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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: 15 nov. 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 nov. 15 ] 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 nov. 15 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2009.12.013
  • Source: Archives of Biochemistry and Biophysics. Unidade: IQ

    Subjects: ZINCO, COBRE, SUPERÓXIDO DISMUTASE, ÓXIDO NÍTRICO, PROTEÍNAS

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      VAZ, Sandra Muntz et al. Oxidation and nitration of ribonuclease and lysozyme by peroxynitrite and myeloperoxidase. Archives of Biochemistry and Biophysics, v. 484, n. 2, p. 127-133, 2009Tradução . . Disponível em: https://doi.org/10.1016/j.abb.2008.12.017. Acesso em: 15 nov. 2024.
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      Vaz, S. M., Prado, F. M., Di Mascio, P., & Augusto, O. (2009). Oxidation and nitration of ribonuclease and lysozyme by peroxynitrite and myeloperoxidase. Archives of Biochemistry and Biophysics, 484( 2), 127-133. doi:10.1016/j.abb.2008.12.017
    • NLM

      Vaz SM, Prado FM, Di Mascio P, Augusto O. Oxidation and nitration of ribonuclease and lysozyme by peroxynitrite and myeloperoxidase [Internet]. Archives of Biochemistry and Biophysics. 2009 ; 484( 2): 127-133.[citado 2024 nov. 15 ] Available from: https://doi.org/10.1016/j.abb.2008.12.017
    • Vancouver

      Vaz SM, Prado FM, Di Mascio P, Augusto O. Oxidation and nitration of ribonuclease and lysozyme by peroxynitrite and myeloperoxidase [Internet]. Archives of Biochemistry and Biophysics. 2009 ; 484( 2): 127-133.[citado 2024 nov. 15 ] Available from: https://doi.org/10.1016/j.abb.2008.12.017
  • Source: Fungal Genetics and Biology. Unidade: IQ

    Subjects: ÓXIDO NÍTRICO, FUNGOS, BIOQUÍMICA

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      VIEIRA, André Luiz Gomes et al. Evidence of a 'Ca POT. 2+'-'PONTO'NO-cGMP signaling pathway controlling zoospore biogenesis in the aquatic fungus Blastocladiella emersonii. Fungal Genetics and Biology, v. 46, n. 8, p. 575-584, 2009Tradução . . Acesso em: 15 nov. 2024.
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      Vieira, A. L. G., Linares, E., Augusto, O., & Gomes, S. L. (2009). Evidence of a 'Ca POT. 2+'-'PONTO'NO-cGMP signaling pathway controlling zoospore biogenesis in the aquatic fungus Blastocladiella emersonii. Fungal Genetics and Biology, 46( 8), 575-584.
    • NLM

      Vieira ALG, Linares E, Augusto O, Gomes SL. Evidence of a 'Ca POT. 2+'-'PONTO'NO-cGMP signaling pathway controlling zoospore biogenesis in the aquatic fungus Blastocladiella emersonii. Fungal Genetics and Biology. 2009 ; 46( 8): 575-584.[citado 2024 nov. 15 ]
    • Vancouver

      Vieira ALG, Linares E, Augusto O, Gomes SL. Evidence of a 'Ca POT. 2+'-'PONTO'NO-cGMP signaling pathway controlling zoospore biogenesis in the aquatic fungus Blastocladiella emersonii. Fungal Genetics and Biology. 2009 ; 46( 8): 575-584.[citado 2024 nov. 15 ]
  • 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: 15 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. 15 ] 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. 15 ] 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: 15 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. 15 ] 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. 15 ] Available from: https://doi.org/10.1016/j.taap.2008.07.023
  • Source: IUBMB Life (International Union of Biochemistry and Molecular Biology: Life). Unidade: IQ

