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TEIXEIRA, P. C. et al. `delta´-aminolevulinic acid, ferritin and oxidative base damage to DNA. 1999, Anais.. São Paulo: SBBq, 1999. . Acesso em: 28 mar. 2024.
APA
Teixeira, P. C., Onuki, J., Medeiros, M. H. G. de, & Di Mascio, P. (1999). `delta´-aminolevulinic acid, ferritin and oxidative base damage to DNA. In Programa e Resumos. São Paulo: SBBq.
NLM
Teixeira PC, Onuki J, Medeiros MHG de, Di Mascio P. `delta´-aminolevulinic acid, ferritin and oxidative base damage to DNA. Programa e Resumos. 1999 ;[citado 2024 mar. 28 ]
Vancouver
Teixeira PC, Onuki J, Medeiros MHG de, Di Mascio P. `delta´-aminolevulinic acid, ferritin and oxidative base damage to DNA. Programa e Resumos. 1999 ;[citado 2024 mar. 28 ]
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GRIJALBA, Mercedes Toledo e VERCESI, Anibal E. e SCHREIER, Shirley. `Ca POT. 2+´-Induced increased lipid packing and domain formation in submitochondrial particles. A possible early step in the mechanism of `Ca POT. 2+´-stimulated generation of reactive oxygen species by the respiratory chain. Biochemistry, v. 38, n. 40, p. 13279-13287, 1999Tradução . . Acesso em: 28 mar. 2024.
APA
Grijalba, M. T., Vercesi, A. E., & Schreier, S. (1999). `Ca POT. 2+´-Induced increased lipid packing and domain formation in submitochondrial particles. A possible early step in the mechanism of `Ca POT. 2+´-stimulated generation of reactive oxygen species by the respiratory chain. Biochemistry, 38( 40), 13279-13287.
NLM
Grijalba MT, Vercesi AE, Schreier S. `Ca POT. 2+´-Induced increased lipid packing and domain formation in submitochondrial particles. A possible early step in the mechanism of `Ca POT. 2+´-stimulated generation of reactive oxygen species by the respiratory chain. Biochemistry. 1999 ; 38( 40): 13279-13287.[citado 2024 mar. 28 ]
Vancouver
Grijalba MT, Vercesi AE, Schreier S. `Ca POT. 2+´-Induced increased lipid packing and domain formation in submitochondrial particles. A possible early step in the mechanism of `Ca POT. 2+´-stimulated generation of reactive oxygen species by the respiratory chain. Biochemistry. 1999 ; 38( 40): 13279-13287.[citado 2024 mar. 28 ]
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CHAN, S. S. et al. `Alfa´-tocopherol modulates tyrosine phosphorylation-dependent signalling pathways in isolated human neutrophils. 1999, Anais.. São Paulo: SBBq, 1999. . Acesso em: 28 mar. 2024.
APA
Chan, S. S., Schindler, F., Junqueira, V. B. C., Stern, A., & Monteiro, H. P. (1999). `Alfa´-tocopherol modulates tyrosine phosphorylation-dependent signalling pathways in isolated human neutrophils. In Programa e Resumos. São Paulo: SBBq.
NLM
Chan SS, Schindler F, Junqueira VBC, Stern A, Monteiro HP. `Alfa´-tocopherol modulates tyrosine phosphorylation-dependent signalling pathways in isolated human neutrophils. Programa e Resumos. 1999 ;[citado 2024 mar. 28 ]
Vancouver
Chan SS, Schindler F, Junqueira VBC, Stern A, Monteiro HP. `Alfa´-tocopherol modulates tyrosine phosphorylation-dependent signalling pathways in isolated human neutrophils. Programa e Resumos. 1999 ;[citado 2024 mar. 28 ]
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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: 28 mar. 2024.
APA
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 mar. 28 ] 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 mar. 28 ] Available from: https://doi.org/10.1016/s0891-5849(00)00240-9
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KOWALTOWSKI, Alicia Juliana. Uma questão de ciência: devemos temer os radicais livres?. Tradução . Nexo, São Paulo, 2019. Disponível em: https://www.nexojornal.com.br/colunistas/2019/Uma-quest%C3%A3o-de-ci%C3%AAncia-devemos-temer-os-radicais-livres. Acesso em: 28 mar. 2024.
