Structural and enzymatic studies of organic hydroperoxide resistance protein (2006)
- Authors:
- Autor USP: NETTO, LUIS EDUARDO SOARES - IB
- Unidade: IB
- Subjects: PROTEÍNAS; BIOQUÍMICA CELULAR
- Language: Inglês
- Imprenta:
- Publisher: SBBq
- Publisher place: Águas de Lindóia
- Date published: 2006
- Source:
- Título do periódico: Resumo
- Conference titles: Reunião Anual da Sociedade Brasileira de Bioquímica e Biologia Molecular
-
ABNT
CUSSIOL, José Renato Rosa et al. Structural and enzymatic studies of organic hydroperoxide resistance protein. 2006, Anais.. Águas de Lindóia: SBBq, 2006. . Acesso em: 19 abr. 2024. -
APA
Cussiol, J. R. R., Oliveira, M. A., Guimarães, B. G., Medrano, F. J., & Netto, L. E. S. (2006). Structural and enzymatic studies of organic hydroperoxide resistance protein. In Resumo. Águas de Lindóia: SBBq. -
NLM
Cussiol JRR, Oliveira MA, Guimarães BG, Medrano FJ, Netto LES. Structural and enzymatic studies of organic hydroperoxide resistance protein. Resumo. 2006 ;[citado 2024 abr. 19 ] -
Vancouver
Cussiol JRR, Oliveira MA, Guimarães BG, Medrano FJ, Netto LES. Structural and enzymatic studies of organic hydroperoxide resistance protein. Resumo. 2006 ;[citado 2024 abr. 19 ] - The involvement of 8-oxoguanine repair in the adaptive response of yeast to oxidative stress
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- Cytosolic thioredoxin peroxidase II is an important defense of yeast against organic peroxide insult independently of mitochondrial activity
- Mithochondrial thioredoxin peroxidase is reduced by ascorbate
- Peroxiredoxin: structure, function and regulation of gene expression
- Structural insights into enzyme-substrate interaction and characterization of enzymatic intermediates of organic hydroperoxide resistance protein from Xylella fastidiosa
- Papel da Tiorredoxina Peroxidase Ahp1 de S. cerevisiae na proteção contra dados oxidativos em células sem o gene da catalase peroxissomal (CTA1)
- NMR solution structure of the reduced form of thioredoxin 1 from Sacharomyces cerevisiae
- Glutaredoxin 2 dethiolic activity upon the S-Glutathionylated 20S proteasome
- S-Glutathionylation of the 20S proteasome increases degradation of oxidized proteins in the yeast Saccharomyces cerevisiae
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