Filtros : "Indexado no Index Medicus" "RADICAIS LIVRES" "IQ" Removido: "STOLF, NOEDIR ANTONIO GROPPO" Limpar

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  • 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: 19 out. 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 out. 19 ] 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 out. 19 ] Available from: https://doi.org/10.1073/pnas.0708211105
  • 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: 19 out. 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
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      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 out. 19 ] 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 out. 19 ] 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: 19 out. 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 out. 19 ] 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 out. 19 ] 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: 19 out. 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 out. 19 ] 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 out. 19 ] 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: 19 out. 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 out. 19 ] 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 out. 19 ] 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: 19 out. 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 out. 19 ] 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 out. 19 ] 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: 19 out. 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
    • NLM

      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 out. 19 ] Available from: https://doi.org/10.1016/s0014-5793(03)00007-3
    • Vancouver

      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 out. 19 ] Available from: https://doi.org/10.1016/s0014-5793(03)00007-3
  • Source: Archives of Biochemistry and Biophysics. Unidade: IQ

    Subjects: BIOQUÍMICA, RADICAIS LIVRES, FERRO

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      ROCHA, Maria E. M. et al. Oxidative damage to ferritin by 5-aminolevulinic acid. Archives of Biochemistry and Biophysics, v. 409, n. 2, p. 349-356, 2003Tradução . . Disponível em: https://doi.org/10.1016/s0003-9861(02)00633-1. Acesso em: 19 out. 2024.
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      Rocha, M. E. M., Dutra, F., Bandy, B., Baldini, R. L., Gomes, S. L., Faljoni-Alário, A., et al. (2003). Oxidative damage to ferritin by 5-aminolevulinic acid. Archives of Biochemistry and Biophysics, 409( 2), 349-356. doi:10.1016/s0003-9861(02)00633-1
    • NLM

      Rocha MEM, Dutra F, Bandy B, Baldini RL, Gomes SL, Faljoni-Alário A, Liria CW, Miranda MTM de, Bechara EJH. Oxidative damage to ferritin by 5-aminolevulinic acid [Internet]. Archives of Biochemistry and Biophysics. 2003 ; 409( 2): 349-356.[citado 2024 out. 19 ] Available from: https://doi.org/10.1016/s0003-9861(02)00633-1
    • Vancouver

      Rocha MEM, Dutra F, Bandy B, Baldini RL, Gomes SL, Faljoni-Alário A, Liria CW, Miranda MTM de, Bechara EJH. Oxidative damage to ferritin by 5-aminolevulinic acid [Internet]. Archives of Biochemistry and Biophysics. 2003 ; 409( 2): 349-356.[citado 2024 out. 19 ] Available from: https://doi.org/10.1016/s0003-9861(02)00633-1
  • 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: 19 out. 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 out. 19 ] 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 out. 19 ] 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: 19 out. 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 out. 19 ] 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 out. 19 ] 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: 19 out. 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
    • NLM

      Kowaltowski AJ, Castilho RF, Vercesi AE. Mitochondrial permeability transition and oxidative stress [Internet]. Febs Letters. 2001 ; 495( 1-2): 12-15.[citado 2024 out. 19 ] 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 out. 19 ] Available from: https://doi.org/10.1016/s0014-5793(01)02316-x
  • Source: Archives of Biochemistry and Biophysics. Unidade: IQ

    Subjects: BIOQUÍMICA, RADICAIS LIVRES

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      BATTHYÁNY, Carlos et al. Direct evidence for apo B-100-mediated copper reduction: studies with purified apo B-100 and detection of tryptophanyl radicals. Archives of Biochemistry and Biophysics, v. 384, n. 2, p. 335-340, 2000Tradução . . Acesso em: 19 out. 2024.
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      Batthyány, C., Santos, C. X. C., Botti, H., Cerveñansky, C., Radi, R., Augusto, O., & Rubbo, H. (2000). Direct evidence for apo B-100-mediated copper reduction: studies with purified apo B-100 and detection of tryptophanyl radicals. Archives of Biochemistry and Biophysics, 384( 2), 335-340.
    • NLM

