Structural and functional characterization of the amino acids involved in 1-cys peroxiredoxins ascorbate-peroxidatic activity (2010)
- Autores:
- Autores USP: SOUZA, GISELE MONTEIRO DE - FCF ; NETTO, LUIS EDUARDO SOARES - IB
- Unidades: FCF; IB
- Assuntos: ÁCIDO SULFÍNICO; ESTRESSE OXIDATIVO
- Idioma: Inglês
- Imprenta:
- Fonte:
- Título do periódico: Abstracts
- Nome do evento: Annual Meeting of Brazilian Biochemistry and Molecular Biology Society (SBBq)
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ABNT
CAVALCANTE, L. S e MONTEIRO, Gisele e NETTO, Luis Eduardo Soares. Structural and functional characterization of the amino acids involved in 1-cys peroxiredoxins ascorbate-peroxidatic activity. 2010, Anais.. São Paulo: SBBq, 2010. . Acesso em: 13 maio 2024. -
APA
Cavalcante, L. S., Monteiro, G., & Netto, L. E. S. (2010). Structural and functional characterization of the amino acids involved in 1-cys peroxiredoxins ascorbate-peroxidatic activity. In Abstracts. São Paulo: SBBq. -
NLM
Cavalcante LS, Monteiro G, Netto LES. Structural and functional characterization of the amino acids involved in 1-cys peroxiredoxins ascorbate-peroxidatic activity. Abstracts. 2010 ;[citado 2024 maio 13 ] -
Vancouver
Cavalcante LS, Monteiro G, Netto LES. Structural and functional characterization of the amino acids involved in 1-cys peroxiredoxins ascorbate-peroxidatic activity. Abstracts. 2010 ;[citado 2024 maio 13 ] - Characterization of YCL047C, a putative adenylyltransferase involved in the Saccharomyces cerevisiae oxidative stress response
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- Characterization of YCL047C, a putative phosphocholine cytidylytransferase involved in lipid reposition during oxidative stress in Saccharomyces cerevisiae
- YMR134W is an essential orf involved in iron homeotase in Saccharomyces cerevisiae
- Enzymatic and structural analysis of thioredoxin reductase 2 from Saccharomyces cerevisiae
- The essential gene YMR134W from saccharomyces cerevisiae is important for appropriate mitochondrial iron utilization and the ergosterol biosynthetic pathway
- The use of Tsa1 protein mutants to investigate substrate binding on peroxiredoxins
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