Peroxiredoxin S-nitrosation and high molecular weight DNIC formation (2015)
- Autores:
- Autores USP: NETTO, LUIS EDUARDO SOARES - IB ; AUGUSTO, OHARA - IQ
- Unidades: IB; IQ
- DOI: 10.1016/j.freeradbiomed.2015.10.214
- Assuntos: PEROXIDASE; BIOQUÍMICA
- Idioma: Inglês
- Imprenta:
- Fonte:
- Título do periódico: Free Radical Biology & Medicine
- ISSN: 0891-5849
- Volume/Número/Paginação/Ano: v. 87, suppl. 1, p. S81 res. 172, 2015
- Nome do evento: Annual Meeting of the Society for Free Radical Biology and Medicine (SFRBM)
- Este periódico é de assinatura
- Este artigo NÃO é de acesso aberto
- Cor do Acesso Aberto: closed
-
ABNT
TRUZZI, Daniela Ramos et al. Peroxiredoxin S-nitrosation and high molecular weight DNIC formation. Free Radical Biology & Medicine. New York: Instituto de Biociências, Universidade de São Paulo. Disponível em: https://doi.org/10.1016/j.freeradbiomed.2015.10.214. Acesso em: 23 abr. 2024. , 2015 -
APA
Truzzi, D. R., Alves, S. S. V., Netto, L. E. S., & Augusto, O. (2015). Peroxiredoxin S-nitrosation and high molecular weight DNIC formation. Free Radical Biology & Medicine. New York: Instituto de Biociências, Universidade de São Paulo. doi:10.1016/j.freeradbiomed.2015.10.214 -
NLM
Truzzi DR, Alves SSV, Netto LES, Augusto O. Peroxiredoxin S-nitrosation and high molecular weight DNIC formation [Internet]. Free Radical Biology & Medicine. 2015 ; 87 S81 res. 172.[citado 2024 abr. 23 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2015.10.214 -
Vancouver
Truzzi DR, Alves SSV, Netto LES, Augusto O. Peroxiredoxin S-nitrosation and high molecular weight DNIC formation [Internet]. Free Radical Biology & Medicine. 2015 ; 87 S81 res. 172.[citado 2024 abr. 23 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2015.10.214 - 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
- Reactions of yeast thioredoxin peroxidases I and II with hydrogen peroxide and peroxynitrite: rate constants by competitive kinetics
- Determination of yeast cytosolic peroxiredoxin reduction rates by thioredoxins and PRX overoxidation through fluorescence approaches
- Peroxiredoxin 1 coordination to dinitrosyl iron complex
- Reduction of 1-CYS peroxiredoxins by ascorbate changes the thiol-specific antioxidant paradigm, revealing a new antioxidant function of vitamin C
- Selective quantification of peroxidatic thiol of peroxiredoxins
- Reactions of yeast cytosolic thioredoxin peroxidase I and II with hydrogen peroxide and peroxynitrine: Kinetics and inhibition of radical production in cultures
- Reaction of yeast thioredoxin peroxidase I and II with hydrogen peroxide and peroxynitrite: rate constants by competitive kinetics
Informações sobre o DOI: 10.1016/j.freeradbiomed.2015.10.214 (Fonte: oaDOI API)
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