    Subjects: BIOQUÍMICA, OXIDAÇÃO

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      MEDINAS, Danilo Bilches et al. The carbonate radical and related oxidants derived from bicarbonate buffer. IUBMB Life (International Union of Biochemistry and Molecular Biology: Life), v. 59, n. 4-5, p. 255-262, 2007Tradução . . Disponível em: https://doi.org/10.1080/15216540701230511. Acesso em: 15 nov. 2024.
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      Medinas, D. B., Cerchiaro, G., Trindade, D. F., & Augusto, O. (2007). The carbonate radical and related oxidants derived from bicarbonate buffer. IUBMB Life (International Union of Biochemistry and Molecular Biology: Life), 59( 4-5), 255-262. doi:10.1080/15216540701230511
    • NLM

      Medinas DB, Cerchiaro G, Trindade DF, Augusto O. The carbonate radical and related oxidants derived from bicarbonate buffer [Internet]. IUBMB Life (International Union of Biochemistry and Molecular Biology: Life). 2007 ; 59( 4-5): 255-262.[citado 2024 nov. 15 ] Available from: https://doi.org/10.1080/15216540701230511
    • Vancouver

      Medinas DB, Cerchiaro G, Trindade DF, Augusto O. The carbonate radical and related oxidants derived from bicarbonate buffer [Internet]. IUBMB Life (International Union of Biochemistry and Molecular Biology: Life). 2007 ; 59( 4-5): 255-262.[citado 2024 nov. 15 ] Available from: https://doi.org/10.1080/15216540701230511
  • Source: Amino Acids. Unidade: IQ

    Subjects: SUPERÓXIDO DISMUTASE, RESSONÂNCIA PARAMAGNÉTICA DE SPIN

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      AUGUSTO, Ohara e VAZ, Sandra Muntz. EPR spin-trapping of protein radicals to investigate biological oxidative mechanisms. Amino Acids, v. 32, n. 4, p. 535-542, 2007Tradução . . Disponível em: https://doi.org/10.1007/s00726-006-0429-4. Acesso em: 15 nov. 2024.
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      Augusto, O., & Vaz, S. M. (2007). EPR spin-trapping of protein radicals to investigate biological oxidative mechanisms. Amino Acids, 32( 4), 535-542. doi:10.1007/s00726-006-0429-4
    • NLM

      Augusto O, Vaz SM. EPR spin-trapping of protein radicals to investigate biological oxidative mechanisms [Internet]. Amino Acids. 2007 ; 32( 4): 535-542.[citado 2024 nov. 15 ] Available from: https://doi.org/10.1007/s00726-006-0429-4
    • Vancouver

      Augusto O, Vaz SM. EPR spin-trapping of protein radicals to investigate biological oxidative mechanisms [Internet]. Amino Acids. 2007 ; 32( 4): 535-542.[citado 2024 nov. 15 ] Available from: https://doi.org/10.1007/s00726-006-0429-4
  • Source: Organometallics. Unidade: IQ

    Subjects: TELÚRIO, QUÍMICA ORGÂNICA, ESPECTROMETRIA DE MASSAS (MÉTODOS)

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      KEPPLER, Artur Franz et al. Organic tellurium-centered radicals evidenced by EPR spin trapping and mass spectrometry experiments: insights into the mechanism of the hydrotelluration reaction. Organometallics, v. 25, n. 21, p. 5059-5066, 2006Tradução . . Acesso em: 15 nov. 2024.
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      Keppler, A. F., Cerchiaro, G., Augusto, O., Miyamoto, S., Prado, F. M., Di Mascio, P., & Comasseto, J. V. (2006). Organic tellurium-centered radicals evidenced by EPR spin trapping and mass spectrometry experiments: insights into the mechanism of the hydrotelluration reaction. Organometallics, 25( 21), 5059-5066.
    • NLM

      Keppler AF, Cerchiaro G, Augusto O, Miyamoto S, Prado FM, Di Mascio P, Comasseto JV. Organic tellurium-centered radicals evidenced by EPR spin trapping and mass spectrometry experiments: insights into the mechanism of the hydrotelluration reaction. Organometallics. 2006 ; 25( 21): 5059-5066.[citado 2024 nov. 15 ]
    • Vancouver

