The carbonylation and covalent dimerization of hSOD1 caused by its bicarbonate-dependent peroxidase activity is inhibited by tempol (2013)
- Authors:
- USP affiliated authors: MASCIO, PAOLO DI - IQ ; AUGUSTO, OHARA - IQ
- Unidade: IQ
- Subjects: PEROXIDASE; BIOQUÍMICA
- Language: Inglês
- Imprenta:
- Source:
- Título do periódico: Free Radical Biology & Medicine
- ISSN: 0891-5849
- Volume/Número/Paginação/Ano: v. 65, Suppl. 2, p. S93 res. 201, 2013
- Conference titles: Annual Meeting of the Society for Free Radical Biology and Medicine (SFRBM)
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ABNT
QUEIROZ, Raphael Ferreira et al. The carbonylation and covalent dimerization of hSOD1 caused by its bicarbonate-dependent peroxidase activity is inhibited by tempol. Free Radical Biology & Medicine. New York: Instituto de Química, Universidade de São Paulo. . Acesso em: 18 abr. 2024. , 2013 -
APA
Queiroz, R. F., Paviani, V., Coelho, F. R., Marques, E. F., Di Mascio, P., & Augusto, O. (2013). The carbonylation and covalent dimerization of hSOD1 caused by its bicarbonate-dependent peroxidase activity is inhibited by tempol. Free Radical Biology & Medicine. New York: Instituto de Química, Universidade de São Paulo. -
NLM
Queiroz RF, Paviani V, Coelho FR, Marques EF, Di Mascio P, Augusto O. The carbonylation and covalent dimerization of hSOD1 caused by its bicarbonate-dependent peroxidase activity is inhibited by tempol. Free Radical Biology & Medicine. 2013 ; 65 S93 res. 201.[citado 2024 abr. 18 ] -
Vancouver
Queiroz RF, Paviani V, Coelho FR, Marques EF, Di Mascio P, Augusto O. The carbonylation and covalent dimerization of hSOD1 caused by its bicarbonate-dependent peroxidase activity is inhibited by tempol. Free Radical Biology & Medicine. 2013 ; 65 S93 res. 201.[citado 2024 abr. 18 ] - Peroxynitrite does not decompose to singlet oxygen ( `ANTPOT. delta IND. g´`O IND. 2´) and nitroxyl (N`O POT. -´)
- Oxidation and nitration of ribonuclease and lysozyme by peroxynitrite and myeloperoxidase
- Evidences for the production of the carbonate radical anion during xanthine oxidase turnover
- Production of the carbonate radical anion during xanthine oxidase turnover in the presence of bicarbonate
- MS characterization of the ditryptophan cross links in lysozyme submitted to enzymatically and photolytically generated carbonate radicals
- Production of the carbonate radical anion during xanthine oxidase turnover in the presence of bicarbonate
- The carbonylation and covalent dimerization of human superoxide dismutase 1 caused by its bicarbonate-dependent peroxidase activity is inhibited by the radical scavenger tempol
- Characterization of a ditryptophan cross-link in hen lysozyme oxidized by the carbonate radical
- Production of lysozyme and lysozyme-superoxide dismutase dimers bound by a ditryptophan cross-link in carbonate radical-treated lysozyme
- Cytochrome c reacts with cholesterol hydroperoxides to produce lipid- and protein-derived radicals
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