APA
Kowaltowski, A. J. (2019). Uma questão de ciência: devemos temer os radicais livres? Nexo. São Paulo: Instituto de Química, Universidade de São Paulo. Recuperado de https://www.nexojornal.com.br/colunistas/2019/Uma-quest%C3%A3o-de-ci%C3%AAncia-devemos-temer-os-radicais-livres
NLM
Kowaltowski AJ. Uma questão de ciência: devemos temer os radicais livres? [Internet]. Nexo. 2019 ;[citado 2024 mar. 28 ] Available from: https://www.nexojornal.com.br/colunistas/2019/Uma-quest%C3%A3o-de-ci%C3%AAncia-devemos-temer-os-radicais-livres
Vancouver
Kowaltowski AJ. Uma questão de ciência: devemos temer os radicais livres? [Internet]. Nexo. 2019 ;[citado 2024 mar. 28 ] Available from: https://www.nexojornal.com.br/colunistas/2019/Uma-quest%C3%A3o-de-ci%C3%AAncia-devemos-temer-os-radicais-livres
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KAWAI, Cintia et al. Two sites of cytochrome C structure can establish electrostatic interaction with mitochondrial mimetic membranes. 2004, Anais.. São Paulo: SBBC, 2004. . Acesso em: 28 mar. 2024.
APA
Kawai, C., Prado, F. M., Carmona-Ribeiro, A. M., Di Mascio, P., & Nantes, I. L. (2004). Two sites of cytochrome C structure can establish electrostatic interaction with mitochondrial mimetic membranes. In Abstracts. São Paulo: SBBC.
NLM
Kawai C, Prado FM, Carmona-Ribeiro AM, Di Mascio P, Nantes IL. Two sites of cytochrome C structure can establish electrostatic interaction with mitochondrial mimetic membranes. Abstracts. 2004 ;[citado 2024 mar. 28 ]
Vancouver
Kawai C, Prado FM, Carmona-Ribeiro AM, Di Mascio P, Nantes IL. Two sites of cytochrome C structure can establish electrostatic interaction with mitochondrial mimetic membranes. Abstracts. 2004 ;[citado 2024 mar. 28 ]
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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: 28 mar. 2024.
APA
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.
NLM
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 mar. 28 ]
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 mar. 28 ]
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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: 28 mar. 2024.
APA
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 mar. 28 ] 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 mar. 28 ] Available from: https://doi.org/10.1016/j.foodchem.2008.12.045
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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: 28 mar. 2024.
APA
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 mar. 28 ] 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 mar. 28 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2009.02.008
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TAHARA, Erich Birelli e NAVARETE, Felipe Donizeti Teston e KOWALTOWSKI, Alicia Juliana. Tissue and substrate-specific characteristics of mitochondrial reactive oxygen species release. 2007, Anais.. Montevideo: Facultad de Medicina/Departamento de Bioquímica, 2007. . Acesso em: 28 mar. 2024.
APA
Tahara, E. B., Navarete, F. D. T., & Kowaltowski, A. J. (2007). Tissue and substrate-specific characteristics of mitochondrial reactive oxygen species release. In Abstracts. Montevideo: Facultad de Medicina/Departamento de Bioquímica.
NLM
Tahara EB, Navarete FDT, Kowaltowski AJ. Tissue and substrate-specific characteristics of mitochondrial reactive oxygen species release. Abstracts. 2007 ;[citado 2024 mar. 28 ]
Vancouver
Tahara EB, Navarete FDT, Kowaltowski AJ. Tissue and substrate-specific characteristics of mitochondrial reactive oxygen species release. Abstracts. 2007 ;[citado 2024 mar. 28 ]
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PRADO, Fernanda Manso et al. Thymine hydroperoxide as a potential source of singlet molecular oxygen in DNA. Free Radical Biology & Medicine, v. 47, n. 4, p. 401-409, 2009Tradução . . Disponível em: https://doi.org/10.1016/j.freeradbiomed.2009.05.001. Acesso em: 28 mar. 2024.
