Peroxynitrite preferentially oxidizes the dithiol redox motifs of protein disulfide isomerase (2018)
- Authors:
- Autor USP: AUGUSTO, OHARA - IQ
- Unidade: IQ
- DOI: 10.1074/jbc.M117.807016
- Subjects: PERÓXIDO DE HIDROGÊNIO; CINÉTICA
- Language: Inglês
- Imprenta:
- Source:
- Título: Journal of Biological Chemistry
- ISSN: 0021-9258
- Volume/Número/Paginação/Ano: v. 293, n. 4, p. 1450-1465, 2018
- Status:
- Artigo aberto em periódico híbrido (Hybrid Open Access)
- Versão do Documento:
- Versão publicada (Published version)
- Acessar versão aberta:
-
ABNT
PEIXOTO, Álbert Souza et al. Peroxynitrite preferentially oxidizes the dithiol redox motifs of protein disulfide isomerase. Journal of Biological Chemistry, v. 293, n. 4, p. 1450-1465, 2018Tradução . . Disponível em: http://www.jbc.org/content/early/2017/11/30/jbc.M117.807016. Acesso em: 01 abr. 2026. -
APA
Peixoto, Á. S., Geyer, R. R., Iqbal, A., Truzzi, D. R., Moretti, A. I. S., Laurindo, F. R. M., & Augusto, O. (2018). Peroxynitrite preferentially oxidizes the dithiol redox motifs of protein disulfide isomerase. Journal of Biological Chemistry, 293( 4), 1450-1465. doi:10.1074/jbc.M117.807016 -
NLM
Peixoto ÁS, Geyer RR, Iqbal A, Truzzi DR, Moretti AIS, Laurindo FRM, Augusto O. Peroxynitrite preferentially oxidizes the dithiol redox motifs of protein disulfide isomerase [Internet]. Journal of Biological Chemistry. 2018 ; 293( 4): 1450-1465.[citado 2026 abr. 01 ] Available from: http://www.jbc.org/content/early/2017/11/30/jbc.M117.807016 -
Vancouver
Peixoto ÁS, Geyer RR, Iqbal A, Truzzi DR, Moretti AIS, Laurindo FRM, Augusto O. Peroxynitrite preferentially oxidizes the dithiol redox motifs of protein disulfide isomerase [Internet]. Journal of Biological Chemistry. 2018 ; 293( 4): 1450-1465.[citado 2026 abr. 01 ] Available from: http://www.jbc.org/content/early/2017/11/30/jbc.M117.807016 - Accumulating evidence on the contribution of free radicals in protein aggregation
- Inactivation and aggregation of protein disulfide isomerase by enzymatically and photolytically generated carbonate radical
- Spin trapping of glutathiyl and protein radicals produced from nitric oxide-derived oxidants
- Oxidants derived from the bicarbonate buffer ('HCO IND. 3'/'CO IND. 2')
- Reaction of human hemoglobin with peroxynitrite Isomerization to nitrate and secondary formation of protein radicals
- Peroxynitrite-mediated free radical formation in human plasma detected by epr
- Ditryptophan cross-links are detected in bovine beta crystallin irradiated with a solar simulator and in human lenses with advanced cataract
- Effects of some soybean flavonoids and aglycone-rich extracts in nitric oxide homeostasis
- Dna methylation by ter-butylhydroperoxide / iron ii
- Tempol reduces inflammation and oxidative damage in cigarette smoke-exposed mice by decreasing neutrophil infiltration and activating the Nrf2 pathway
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