S-Glutathionylation of the 20S proteasome increases degradation of oxidized proteins in the yeast Saccharomyces cerevisiae (2007)
- Authors:
- Autor USP: NETTO, LUIS EDUARDO SOARES - IB
- Unidade: IB
- Subjects: PROTEÍNAS; PEROXIDASE
- Language: Inglês
- Imprenta:
- Publisher place: Montevideo
- Date published: 2007
- Source:
- Título do periódico: Poster
- Conference titles: Free Radicals in Montevideo
-
ABNT
SILVA, G. M. e NETTO, Luis Eduardo Soares e DEMASI, M. S-Glutathionylation of the 20S proteasome increases degradation of oxidized proteins in the yeast Saccharomyces cerevisiae. 2007, Anais.. Montevideo: Instituto de Biociências, Universidade de São Paulo, 2007. . Acesso em: 30 jan. 2023. -
APA
Silva, G. M., Netto, L. E. S., & Demasi, M. (2007). S-Glutathionylation of the 20S proteasome increases degradation of oxidized proteins in the yeast Saccharomyces cerevisiae. In Poster. Montevideo: Instituto de Biociências, Universidade de São Paulo. -
NLM
Silva GM, Netto LES, Demasi M. S-Glutathionylation of the 20S proteasome increases degradation of oxidized proteins in the yeast Saccharomyces cerevisiae. Poster. 2007 ;[citado 2023 jan. 30 ] -
Vancouver
Silva GM, Netto LES, Demasi M. S-Glutathionylation of the 20S proteasome increases degradation of oxidized proteins in the yeast Saccharomyces cerevisiae. Poster. 2007 ;[citado 2023 jan. 30 ] - Cytosolic thioredoxin peroxidase II is an important defense of yeast against organic peroxide insult independently of mitochondrial activity
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- Peroxiredoxin: structure, function and regulation of gene expression
- Conformational changes between reduced and oxidized states of the reductase thioredoxin (TrxR1) from Saccharomices cerevisae: insights in Thioredoxin system evolution
- NMR solution structure of the reduced form of thioredoxin 1 from Sacharomyces cerevisiae
- Glutaredoxin 2 dethiolic activity upon the S-Glutathionylated 20S proteasome
- Structural characterization of the thioredoxin-thioredoxin reductase citoplasmic complexes from Saccharomyces cerevisiae
- Caracterização funcional do sistema antioxidante AhpR de Xylella fastidiosa
- New possibilities to study the interaction between cTPxl and Trxl C33S: stable ptotein complexes linked by mixed disulfide
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