APA
Prado, F. M., Oliveira, M. C. B. de, Miyamoto, S., Martinez, G. R., Medeiros, M. H. G. de, Ronsein, G. E., & Di Mascio, P. (2009). Thymine hydroperoxide as a potential source of singlet molecular oxygen in DNA. Free Radical Biology & Medicine, 47( 4), 401-409. doi:10.1016/j.freeradbiomed.2009.05.001
NLM
Prado FM, Oliveira MCB de, Miyamoto S, Martinez GR, Medeiros MHG de, Ronsein GE, Di Mascio P. Thymine hydroperoxide as a potential source of singlet molecular oxygen in DNA [Internet]. Free Radical Biology & Medicine. 2009 ; 47( 4): 401-409.[citado 2024 mar. 28 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2009.05.001
Vancouver
Prado FM, Oliveira MCB de, Miyamoto S, Martinez GR, Medeiros MHG de, Ronsein GE, Di Mascio P. Thymine hydroperoxide as a potential source of singlet molecular oxygen in DNA [Internet]. Free Radical Biology & Medicine. 2009 ; 47( 4): 401-409.[citado 2024 mar. 28 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2009.05.001
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TRUZZI, Daniela Ramos e AUGUSTO, Ohara e FORD, Peter C. Thiyl radicals are co-products of Dinitrosyl Iron Complexes (DNIC) formation. Free Radical Biology & Medicine. New York: Instituto de Química, Universidade de São Paulo. Disponível em: https://doi.org/10.1016/j.freeradbiomed.2019.10.041. Acesso em: 28 mar. 2024. , 2019
APA
Truzzi, D. R., Augusto, O., & Ford, P. C. (2019). Thiyl radicals are co-products of Dinitrosyl Iron Complexes (DNIC) formation. Free Radical Biology & Medicine. New York: Instituto de Química, Universidade de São Paulo. doi:10.1016/j.freeradbiomed.2019.10.041
NLM
Truzzi DR, Augusto O, Ford PC. Thiyl radicals are co-products of Dinitrosyl Iron Complexes (DNIC) formation [Internet]. Free Radical Biology & Medicine. 2019 ; 145 S17-S18 res. 03.[citado 2024 mar. 28 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2019.10.041
Vancouver
Truzzi DR, Augusto O, Ford PC. Thiyl radicals are co-products of Dinitrosyl Iron Complexes (DNIC) formation [Internet]. Free Radical Biology & Medicine. 2019 ; 145 S17-S18 res. 03.[citado 2024 mar. 28 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2019.10.041
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QUEIROZ, Raphael Ferreira et al. The carbonylation and covalent dimerization of human superoxide dismutase 1 caused by its bicarbonate-dependent peroxidase activity is inhibited by the radical scavenger tempol. Biochemical Journal, v. 455, p. 37-46 : + Supplementary materials ( S1-S2), 2013Tradução . . Disponível em: https://doi.org/10.1042/BJ20130180. Acesso em: 28 mar. 2024.
