Peroxiredoxin Qβ is a bacterial Cys-based peroxidase that presents unique structural redox rearrangements and is highly reactive towards hydrogen peroxide and peroxynitrite (2010)
- Authors:
- Autor USP: NETTO, LUIS EDUARDO SOARES - IB
- Unidade: IB
- DOI: 10.1016/j.freeradbiomed.2010.10.554
- Assunto: PEROXIDASE
- Language: Inglês
- Imprenta:
- Publisher place: Philadelphia
- Date published: 2010
- Source:
- Título: Free Radical Biology and Medicine
- Volume/Número/Paginação/Ano: v. 49, suppl. 1, p. S192, abst. 541, 2010
- Conference titles: Annual Meeting of the Society for Free Radical Biology and Medicine
- Este periódico é de acesso aberto
- Este artigo NÃO é de acesso aberto
-
ABNT
HORTA, Bruno Brasil et al. Peroxiredoxin Qβ is a bacterial Cys-based peroxidase that presents unique structural redox rearrangements and is highly reactive towards hydrogen peroxide and peroxynitrite. Free Radical Biology and Medicine. Philadelphia: Instituto de Biociências, Universidade de São Paulo. Disponível em: https://doi.org/10.1016/j.freeradbiomed.2010.10.554. Acesso em: 24 jan. 2026. , 2010 -
APA
Horta, B. B., Oliveira, M. A., Discola, K. F., Cussiol, J. R. R., & Netto, L. E. S. (2010). Peroxiredoxin Qβ is a bacterial Cys-based peroxidase that presents unique structural redox rearrangements and is highly reactive towards hydrogen peroxide and peroxynitrite. Free Radical Biology and Medicine. Philadelphia: Instituto de Biociências, Universidade de São Paulo. doi:10.1016/j.freeradbiomed.2010.10.554 -
NLM
Horta BB, Oliveira MA, Discola KF, Cussiol JRR, Netto LES. Peroxiredoxin Qβ is a bacterial Cys-based peroxidase that presents unique structural redox rearrangements and is highly reactive towards hydrogen peroxide and peroxynitrite [Internet]. Free Radical Biology and Medicine. 2010 ; 49 S192.[citado 2026 jan. 24 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2010.10.554 -
Vancouver
Horta BB, Oliveira MA, Discola KF, Cussiol JRR, Netto LES. Peroxiredoxin Qβ is a bacterial Cys-based peroxidase that presents unique structural redox rearrangements and is highly reactive towards hydrogen peroxide and peroxynitrite [Internet]. Free Radical Biology and Medicine. 2010 ; 49 S192.[citado 2026 jan. 24 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2010.10.554 - Ohr (organic hydroperoxide resistance protein) possesses a previously undescribed activity, lipoyl-dependent peroxidase
- Investigating the redox structural transitions of Saccharomyces cereviseae Tsa1p
- Cloning, purification and enzymatic activities of Xylella fastidiosa alkyl hydroperoxidase system
- Lipoamide from metabolic enzymes is probable the reducing system of organic hydroperoxide resistance protein
- Structural and functional analysis of yeast thioredoxin system reveals structural elements of substrate specificity
- Structural aspects of the distinct biochemical properties of Glutaredoxin 1 and Glutaredoxin 2 from Saccharomyces cerevisiae
- Structural aspects of the distinct biochemical properties of Glutaredoxin 1 and Glutaredoxin 2 from Saccharomyces cerevisiae
- Role of glutaredoxin 2 and cytosolic thioredoxins in cysteinyl-based redox modification of the 20S proteasome
- Biological characterization of the AhpR system from the phytopatogenic bacteria Xylella fastidiosa
- Antioxidant defenses of the peroxisome in Saccharomyces cerevisiae
Informações sobre o DOI: 10.1016/j.freeradbiomed.2010.10.554 (Fonte: oaDOI API)
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