Mixed disulfide protein complexes between thioredoxin and peroxiredoxin (2011)
- Authors:
- USP affiliated author: NETTO, LUIS EDUARDO SOARES - IB
- School: IB
- Subjects: PROTEÍNAS; BIOLOGIA
- Language: Inglês
- Imprenta:
- Source:
- Título do periódico: Resumos de Trabalhos Científicos
- Conference title: Reunião Anual de Usuários do LNLS
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ABNT
KIDO, L. Y.; SANTOS, V. F.; OLIVEIRA, M. A.; NETTO, Luis Eduardo Soares. Mixed disulfide protein complexes between thioredoxin and peroxiredoxin. Anais.. Campinas: LNLS, 2011. -
APA
Kido, L. Y., Santos, V. F., Oliveira, M. A., & Netto, L. E. S. (2011). Mixed disulfide protein complexes between thioredoxin and peroxiredoxin. In Resumos de Trabalhos Científicos. Campinas: LNLS. -
NLM
Kido LY, Santos VF, Oliveira MA, Netto LES. Mixed disulfide protein complexes between thioredoxin and peroxiredoxin. Resumos de Trabalhos Científicos. 2011 ; -
Vancouver
Kido LY, Santos VF, Oliveira MA, Netto LES. Mixed disulfide protein complexes between thioredoxin and peroxiredoxin. Resumos de Trabalhos Científicos. 2011 ; - Caracterização genética e bioquímica de CP-PRXp, uma proteína antioxidante de Crinipellis perniciosa
- Structural characterization of proteins involved in the cellular response to oxidative stress
- Responses of yeast and bacteria to peroxide-induced stress
- Cytossolic Thioredoxin Peroxidase I from Saccharomyces cerevisiae possesses a second antioxidant mechanism that does not involve peroxide decomposition
- Structural and functional characterization of glutaredoxins from Saccharomyces cerevisiae
- Structural and enzymatic studies of organic hydroperoxide resistance protein
- 20S proteasome glutathionylation: implications upon site-specific activities and proteolysis
- 'ANTIND. 1 H', 'ANTIND.13 C' and 'ANTIND.15 N' resonance assignments for the reduced forms of thioredoxin 1 and 2 from S. cerevisiae. [Letter to the editor]
- Structural and functional characterization of organic hydroperoxide resistant protein (Ohr): Ohr/OsmC is a new class of antioxidant proteins
- Glutaredoxin 1 and glutaredoxin 2 from Saccharomyces cerevisiae have very distinct biochemical properties although they share 85% of amino acid sequence similarity
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