      Keppler AF, Cerchiaro G, Augusto O, Miyamoto S, Prado FM, Di Mascio P, Comasseto JV. Organic tellurium-centered radicals evidenced by EPR spin trapping and mass spectrometry experiments: insights into the mechanism of the hydrotelluration reaction. Organometallics. 2006 ; 25( 21): 5059-5066.[citado 2024 nov. 15 ]
  • Source: Chemical Research in Toxicology. Unidade: IQ

    Subjects: SOLUÇÕES AQUOSAS, BIOQUÍMICA, SUPERÓXIDO DISMUTASE

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      TRINDADE, Daniel Fernando e CERCHIARO, Giselle e AUGUSTO, Ohara. A role for peroxymonocarbonate in the stimulation of biothiol peroxidation by the bicarbonate/carbon dioxide pair. Chemical Research in Toxicology, v. 19, n. 11, p. 1475-1482, 2006Tradução . . Acesso em: 15 nov. 2024.
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      Trindade, D. F., Cerchiaro, G., & Augusto, O. (2006). A role for peroxymonocarbonate in the stimulation of biothiol peroxidation by the bicarbonate/carbon dioxide pair. Chemical Research in Toxicology, 19( 11), 1475-1482.
    • NLM

      Trindade DF, Cerchiaro G, Augusto O. A role for peroxymonocarbonate in the stimulation of biothiol peroxidation by the bicarbonate/carbon dioxide pair. Chemical Research in Toxicology. 2006 ; 19( 11): 1475-1482.[citado 2024 nov. 15 ]
    • Vancouver

      Trindade DF, Cerchiaro G, Augusto O. A role for peroxymonocarbonate in the stimulation of biothiol peroxidation by the bicarbonate/carbon dioxide pair. Chemical Research in Toxicology. 2006 ; 19( 11): 1475-1482.[citado 2024 nov. 15 ]
  • 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: 15 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. 15 ] 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. 15 ] 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: 15 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. 15 ] 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. 15 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2004.09.027
  • Source: Journal of Biological Chemistry. Unidade: IQ

    Subjects: ÓXIDO NÍTRICO, BIOQUÍMICA, APOPTOSE

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      CHEN, Yeong-Renn et al. Formation of protein tyrosine ortho-semiquinone radical and nitrotyrosine from cytochrome c-derived tyrosyl radical. Journal of Biological Chemistry, v. 279, n. 17, p. 18054-18062, 2004Tradução . . Acesso em: 15 nov. 2024.
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      Chen, Y. -R., Chen, C. -L., Chen, W., Zweier, J. L., Augusto, O., Radi, R., & Mason, R. P. (2004). Formation of protein tyrosine ortho-semiquinone radical and nitrotyrosine from cytochrome c-derived tyrosyl radical. Journal of Biological Chemistry, 279( 17), 18054-18062.
    • NLM

      Chen Y-R, Chen C-L, Chen W, Zweier JL, Augusto O, Radi R, Mason RP. Formation of protein tyrosine ortho-semiquinone radical and nitrotyrosine from cytochrome c-derived tyrosyl radical. Journal of Biological Chemistry. 2004 ; 279( 17): 18054-18062.[citado 2024 nov. 15 ]
    • Vancouver

      Chen Y-R, Chen C-L, Chen W, Zweier JL, Augusto O, Radi R, Mason RP. Formation of protein tyrosine ortho-semiquinone radical and nitrotyrosine from cytochrome c-derived tyrosyl radical. Journal of Biological Chemistry. 2004 ; 279( 17): 18054-18062.[citado 2024 nov. 15 ]
  • 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: 15 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. 15 ] 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. 15 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2004.02.076
  • Source: Journal of Biological Chemistry. Unidade: IQ

