Characterization of changes in the apo form of enzyme Cu, Zn superoxide dismutase promoted by docosahexaenoic acid and their hydroperoxides (2012)
- Authors:
- USP affiliated authors: NETTO, LUIS EDUARDO SOARES - IB ; AUGUSTO, OHARA - IQ ; MIYAMOTO, SAYURI - IQ
- Unidades: IB; IQ
- Subjects: SUPERÓXIDO DISMUTASE; ÁCIDOS GRAXOS
- Language: Inglês
- Imprenta:
- Source:
- Título: Free Radical Biology & Medicine
- ISSN: 0891-5849
- Volume/Número/Paginação/Ano: v. 53, suppl. 2, p. S133 res. 322, 2012
- Conference titles: Annual Meeting of the Society for Free Radical Biology and Medicine (SFRBM)
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ABNT
APPOLINÁRIO, Patricia Postilione et al. Characterization of changes in the apo form of enzyme Cu, Zn superoxide dismutase promoted by docosahexaenoic acid and their hydroperoxides. Free Radical Biology & Medicine. New York: Instituto de Biociências, Universidade de São Paulo. . Acesso em: 27 dez. 2025. , 2012 -
APA
Appolinário, P. P., Medinas, D. B., Genaro-Mattos, T. C., Kazaoka, R. M. A., Cussiol, J. R. R., Netto, L. E. S., et al. (2012). Characterization of changes in the apo form of enzyme Cu, Zn superoxide dismutase promoted by docosahexaenoic acid and their hydroperoxides. Free Radical Biology & Medicine. New York: Instituto de Biociências, Universidade de São Paulo. -
NLM
Appolinário PP, Medinas DB, Genaro-Mattos TC, Kazaoka RMA, Cussiol JRR, Netto LES, Augusto O, Miyamoto S. Characterization of changes in the apo form of enzyme Cu, Zn superoxide dismutase promoted by docosahexaenoic acid and their hydroperoxides. Free Radical Biology & Medicine. 2012 ; 53 S133 res. 322.[citado 2025 dez. 27 ] -
Vancouver
Appolinário PP, Medinas DB, Genaro-Mattos TC, Kazaoka RMA, Cussiol JRR, Netto LES, Augusto O, Miyamoto S. Characterization of changes in the apo form of enzyme Cu, Zn superoxide dismutase promoted by docosahexaenoic acid and their hydroperoxides. Free Radical Biology & Medicine. 2012 ; 53 S133 res. 322.[citado 2025 dez. 27 ] - Oligomerization of Cu,Zn-superoxide dismutase (SOD1) by docosahexaenoic acid and its hydroperoxides in vitro: aggregation dependence on fatty acid unsaturation and thiols
- The role of cysteine residues on sod1 oligomerization induced by docosahexaenoic acid
- Peroxiredoxin S-nitrosation and high molecular weight DNIC formation
- Superoxide dismutase 1-mediated production of ethanol- and DNA-derived radicals in yeasts challenged with hydrogen peroxide: molecular insights into genome instability of peroxiredoxin-null strains
- Increased radical production in Saccharomyces cerevisiae Tsa1/Tsa2-Null cultures challenged with hydrogen peroxide is likely to be mediated by SOD1
- Peroxiredoxin 1 coordination to the dinitrosyl iron complex of glutathione
- Cytochrome c reacts with cholesterol hydroperoxides producing protein and lipid carbon-centered radicals
- SOD1 aggregation induced by docosahexaenoic acid and docosahexaenoic acid hydroperoxides
- Cholesterol aldehydes-induced aggregation of superoxide dismutase-1 (SOD1)
- Docosahexaenoic acid induced SOD1 aggregation: the role of fatty acid conformation and the cysteine residues
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