Antioxidant defenses of the peroxisome in Saccharomyces cerevisiae (2011)
- Authors:
- Autor USP: NETTO, LUIS EDUARDO SOARES - IB
- Unidade: IB
- Subjects: ANTIOXIDANTES; PEROXIDASE; SACCHAROMYCES
- Language: Inglês
- Imprenta:
- Publisher place: Montevideo
- Date published: 2011
- Source:
- Título do periódico: Abstracts
- Conference titles: Symposium "Thiol metabolism and redox regulation of cellular functions"
-
ABNT
REYDON, Aline F C e NETTO, Luis Eduardo Soares. Antioxidant defenses of the peroxisome in Saccharomyces cerevisiae. 2011, Anais.. Montevideo: Instituto de Biociências, Universidade de São Paulo, 2011. . Acesso em: 19 jul. 2024. -
APA
Reydon, A. F. C., & Netto, L. E. S. (2011). Antioxidant defenses of the peroxisome in Saccharomyces cerevisiae. In Abstracts. Montevideo: Instituto de Biociências, Universidade de São Paulo. -
NLM
Reydon AFC, Netto LES. Antioxidant defenses of the peroxisome in Saccharomyces cerevisiae. Abstracts. 2011 ;[citado 2024 jul. 19 ] -
Vancouver
Reydon AFC, Netto LES. Antioxidant defenses of the peroxisome in Saccharomyces cerevisiae. Abstracts. 2011 ;[citado 2024 jul. 19 ] - The involvement of 8-oxoguanine repair in the adaptive response of yeast to oxidative stress
- Clonagem, expressão e estudos estruturais de tioredoxina redutase I de Saccharomyces cerevisiae
- 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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