      Batthyány C, Santos CXC, Botti H, Cerveñansky C, Radi R, Augusto O, Rubbo H. Direct evidence for apo B-100-mediated copper reduction: studies with purified apo B-100 and detection of tryptophanyl radicals. Archives of Biochemistry and Biophysics. 2000 ; 384( 2): 335-340.[citado 2024 out. 19 ]
    • Vancouver

      Batthyány C, Santos CXC, Botti H, Cerveñansky C, Radi R, Augusto O, Rubbo H. Direct evidence for apo B-100-mediated copper reduction: studies with purified apo B-100 and detection of tryptophanyl radicals. Archives of Biochemistry and Biophysics. 2000 ; 384( 2): 335-340.[citado 2024 out. 19 ]
  • 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: 19 out. 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 out. 19 ] 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 out. 19 ] 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: 19 out. 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 out. 19 ] 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 out. 19 ] 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: 19 out. 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 out. 19 ] 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 out. 19 ] Available from: https://doi.org/10.1016/s0891-5849(00)00159-3
  • Source: Free Radical Biology & Medicine. Unidade: IQ

    Subjects: BIOQUÍMICA, RADICAIS LIVRES

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      NAKAO, Lia S et al. Metabolism of acetaldehyde to methyl and acetyl radicals: in vitro and in vivo electron paramagnetic resonance spin-trapping studies. Free Radical Biology & Medicine, v. 29, n. 8, p. 721-729, 2000Tradução . . Disponível em: https://doi.org/10.1016/s0891-5849(00)00374-9. Acesso em: 19 out. 2024.
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      Nakao, L. S., Kadiiska, M. B., Mason, R. P., Grijalba, M. T., & Augusto, O. (2000). Metabolism of acetaldehyde to methyl and acetyl radicals: in vitro and in vivo electron paramagnetic resonance spin-trapping studies. Free Radical Biology & Medicine, 29( 8), 721-729. doi:10.1016/s0891-5849(00)00374-9
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      Nakao LS, Kadiiska MB, Mason RP, Grijalba MT, Augusto O. Metabolism of acetaldehyde to methyl and acetyl radicals: in vitro and in vivo electron paramagnetic resonance spin-trapping studies [Internet]. Free Radical Biology & Medicine. 2000 ; 29( 8): 721-729.[citado 2024 out. 19 ] Available from: https://doi.org/10.1016/s0891-5849(00)00374-9
    • Vancouver

      Nakao LS, Kadiiska MB, Mason RP, Grijalba MT, Augusto O. Metabolism of acetaldehyde to methyl and acetyl radicals: in vitro and in vivo electron paramagnetic resonance spin-trapping studies [Internet]. Free Radical Biology & Medicine. 2000 ; 29( 8): 721-729.[citado 2024 out. 19 ] Available from: https://doi.org/10.1016/s0891-5849(00)00374-9
  • Source: Free Radical Biology & Medicine. Unidade: IQ

    Subjects: BIOQUÍMICA, RADICAIS LIVRES

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      ROCHA, Maria Eliane Merlin e FERREIRA, Ana Maria da Costa e BECHARA, Etelvino José Henriques. Roles od phosphate and an enoyl radical in ferritin iron mobilization by 5-aminolevulinic acid. Free Radical Biology & Medicine, v. 29, n. 12, p. 1272-1279, 2000Tradução . . Disponível em: https://doi.org/10.1016/s0891-5849(00)00437-8. Acesso em: 19 out. 2024.
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      Rocha, M. E. M., Ferreira, A. M. da C., & Bechara, E. J. H. (2000). Roles od phosphate and an enoyl radical in ferritin iron mobilization by 5-aminolevulinic acid. Free Radical Biology & Medicine, 29( 12), 1272-1279. doi:10.1016/s0891-5849(00)00437-8
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      Rocha MEM, Ferreira AM da C, Bechara EJH. Roles od phosphate and an enoyl radical in ferritin iron mobilization by 5-aminolevulinic acid [Internet]. Free Radical Biology & Medicine. 2000 ; 29( 12): 1272-1279.[citado 2024 out. 19 ] Available from: https://doi.org/10.1016/s0891-5849(00)00437-8
    • Vancouver

