Biological characterization of the AhpR system from the phytopatogenic bacteria Xylella fastidiosa (2011)
- Autores:
- Autor USP: NETTO, LUIS EDUARDO SOARES - IB
- Unidade: IB
- Assuntos: ENZIMAS OXIRREDUTORAS; ANTIOXIDANTES
- Idioma: Inglês
- Imprenta:
- Local: Montevideo
- Data de publicação: 2011
- Fonte:
- Título do periódico: Abstracts
- Nome do evento: Symposium "Thiol metabolism and redox regulation of cellular functions"
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ABNT
PIMENTA, M. V et al. Biological characterization of the AhpR system from the phytopatogenic bacteria Xylella fastidiosa. 2011, Anais.. Montevideo: Instituto de Biociências, Universidade de São Paulo, 2011. . Acesso em: 24 abr. 2024. -
APA
Pimenta, M. V., Horta, B. B., Discola, K. F., & Netto, L. E. S. (2011). Biological characterization of the AhpR system from the phytopatogenic bacteria Xylella fastidiosa. In Abstracts. Montevideo: Instituto de Biociências, Universidade de São Paulo. -
NLM
Pimenta MV, Horta BB, Discola KF, Netto LES. Biological characterization of the AhpR system from the phytopatogenic bacteria Xylella fastidiosa. Abstracts. 2011 ;[citado 2024 abr. 24 ] -
Vancouver
Pimenta MV, Horta BB, Discola KF, Netto LES. Biological characterization of the AhpR system from the phytopatogenic bacteria Xylella fastidiosa. Abstracts. 2011 ;[citado 2024 abr. 24 ] - 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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