Proteasome redox modulation through S-glutatiolation increases proteolysis rates and modifies protein fragmentation (2011)
- Authors:
- USP affiliated author: NETTO, LUIS EDUARDO SOARES - IB
- School: IB
- Subjects: PROTEÍNAS; ENZIMAS; BIOQUÍMICA
- Language: Inglês
- Imprenta:
- Source:
- Título do periódico: Program Book Proceedings
- Conference title: São Paulo Advanced School on Redox Processes in Biomedicine
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ABNT
SIMOES, V. et al. Proteasome redox modulation through S-glutatiolation increases proteolysis rates and modifies protein fragmentation. 2011, Anais.. São Pedro: Instituto de Biociências, Universidade de São Paulo, 2011. . Acesso em: 09 ago. 2022. -
APA
Simoes, V., Silva, G. M., Netto, L. E. S., & Demasi, M. (2011). Proteasome redox modulation through S-glutatiolation increases proteolysis rates and modifies protein fragmentation. In Program Book Proceedings. São Pedro: Instituto de Biociências, Universidade de São Paulo. -
NLM
Simoes V, Silva GM, Netto LES, Demasi M. Proteasome redox modulation through S-glutatiolation increases proteolysis rates and modifies protein fragmentation. Program Book Proceedings. 2011 ;[citado 2022 ago. 09 ] -
Vancouver
Simoes V, Silva GM, Netto LES, Demasi M. Proteasome redox modulation through S-glutatiolation increases proteolysis rates and modifies protein fragmentation. Program Book Proceedings. 2011 ;[citado 2022 ago. 09 ] - Cytosolic thioredoxin peroxidase II is an important defense of yeast against organic peroxide insult independently of mitochondrial activity
- Clonagem, expressão e estudos estruturais de tioredoxina redutase I de Saccharomyces cerevisiae
- Mithochondrial thioredoxin peroxidase is reduced by ascorbate
- 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
- S-Glutathionylation of the 20S proteasome increases degradation of oxidized proteins in the yeast Saccharomyces cerevisiae
- Structural characterization of the thioredoxin-thioredoxin reductase citoplasmic complexes from Saccharomyces cerevisiae
- Caracterização funcional do sistema antioxidante AhpR de Xylella fastidiosa
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