      Rocha MEM, Ferreira AM da C, Bechara EJH. Roles od phosphate and an enoyl radical in ferritin iron mobilization by 5-aminolevulinic acid [Internet]. Free Radical Biology & Medicine. 2000 ; 29( 12): 1272-1279.[citado 2024 out. 19 ] Available from: https://doi.org/10.1016/s0891-5849(00)00437-8
  • Source: Free Radical Biology & Medicine. Unidade: IQ

    Subjects: BIOQUÍMICA, RADICAIS LIVRES

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      TIMMINS, Graham S. et al. Trapping of free radicals with direct in vivo EPR detection: a comparison of 5,5-dimethyl-1-pyrroline-N-oxide and 5-diethoxyphosphoryl-5-methyl-1-pyrroline-N-oxide as spin traps for `H´`O PONTO´ and `S´`O IND. 4 POT. PONTO-´. Free Radical Biology & Medicine, v. 27, n. 3/4, p. 329-333, 1999Tradução . . Acesso em: 19 out. 2024.
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      Timmins, G. S., Liu, K. J., Bechara, E. J. H., Kotake, Y., & Swartz, H. M. (1999). Trapping of free radicals with direct in vivo EPR detection: a comparison of 5,5-dimethyl-1-pyrroline-N-oxide and 5-diethoxyphosphoryl-5-methyl-1-pyrroline-N-oxide as spin traps for `H´`O PONTO´ and `S´`O IND. 4 POT. PONTO-´. Free Radical Biology & Medicine, 27( 3/4), 329-333.
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      Timmins GS, Liu KJ, Bechara EJH, Kotake Y, Swartz HM. Trapping of free radicals with direct in vivo EPR detection: a comparison of 5,5-dimethyl-1-pyrroline-N-oxide and 5-diethoxyphosphoryl-5-methyl-1-pyrroline-N-oxide as spin traps for `H´`O PONTO´ and `S´`O IND. 4 POT. PONTO-´. Free Radical Biology & Medicine. 1999 ; 27( 3/4): 329-333.[citado 2024 out. 19 ]
    • Vancouver

      Timmins GS, Liu KJ, Bechara EJH, Kotake Y, Swartz HM. Trapping of free radicals with direct in vivo EPR detection: a comparison of 5,5-dimethyl-1-pyrroline-N-oxide and 5-diethoxyphosphoryl-5-methyl-1-pyrroline-N-oxide as spin traps for `H´`O PONTO´ and `S´`O IND. 4 POT. PONTO-´. Free Radical Biology & Medicine. 1999 ; 27( 3/4): 329-333.[citado 2024 out. 19 ]
  • Source: Free Radical Biology & Medicine. Unidade: IQ

    Subjects: BIOQUÍMICA, RADICAIS LIVRES

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      ALMEIDA, Andréa M. et al. Diphenylacetaldehyde-generated excited states promote damage to isolated rat liver mitochondrial DNA, phospholipids, and proteins. Free Radical Biology & Medicine, v. 27, n. 7/8, p. 744-751, 1999Tradução . . Disponível em: https://doi.org/10.1016/s0891-5849(99)00136-7. Acesso em: 19 out. 2024.
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      Almeida, A. M., Bechara, E. J. H., Vercesi, A. E., & Nantes, I. L. (1999). Diphenylacetaldehyde-generated excited states promote damage to isolated rat liver mitochondrial DNA, phospholipids, and proteins. Free Radical Biology & Medicine, 27( 7/8), 744-751. doi:10.1016/s0891-5849(99)00136-7
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      Almeida AM, Bechara EJH, Vercesi AE, Nantes IL. Diphenylacetaldehyde-generated excited states promote damage to isolated rat liver mitochondrial DNA, phospholipids, and proteins [Internet]. Free Radical Biology & Medicine. 1999 ; 27( 7/8): 744-751.[citado 2024 out. 19 ] Available from: https://doi.org/10.1016/s0891-5849(99)00136-7
    • Vancouver

      Almeida AM, Bechara EJH, Vercesi AE, Nantes IL. Diphenylacetaldehyde-generated excited states promote damage to isolated rat liver mitochondrial DNA, phospholipids, and proteins [Internet]. Free Radical Biology & Medicine. 1999 ; 27( 7/8): 744-751.[citado 2024 out. 19 ] Available from: https://doi.org/10.1016/s0891-5849(99)00136-7

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