Cysteine-based peroxidases: change of thiol specific paradigm and characterization of a novel family (2007)
- Autor:
- Autor USP: NETTO, LUIS EDUARDO SOARES - IB
- Unidade: IB
- Subjects: PEROXIDASE; ESTRESSE OXIDATIVO
- Language: Inglês
- Imprenta:
- Source:
- Título do periódico: Abstract
- Conference titles: Latin American Protein Society Meeting
-
ABNT
NETTO, Luis Eduardo Soares. Cysteine-based peroxidases: change of thiol specific paradigm and characterization of a novel family. 2007, Anais.. Acapulco: Instituto de Biociências, Universidade de São Paulo, 2007. . Acesso em: 21 maio 2024. -
APA
Netto, L. E. S. (2007). Cysteine-based peroxidases: change of thiol specific paradigm and characterization of a novel family. In Abstract. Acapulco: Instituto de Biociências, Universidade de São Paulo. -
NLM
Netto LES. Cysteine-based peroxidases: change of thiol specific paradigm and characterization of a novel family. Abstract. 2007 ;[citado 2024 maio 21 ] -
Vancouver
Netto LES. Cysteine-based peroxidases: change of thiol specific paradigm and characterization of a novel family. Abstract. 2007 ;[citado 2024 maio 21 ] - 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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