Glutaredoxin 2 dethiolic activity upon the S-Glutathionylated 20S proteasome (2007)
- Authors:
- Autor USP: NETTO, LUIS EDUARDO SOARES - IB
- Unidade: IB
- Subjects: ANTIOXIDANTES; BIOQUÍMICA CELULAR
- Language: Inglês
- Imprenta:
- Source:
- Título do periódico: Abstract
- Conference titles: Annual Meeting of the Brazilian Society for Biochemistry and Molecular Biology - SBBq
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ABNT
SILVA, Gustavo M. et al. Glutaredoxin 2 dethiolic activity upon the S-Glutathionylated 20S proteasome. 2007, Anais.. Salvador: Instituto de Biociências, Universidade de São Paulo, 2007. . Acesso em: 29 mar. 2024. -
APA
Silva, G. M., Netto, L. E. S., Piassa, G. M., Pimenta, D. C., & Demasi, M. (2007). Glutaredoxin 2 dethiolic activity upon the S-Glutathionylated 20S proteasome. In Abstract. Salvador: Instituto de Biociências, Universidade de São Paulo. -
NLM
Silva GM, Netto LES, Piassa GM, Pimenta DC, Demasi M. Glutaredoxin 2 dethiolic activity upon the S-Glutathionylated 20S proteasome. Abstract. 2007 ;[citado 2024 mar. 29 ] -
Vancouver
Silva GM, Netto LES, Piassa GM, Pimenta DC, Demasi M. Glutaredoxin 2 dethiolic activity upon the S-Glutathionylated 20S proteasome. Abstract. 2007 ;[citado 2024 mar. 29 ] - The involvement of 8-oxoguanine repair in the adaptive response of yeast to oxidative stress
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- 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
- S-Glutathionylation of the 20S proteasome increases degradation of oxidized proteins in the yeast Saccharomyces cerevisiae
- Conformational changes between reduced and oxidized states of the reductase thioredoxin (TrxR1) from Saccharomices cerevisae: insights in Thioredoxin system evolution
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