    Subjects: ÓXIDO NÍTRICO, SUPERÓXIDO DISMUTASE, PEROXIDASE

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      BONINI, Marcelo Gialluisi et al. Production of the carbonate radical anion during xanthine oxidase turnover in the presence of bicarbonate. Journal of Biological Chemistry, v. 279, n. 50, p. 51836-51843, 2004Tradução . . Acesso em: 15 nov. 2024.
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      Bonini, M. G., Miyamoto, S., Di Mascio, P., & Augusto, O. (2004). Production of the carbonate radical anion during xanthine oxidase turnover in the presence of bicarbonate. Journal of Biological Chemistry, 279( 50), 51836-51843.
    • NLM

      Bonini MG, Miyamoto S, Di Mascio P, Augusto O. Production of the carbonate radical anion during xanthine oxidase turnover in the presence of bicarbonate. Journal of Biological Chemistry. 2004 ; 279( 50): 51836-51843.[citado 2024 nov. 15 ]
    • Vancouver

      Bonini MG, Miyamoto S, Di Mascio P, Augusto O. Production of the carbonate radical anion during xanthine oxidase turnover in the presence of bicarbonate. Journal of Biological Chemistry. 2004 ; 279( 50): 51836-51843.[citado 2024 nov. 15 ]
  • Source: Biochemistry. Unidade: IQ

    Subjects: AMINOÁCIDOS, BIOQUÍMICA, ALBUMINAS

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      BONINI, Marcelo Gialluisi e FERNANDES, Denise de Castro e AUGUSTO, Ohara. Albumin oxidation to diverse radicals by the peroxidase activity of Cu,Zn-superoxide dismutase in the presence of bicarbonate or nitrite: diffusible radicals produce cysteinyl and solvent-exposed and -unexposed tyrosyl radicals. Biochemistry, v. 43, n. 2, p. 344-351, 2004Tradução . . Acesso em: 15 nov. 2024.
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      Bonini, M. G., Fernandes, D. de C., & Augusto, O. (2004). Albumin oxidation to diverse radicals by the peroxidase activity of Cu,Zn-superoxide dismutase in the presence of bicarbonate or nitrite: diffusible radicals produce cysteinyl and solvent-exposed and -unexposed tyrosyl radicals. Biochemistry, 43( 2), 344-351.
    • NLM

      Bonini MG, Fernandes D de C, Augusto O. Albumin oxidation to diverse radicals by the peroxidase activity of Cu,Zn-superoxide dismutase in the presence of bicarbonate or nitrite: diffusible radicals produce cysteinyl and solvent-exposed and -unexposed tyrosyl radicals. Biochemistry. 2004 ; 43( 2): 344-351.[citado 2024 nov. 15 ]
    • Vancouver

      Bonini MG, Fernandes D de C, Augusto O. Albumin oxidation to diverse radicals by the peroxidase activity of Cu,Zn-superoxide dismutase in the presence of bicarbonate or nitrite: diffusible radicals produce cysteinyl and solvent-exposed and -unexposed tyrosyl radicals. Biochemistry. 2004 ; 43( 2): 344-351.[citado 2024 nov. 15 ]
  • Source: Journal of Biological Chemistry. Unidade: IQ

    Subjects: BIOQUÍMICA, OXIDAÇÃO

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      ROMERO, Natalia et al. Reaction of human hemoglobin with peroxynitrite Isomerization to nitrate and secondary formation of protein radicals. Journal of Biological Chemistry, v. 278, n. 45, p. 44049-44057, 2003Tradução . . Acesso em: 15 nov. 2024.
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      Romero, N., Radi, R., Linares, E., Augusto, O., Detweiler, C. D., Manson, R. P., & Denicola, A. (2003). Reaction of human hemoglobin with peroxynitrite Isomerization to nitrate and secondary formation of protein radicals. Journal of Biological Chemistry, 278( 45), 44049-44057.
    • NLM

