Fonte: Journal of Biological Chemistry. Unidade: IQ
Assuntos: SUPERÓXIDO DISMUTASE, PEROXIDASE, ENZIMAS
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COELHO, Fernando Rodrigues et al. Oxidation of the tryptophan 32 residue of human superoxide dismutase 1 caused by its bicarbonate-dependent peroxidase activity triggers the non-amyloid aggregation of the enzyme. Journal of Biological Chemistry, v. 289, n. 44, p. 30690-30701, 2014Tradução . . Disponível em: https://doi.org/10.1074/jbc.M114.586370. Acesso em: 26 ago. 2024.APA
Coelho, F. R., Iqbal, A., Linares, E., Silva, D. F., Lima, F. da S., Cuccovia, I. M., & Augusto, O. (2014). Oxidation of the tryptophan 32 residue of human superoxide dismutase 1 caused by its bicarbonate-dependent peroxidase activity triggers the non-amyloid aggregation of the enzyme. Journal of Biological Chemistry, 289( 44), 30690-30701. doi:10.1074/jbc.M114.586370NLM
Coelho FR, Iqbal A, Linares E, Silva DF, Lima F da S, Cuccovia IM, Augusto O. Oxidation of the tryptophan 32 residue of human superoxide dismutase 1 caused by its bicarbonate-dependent peroxidase activity triggers the non-amyloid aggregation of the enzyme [Internet]. Journal of Biological Chemistry. 2014 ; 289( 44): 30690-30701.[citado 2024 ago. 26 ] Available from: https://doi.org/10.1074/jbc.M114.586370Vancouver
Coelho FR, Iqbal A, Linares E, Silva DF, Lima F da S, Cuccovia IM, Augusto O. Oxidation of the tryptophan 32 residue of human superoxide dismutase 1 caused by its bicarbonate-dependent peroxidase activity triggers the non-amyloid aggregation of the enzyme [Internet]. Journal of Biological Chemistry. 2014 ; 289( 44): 30690-30701.[citado 2024 ago. 26 ] Available from: https://doi.org/10.1074/jbc.M114.586370