Biological characterization of the AhpR system from the phytopatogenic bacteria Xylella fastidiosa (2011)
- Authors:
- Autor USP: NETTO, LUIS EDUARDO SOARES - IB
- Unidade: IB
- Subjects: ENZIMAS OXIRREDUTORAS; ANTIOXIDANTES
- Language: Inglês
- Imprenta:
- Publisher place: Montevideo
- Date published: 2011
- Source:
- Título: Abstracts
- Conference titles: 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: 23 jan. 2026. -
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 2026 jan. 23 ] -
Vancouver
Pimenta MV, Horta BB, Discola KF, Netto LES. Biological characterization of the AhpR system from the phytopatogenic bacteria Xylella fastidiosa. Abstracts. 2011 ;[citado 2026 jan. 23 ] - Ohr (organic hydroperoxide resistance protein) possesses a previously undescribed activity, lipoyl-dependent peroxidase
- Investigating the redox structural transitions of Saccharomyces cereviseae Tsa1p
- Peroxiredoxin Qβ is a bacterial Cys-based peroxidase that presents unique structural redox rearrangements and is highly reactive towards hydrogen peroxide and peroxynitrite
- Cloning, purification and enzymatic activities of Xylella fastidiosa alkyl hydroperoxidase system
- Lipoamide from metabolic enzymes is probable the reducing system of organic hydroperoxide resistance protein
- Structural and functional analysis of yeast thioredoxin system reveals structural elements of substrate specificity
- Structural aspects of the distinct biochemical properties of Glutaredoxin 1 and Glutaredoxin 2 from Saccharomyces cerevisiae
- Structural aspects of the distinct biochemical properties of Glutaredoxin 1 and Glutaredoxin 2 from Saccharomyces cerevisiae
- Role of glutaredoxin 2 and cytosolic thioredoxins in cysteinyl-based redox modification of the 20S proteasome
- Antioxidant defenses of the peroxisome in Saccharomyces cerevisiae
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