Peroxiredoxin: structure, function and regulation of gene expression (2006)
- Authors:
- USP affiliated authors: NETTO, LUIS EDUARDO SOARES - IB
- Unidades: IB
- Subjects: PEROXIDASE; EXPRESSÃO GÊNICA
- Language: Inglês
- Imprenta:
- Place of publication: Águas de Lindóia
- Date published: 2006
- Source:
- Título do periódico: Resumo da palestra
- Conference title: Reunião Anual da Sociedade Brasileira de Bioquímica e Biologia Molecular
-
ABNT
NETTO, Luis Eduardo Soares; MONTEIRO, G.; GENU, Victor; et al. Peroxiredoxin: structure, function and regulation of gene expression. Anais.. Águas de Lindóia: [s.n.], 2006. -
APA
Netto, L. E. S., Monteiro, G., Genu, V., Cogueto, C. V., Demasi, A. P. D., Oliveira, M. A., & Munhoz, D. C. (2006). Peroxiredoxin: structure, function and regulation of gene expression. In Resumo da palestra. Águas de Lindóia. -
NLM
Netto LES, Monteiro G, Genu V, Cogueto CV, Demasi APD, Oliveira MA, Munhoz DC. Peroxiredoxin: structure, function and regulation of gene expression. Resumo da palestra. 2006 ; -
Vancouver
Netto LES, Monteiro G, Genu V, Cogueto CV, Demasi APD, Oliveira MA, Munhoz DC. Peroxiredoxin: structure, function and regulation of gene expression. Resumo da palestra. 2006 ; - Site-directed mutagenesis as a tool to characterize specificity in thiol-based redox interactions between proteins and substrates
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- Regulation of genes encoding organic hydroperoxide resistance (Ohr) proteins in Chromobacterium violaceum
- The involvement of 8-oxoguanine repair in the adaptive response of yeast to oxidative stress
- 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
- Glutaredoxin 2 dethiolic activity upon the S-Glutathionylated 20S proteasome
- Conformational changes between reduced and oxidized states of the reductase thioredoxin (TrxR1) from Saccharomices cerevisae: insights in Thioredoxin system evolution
- Mithochondrial thioredoxin peroxidase is reduced by ascorbate
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