APA
Queiroz, R. F., Paviani, V., Coelho, F. R., Marques, E. F., Di Mascio, P., & Augusto, O. (2013). The carbonylation and covalent dimerization of human superoxide dismutase 1 caused by its bicarbonate-dependent peroxidase activity is inhibited by the radical scavenger tempol. Biochemical Journal, 455, 37-46 : + Supplementary materials ( S1-S2). doi:10.1042/BJ20130180
NLM
Queiroz RF, Paviani V, Coelho FR, Marques EF, Di Mascio P, Augusto O. The carbonylation and covalent dimerization of human superoxide dismutase 1 caused by its bicarbonate-dependent peroxidase activity is inhibited by the radical scavenger tempol [Internet]. Biochemical Journal. 2013 ; 455 37-46 : + Supplementary materials ( S1-S2).[citado 2024 mar. 28 ] Available from: https://doi.org/10.1042/BJ20130180
Vancouver
Queiroz RF, Paviani V, Coelho FR, Marques EF, Di Mascio P, Augusto O. The carbonylation and covalent dimerization of human superoxide dismutase 1 caused by its bicarbonate-dependent peroxidase activity is inhibited by the radical scavenger tempol [Internet]. Biochemical Journal. 2013 ; 455 37-46 : + Supplementary materials ( S1-S2).[citado 2024 mar. 28 ] Available from: https://doi.org/10.1042/BJ20130180
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DIAS, Valéria e AUGUSTO, Ohara e RIBEIRO, Antonio Augusto Coppi Maciel. Tempol tem efeito neuroprotetor leve em modelo animal de ELA. . São Paulo: Instituto de Química, Universidade de São Paulo. Disponível em: http://www.usp.br/agen/?p=143695. Acesso em: 28 mar. 2024. , 2013
APA
Dias, V., Augusto, O., & Ribeiro, A. A. C. M. (2013). Tempol tem efeito neuroprotetor leve em modelo animal de ELA. São Paulo: Instituto de Química, Universidade de São Paulo. Recuperado de http://www.usp.br/agen/?p=143695
NLM
Dias V, Augusto O, Ribeiro AACM. Tempol tem efeito neuroprotetor leve em modelo animal de ELA [Internet]. 2013 ;[citado 2024 mar. 28 ] Available from: http://www.usp.br/agen/?p=143695
Vancouver
Dias V, Augusto O, Ribeiro AACM. Tempol tem efeito neuroprotetor leve em modelo animal de ELA [Internet]. 2013 ;[citado 2024 mar. 28 ] Available from: http://www.usp.br/agen/?p=143695
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LINARES, Edlaine et al. Tempol moderately extends survival in a 'HSOD1 POT. G93A' ALS rat model by inhibiting neuronal cell loss, oxidative damage and levels of non-native 'HSOD1 POT. G93A' forms. PLOS ONE, v. 8, n. 2, p. 1-12, 2013Tradução . . Disponível em: https://doi.org/10.1371/journal.pone.0055868. Acesso em: 28 mar. 2024.
APA
Linares, E., Seixas, L. V., Prazeres, J. N. dos, Ladd, F. V. L., Ladd, A. A. B. L., Ribeiro, A. A. C. M., & Augusto, O. (2013). Tempol moderately extends survival in a 'HSOD1 POT. G93A' ALS rat model by inhibiting neuronal cell loss, oxidative damage and levels of non-native 'HSOD1 POT. G93A' forms. PLOS ONE, 8( 2), 1-12. doi:10.1371/journal.pone.0055868
NLM
Linares E, Seixas LV, Prazeres JN dos, Ladd FVL, Ladd AABL, Ribeiro AACM, Augusto O. Tempol moderately extends survival in a 'HSOD1 POT. G93A' ALS rat model by inhibiting neuronal cell loss, oxidative damage and levels of non-native 'HSOD1 POT. G93A' forms [Internet]. PLOS ONE. 2013 ; 8( 2): 1-12.[citado 2024 mar. 28 ] Available from: https://doi.org/10.1371/journal.pone.0055868
Vancouver
Linares E, Seixas LV, Prazeres JN dos, Ladd FVL, Ladd AABL, Ribeiro AACM, Augusto O. Tempol moderately extends survival in a 'HSOD1 POT. G93A' ALS rat model by inhibiting neuronal cell loss, oxidative damage and levels of non-native 'HSOD1 POT. G93A' forms [Internet]. PLOS ONE. 2013 ; 8( 2): 1-12.[citado 2024 mar. 28 ] Available from: https://doi.org/10.1371/journal.pone.0055868
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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: 28 mar. 2024.
APA
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 mar. 28 ] 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 mar. 28 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2004.09.027
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MEDINAS, D. B. e FERNANDES, D. C. e AUGUSTO, Ohara. Tempol diverts peroxynitrite reactivity towards albumin from tyrosine nitration and cysteine oxidation to cysteine nitrosation. 2003, Anais.. São Paulo: SBBq, 2003. . Acesso em: 28 mar. 2024.
APA
Medinas, D. B., Fernandes, D. C., & Augusto, O. (2003). Tempol diverts peroxynitrite reactivity towards albumin from tyrosine nitration and cysteine oxidation to cysteine nitrosation. In Programa e Resumos. São Paulo: SBBq.
