • Source: FEBS Letters. Unidade: IQ

    Subjects: BIOQUÍMICA, RADICAIS LIVRES, ISQUEMIA

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      FERRANTI, Renato e SILVA, Mirian Mateus da e KOWALTOWSKI, Alicia Juliana. Mitochondrial ATP-sensitive 'K POT. +' channel opening decreases reactive oxygen species generation. FEBS Letters, v. 536, n. 1-3, p. 51-55, 2003Tradução . . Disponível em: https://doi.org/10.1016/s0014-5793(03)00007-3. Acesso em: 06 jun. 2024.
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      Ferranti, R., Silva, M. M. da, & Kowaltowski, A. J. (2003). Mitochondrial ATP-sensitive 'K POT. +' channel opening decreases reactive oxygen species generation. FEBS Letters, 536( 1-3), 51-55. doi:10.1016/s0014-5793(03)00007-3
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      Ferranti R, Silva MM da, Kowaltowski AJ. Mitochondrial ATP-sensitive 'K POT. +' channel opening decreases reactive oxygen species generation [Internet]. FEBS Letters. 2003 ; 536( 1-3): 51-55.[citado 2024 jun. 06 ] Available from: https://doi.org/10.1016/s0014-5793(03)00007-3
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      Ferranti R, Silva MM da, Kowaltowski AJ. Mitochondrial ATP-sensitive 'K POT. +' channel opening decreases reactive oxygen species generation [Internet]. FEBS Letters. 2003 ; 536( 1-3): 51-55.[citado 2024 jun. 06 ] Available from: https://doi.org/10.1016/s0014-5793(03)00007-3
  • 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: 06 jun. 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
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      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 jun. 06 ] 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 jun. 06 ] Available from: https://doi.org/10.1016/s0891-5849(02)00786-4
  • 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: 06 jun. 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
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      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 jun. 06 ] Available from: https://doi.org/10.1016/s0891-5849(01)00516-0
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      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 jun. 06 ] Available from: https://doi.org/10.1016/s0891-5849(01)00516-0
  • Source: Febs Letters. Unidade: IQ

    Subjects: BIOQUÍMICA, CÁLCIO, RADICAIS LIVRES

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      KOWALTOWSKI, Alicia Juliana e CASTILHO, Roger F. e VERCESI, Anibal E. Mitochondrial permeability transition and oxidative stress. Febs Letters, v. 495, n. 1-2, p. 12-15, 2001Tradução . . Disponível em: https://doi.org/10.1016/s0014-5793(01)02316-x. Acesso em: 06 jun. 2024.
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      Kowaltowski, A. J., Castilho, R. F., & Vercesi, A. E. (2001). Mitochondrial permeability transition and oxidative stress. Febs Letters, 495( 1-2), 12-15. doi:10.1016/s0014-5793(01)02316-x
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      Kowaltowski AJ, Castilho RF, Vercesi AE. Mitochondrial permeability transition and oxidative stress [Internet]. Febs Letters. 2001 ; 495( 1-2): 12-15.[citado 2024 jun. 06 ] Available from: https://doi.org/10.1016/s0014-5793(01)02316-x
    • Vancouver

      Kowaltowski AJ, Castilho RF, Vercesi AE. Mitochondrial permeability transition and oxidative stress [Internet]. Febs Letters. 2001 ; 495( 1-2): 12-15.[citado 2024 jun. 06 ] Available from: https://doi.org/10.1016/s0014-5793(01)02316-x

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