Horseradish peroxidase compound I as a tool to investigate reactive protein-cysteine residues: from quantification to kinetics (2011)
- Authors:
- USP affiliated authors: SOUZA, GISELE MONTEIRO DE - FCF ; TOLEDO JUNIOR, JOSÉ CARLOS - FFCLRP ; AUGUSTO, OHARA - IQ ; NETTO, LUIS EDUARDO SOARES - IB
- Unidades: FCF; FFCLRP; IQ; IB
- DOI: 10.1016/j.freeradbiomed.2011.02.020
- Subjects: PEROXIDASE; ESTRESSE OXIDATIVO
- Language: Inglês
- Imprenta:
- Source:
- Título: Free Radical Biology & Medicine
- ISSN: 0891-5849
- Volume/Número/Paginação/Ano: v. 50, n. 9, p. 1032-1038, 2011
- Status:
- Artigo possui versão em acesso aberto em repositório (Green Open Access)
- Versão do Documento:
- Versão submetida (Pré-print)
- Acessar versão aberta:
-
ABNT
TOLEDO JUNIOR, José Carlos et al. Horseradish peroxidase compound I as a tool to investigate reactive protein-cysteine residues: from quantification to kinetics. Free Radical Biology & Medicine, v. 50, n. 9, p. 1032-1038, 2011Tradução . . Disponível em: https://doi.org/10.1016/j.freeradbiomed.2011.02.020. Acesso em: 01 abr. 2026. -
APA
Toledo Junior, J. C., Audi, R., Ogusucu, R., Monteiro, G., Netto, L. E. S., & Augusto, O. (2011). Horseradish peroxidase compound I as a tool to investigate reactive protein-cysteine residues: from quantification to kinetics. Free Radical Biology & Medicine, 50( 9), 1032-1038. doi:10.1016/j.freeradbiomed.2011.02.020 -
NLM
Toledo Junior JC, Audi R, Ogusucu R, Monteiro G, Netto LES, Augusto O. Horseradish peroxidase compound I as a tool to investigate reactive protein-cysteine residues: from quantification to kinetics [Internet]. Free Radical Biology & Medicine. 2011 ; 50( 9): 1032-1038.[citado 2026 abr. 01 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2011.02.020 -
Vancouver
Toledo Junior JC, Audi R, Ogusucu R, Monteiro G, Netto LES, Augusto O. Horseradish peroxidase compound I as a tool to investigate reactive protein-cysteine residues: from quantification to kinetics [Internet]. Free Radical Biology & Medicine. 2011 ; 50( 9): 1032-1038.[citado 2026 abr. 01 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2011.02.020 - Catalytic Thr or ser residue modulates structural switches in 2-Cys peroxiredoxin by distinct mechanisms
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- The use of Tsa1 protein mutants to investigate substrate binding on peroxiredoxins
- YMR134W is an essential orf involved in iron homeotase in Saccharomyces cerevisiae
- Characterization of YCL047C, a putative phosphocholine cytidylytransferase involved in lipid reposition during oxidative stress in Saccharomyces cerevisiae
- Structural and functional characterization of the amino acids involved in 1-cys peroxiredoxins ascorbate-peroxidatic activity
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