NLM
Medinas DB, Fernandes DC, Augusto O. Tempol diverts peroxynitrite reactivity towards albumin from tyrosine nitration and cysteine oxidation to cysteine nitrosation. Programa e Resumos. 2003 ;[citado 2024 mar. 28 ]
Vancouver
Medinas DB, Fernandes DC, Augusto O. Tempol diverts peroxynitrite reactivity towards albumin from tyrosine nitration and cysteine oxidation to cysteine nitrosation. Programa e Resumos. 2003 ;[citado 2024 mar. 28 ]
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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: 28 mar. 2024.
APA
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 mar. 28 ] 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 mar. 28 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2009.12.013
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CASTANHEIRA, Bruna et al. Synthesis of novel periodic mesoporous organosilicas containing 1,4,5,8-Naphthalenediimides within the pore walls and their reduction To generate wall-embedded free radicals. Langmuir, v. 34, p. 8195-8204, 2018Tradução . . Disponível em: https://doi.org/10.1021/acs.langmuir.8b00220. Acesso em: 28 mar. 2024.
APA
Castanheira, B., Triboni, E. R., Andrade, L. dos S., Trindade, F. D. J., Otubo, L., Teixeira, A. C. S. C., et al. (2018). Synthesis of novel periodic mesoporous organosilicas containing 1,4,5,8-Naphthalenediimides within the pore walls and their reduction To generate wall-embedded free radicals. Langmuir, 34, 8195-8204. doi:10.1021/acs.langmuir.8b00220
NLM
Castanheira B, Triboni ER, Andrade L dos S, Trindade FDJ, Otubo L, Teixeira ACSC, Queiroz TB de, Brochsztain S, Politi MJ. Synthesis of novel periodic mesoporous organosilicas containing 1,4,5,8-Naphthalenediimides within the pore walls and their reduction To generate wall-embedded free radicals [Internet]. Langmuir. 2018 ; 34 8195-8204.[citado 2024 mar. 28 ] Available from: https://doi.org/10.1021/acs.langmuir.8b00220
Vancouver
Castanheira B, Triboni ER, Andrade L dos S, Trindade FDJ, Otubo L, Teixeira ACSC, Queiroz TB de, Brochsztain S, Politi MJ. Synthesis of novel periodic mesoporous organosilicas containing 1,4,5,8-Naphthalenediimides within the pore walls and their reduction To generate wall-embedded free radicals [Internet]. Langmuir. 2018 ; 34 8195-8204.[citado 2024 mar. 28 ] Available from: https://doi.org/10.1021/acs.langmuir.8b00220
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ABNT
MANO, Camila M. et al. Superoxide radical protects liposome-contained cytochrome c against oxidative damage promoted by peroxynitrite and free radicals. Free Radical Biology and Medicine, v. 47, p. 841-849, 2009Tradução . . Disponível em: https://doi.org/10.1016/j.freeradbiomed.2009.06.028. Acesso em: 28 mar. 2024.
APA
Mano, C. M., Barros, M. P., Faria, P. A., Prieto, T., Dyszy, F. H., Nascimento, O. R., et al. (2009). Superoxide radical protects liposome-contained cytochrome c against oxidative damage promoted by peroxynitrite and free radicals. Free Radical Biology and Medicine, 47, 841-849. doi:10.1016/j.freeradbiomed.2009.06.028
NLM
Mano CM, Barros MP, Faria PA, Prieto T, Dyszy FH, Nascimento OR, Nantes IL, Bechara EJH. Superoxide radical protects liposome-contained cytochrome c against oxidative damage promoted by peroxynitrite and free radicals [Internet]. Free Radical Biology and Medicine. 2009 ; 47 841-849.[citado 2024 mar. 28 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2009.06.028
Vancouver
Mano CM, Barros MP, Faria PA, Prieto T, Dyszy FH, Nascimento OR, Nantes IL, Bechara EJH. Superoxide radical protects liposome-contained cytochrome c against oxidative damage promoted by peroxynitrite and free radicals [Internet]. Free Radical Biology and Medicine. 2009 ; 47 841-849.[citado 2024 mar. 28 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2009.06.028