      Romero N, Radi R, Linares E, Augusto O, Detweiler CD, Manson RP, Denicola A. Reaction of human hemoglobin with peroxynitrite Isomerization to nitrate and secondary formation of protein radicals. Journal of Biological Chemistry. 2003 ; 278( 45): 44049-44057.[citado 2024 nov. 15 ]
    • Vancouver

      Romero N, Radi R, Linares E, Augusto O, Detweiler CD, Manson RP, Denicola A. Reaction of human hemoglobin with peroxynitrite Isomerization to nitrate and secondary formation of protein radicals. Journal of Biological Chemistry. 2003 ; 278( 45): 44049-44057.[citado 2024 nov. 15 ]
  • Source: Free Radical Research. Unidade: IQ

    Subjects: BIOQUÍMICA, OXIDAÇÃO, REDUÇÃO, HIDROGÊNIO (TRANSFERÊNCIA)

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      ALIAGA, C. et al. Kinetics and mechanism of the reaction of a nitroxide radical (Tempol) with a phenolic antioxidant. Free Radical Research, v. 37, n. 3, p. 225-230, 2003Tradução . . Acesso em: 15 nov. 2024.
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      Aliaga, C., Lissi, E. A., Augusto, O., & Linares, E. (2003). Kinetics and mechanism of the reaction of a nitroxide radical (Tempol) with a phenolic antioxidant. Free Radical Research, 37( 3), 225-230.
    • NLM

      Aliaga C, Lissi EA, Augusto O, Linares E. Kinetics and mechanism of the reaction of a nitroxide radical (Tempol) with a phenolic antioxidant. Free Radical Research. 2003 ; 37( 3): 225-230.[citado 2024 nov. 15 ]
    • Vancouver

      Aliaga C, Lissi EA, Augusto O, Linares E. Kinetics and mechanism of the reaction of a nitroxide radical (Tempol) with a phenolic antioxidant. Free Radical Research. 2003 ; 37( 3): 225-230.[citado 2024 nov. 15 ]
  • 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: 15 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. 15 ] 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. 15 ] Available from: https://doi.org/10.1016/s0891-5849(02)01424-7
  • Source: Chemical Research in Toxicology. Unidade: IQ

    Subjects: BIOQUÍMICA, SUPERÓXIDO DISMUTASE (ATIVIDADE), ÓXIDO NÍTRICO, OXIDAÇÃO

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      BONINI, Marcelo G. e MASON, Ronald P. e AUGUSTO, Ohara. The mechanism by which 4-hydroxy-2,2,6,6-tetramethylpiperidene-1-oxyl (tempol) diverts peroxynitrite decomposition from nitrating to nitrosating species. Chemical Research in Toxicology, v. 15, n. 4, p. 506-511, 2002Tradução . . Acesso em: 15 nov. 2024.
    • APA

      Bonini, M. G., Mason, R. P., & Augusto, O. (2002). The mechanism by which 4-hydroxy-2,2,6,6-tetramethylpiperidene-1-oxyl (tempol) diverts peroxynitrite decomposition from nitrating to nitrosating species. Chemical Research in Toxicology, 15( 4), 506-511.
    • NLM

      Bonini MG, Mason RP, Augusto O. The mechanism by which 4-hydroxy-2,2,6,6-tetramethylpiperidene-1-oxyl (tempol) diverts peroxynitrite decomposition from nitrating to nitrosating species. Chemical Research in Toxicology. 2002 ; 15( 4): 506-511.[citado 2024 nov. 15 ]
    • Vancouver

      Bonini MG, Mason RP, Augusto O. The mechanism by which 4-hydroxy-2,2,6,6-tetramethylpiperidene-1-oxyl (tempol) diverts peroxynitrite decomposition from nitrating to nitrosating species. Chemical Research in Toxicology. 2002 ; 15( 4): 506-511.[citado 2024 nov. 15 ]
  • 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: 15 nov. 2024.
    • APA

      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. 15 ] 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. 15 ] Available from: https://doi.org/10.1016/s0891-5849(02)00786-4

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