Structural characterization of proteins involved in the cellular response to oxidative stress (2004)
- Authors:
- Autor USP: SOARES NETTO, LUIS EDUARDO - IB
- Unidade: IB
- Subjects: PROTEÍNAS; ANTIOXIDANTES; PEROXIDASE
- Language: Inglês
- Imprenta:
- Source:
- Título do periódico: Poster
- Conference titles: Reunião Anual da Sociedade Brasileira de Bioquímica e Biologia Molecular
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ABNT
OLIVEIRA, M. A. et al. Structural characterization of proteins involved in the cellular response to oxidative stress. 2004, Anais.. Caxambu: Instituto de Biociências, Universidade de São Paulo, 2004. . Acesso em: 20 abr. 2024. -
APA
Oliveira, M. A., Guimarães, B. G. G., Medrano, F. J., Barbosa, J. A., Genu, V., Monteiro, G., et al. (2004). Structural characterization of proteins involved in the cellular response to oxidative stress. In Poster. Caxambu: Instituto de Biociências, Universidade de São Paulo. -
NLM
Oliveira MA, Guimarães BGG, Medrano FJ, Barbosa JA, Genu V, Monteiro G, Vidigal SA, Iscola K, Demasi AP, Cussiol JRR, Netto LES. Structural characterization of proteins involved in the cellular response to oxidative stress. Poster. 2004 ;[citado 2024 abr. 20 ] -
Vancouver
Oliveira MA, Guimarães BGG, Medrano FJ, Barbosa JA, Genu V, Monteiro G, Vidigal SA, Iscola K, Demasi AP, Cussiol JRR, Netto LES. Structural characterization of proteins involved in the cellular response to oxidative stress. Poster. 2004 ;[citado 2024 abr. 20 ] - The involvement of 8-oxoguanine repair in the adaptive response of yeast to oxidative stress
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- 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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