New possibilities to study the interaction between cTPxl and Trxl C33S: stable ptotein complexes linked by mixed disulfide (2010)
- Authors:
- Autor USP: NETTO, LUIS EDUARDO SOARES - IB
- Unidade: IB
- Assunto: PROTEÍNAS (INTERAÇÃO)
- Language: Inglês
- Imprenta:
- Source:
- Título do periódico: Abstracts
- Conference titles: Annual Meeting of Brazilian Biochemistry and Molecular Biology (SBBq)
-
ABNT
KIDO, L. Y e NETTO, Luis Eduardo Soares e OLIVEIRA, M. A. New possibilities to study the interaction between cTPxl and Trxl C33S: stable ptotein complexes linked by mixed disulfide. 2010, Anais.. São Paulo: SBBq, 2010. . Acesso em: 19 abr. 2024. -
APA
Kido, L. Y., Netto, L. E. S., & Oliveira, M. A. (2010). New possibilities to study the interaction between cTPxl and Trxl C33S: stable ptotein complexes linked by mixed disulfide. In Abstracts. São Paulo: SBBq. -
NLM
Kido LY, Netto LES, Oliveira MA. New possibilities to study the interaction between cTPxl and Trxl C33S: stable ptotein complexes linked by mixed disulfide. Abstracts. 2010 ;[citado 2024 abr. 19 ] -
Vancouver
Kido LY, Netto LES, Oliveira MA. New possibilities to study the interaction between cTPxl and Trxl C33S: stable ptotein complexes linked by mixed disulfide. Abstracts. 2010 ;[citado 2024 abr. 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
How to cite
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
