Presence of Ser instead of thr in the catalytic triad of typical 2-Cys Prx increases their resistance to hyperoxidation and inactivation (2020)
- Authors:
- Autor USP: AUGUSTO, OHARA - IQ
- Unidade: IQ
- DOI: 10.1016/j.freeradbiomed.2020.10.099
- Subjects: PEROXIDASE; ENZIMAS
- Agências de fomento:
- Language: Inglês
- Imprenta:
- Source:
- Título: Free Radical Biology and Medicine
- ISSN: 0891-5849
- Volume/Número/Paginação/Ano: v. 159, Suppl. 1, p. S34, 2020
- Conference titles: SfRBM Annual Conference (Presented Virtually)
- Este periódico é de acesso aberto
- Este artigo NÃO é de acesso aberto
-
ABNT
SANTOS, Melina et al. Presence of Ser instead of thr in the catalytic triad of typical 2-Cys Prx increases their resistance to hyperoxidation and inactivation. Free Radical Biology and Medicine. New York: Instituto de Química, Universidade de São Paulo. Disponível em: https://doi.org/10.1016/j.freeradbiomed.2020.10.099. Acesso em: 28 fev. 2026. , 2020 -
APA
Santos, M., Breyer, C., Tairum, C., Oliveira, A. L. P. de, Montanhero, V. I., Silva, G. T., et al. (2020). Presence of Ser instead of thr in the catalytic triad of typical 2-Cys Prx increases their resistance to hyperoxidation and inactivation. Free Radical Biology and Medicine. New York: Instituto de Química, Universidade de São Paulo. doi:10.1016/j.freeradbiomed.2020.10.099 -
NLM
Santos M, Breyer C, Tairum C, Oliveira ALP de, Montanhero VI, Silva GT, Mori GM, Toyama MH, Augusto O, Netto LES, Oliveira M. Presence of Ser instead of thr in the catalytic triad of typical 2-Cys Prx increases their resistance to hyperoxidation and inactivation [Internet]. Free Radical Biology and Medicine. 2020 ; 159 S34.[citado 2026 fev. 28 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2020.10.099 -
Vancouver
Santos M, Breyer C, Tairum C, Oliveira ALP de, Montanhero VI, Silva GT, Mori GM, Toyama MH, Augusto O, Netto LES, Oliveira M. Presence of Ser instead of thr in the catalytic triad of typical 2-Cys Prx increases their resistance to hyperoxidation and inactivation [Internet]. Free Radical Biology and Medicine. 2020 ; 159 S34.[citado 2026 fev. 28 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2020.10.099 - Accumulating evidence on the contribution of free radicals in protein aggregation
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- Peroxynitrite-mediated free radical formation in human plasma detected by epr
- Peroxynitrite preferentially oxidizes the dithiol redox motifs of protein disulfide isomerase
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Informações sobre o DOI: 10.1016/j.freeradbiomed.2020.10.099 (Fonte: oaDOI API)
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