Responses of yeast and bacteria to oxidative stress induced by peroxides (2004)
- Autor:
- Autor USP: SOARES NETTO, LUIS EDUARDO - IB
- Unidade: IB
- Subjects: CÉLULAS; MITOCÔNDRIAS; PEROXIDASE; ENZIMAS OXIRREDUTORAS
- Language: Inglês
- Imprenta:
- Source:
- Título: Simpósio
- Conference titles: Reunião Anual da Sociedade Brasileira de Bioquímica e Biologia Molecular
-
ABNT
NETTO, Luis Eduardo Soares. Responses of yeast and bacteria to oxidative stress induced by peroxides. 2004, Anais.. Caxambu: Instituto de Biociências, Universidade de São Paulo, 2004. . Acesso em: 23 jan. 2026. -
APA
Netto, L. E. S. (2004). Responses of yeast and bacteria to oxidative stress induced by peroxides. In Simpósio. Caxambu: Instituto de Biociências, Universidade de São Paulo. -
NLM
Netto LES. Responses of yeast and bacteria to oxidative stress induced by peroxides. Simpósio. 2004 ;[citado 2026 jan. 23 ] -
Vancouver
Netto LES. Responses of yeast and bacteria to oxidative stress induced by peroxides. Simpósio. 2004 ;[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
- Biological characterization of the AhpR system from the phytopatogenic bacteria Xylella fastidiosa
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