Crystallographic studies of cys-based proteins (2009)
- Authors:
- Autor USP: NETTO, LUIS EDUARDO SOARES - IB
- Unidade: IB
- Subjects: PROTEÍNAS; BIOLOGIA MOLECULAR
- Language: Inglês
- Imprenta:
- Source:
- Título: Resumo
- Conference titles: Reunião Anual de Usuários do Laboratório Nacional de Luz Síncroton
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ABNT
MONTEIRO, G. et al. Crystallographic studies of cys-based proteins. 2009, Anais.. Campinas: Instituto de Biociências, Universidade de São Paulo, 2009. . Acesso em: 10 out. 2024. -
APA
Monteiro, G., Horta, B. B., Nakamatsu, E. H., Discola, K. F., & Netto, L. E. S. (2009). Crystallographic studies of cys-based proteins. In Resumo. Campinas: Instituto de Biociências, Universidade de São Paulo. -
NLM
Monteiro G, Horta BB, Nakamatsu EH, Discola KF, Netto LES. Crystallographic studies of cys-based proteins. Resumo. 2009 ;[citado 2024 out. 10 ] -
Vancouver
Monteiro G, Horta BB, Nakamatsu EH, Discola KF, Netto LES. Crystallographic studies of cys-based proteins. Resumo. 2009 ;[citado 2024 out. 10 ] - Glutaredoxin 1 and glutaredoxin 2 from Saccharomyces cerevisiae have very distinct biochemical properties although they share 85% of amino acid sequence similarity
- Caracterização estrutural de proteínas envolvidas na resposta celular ao estresse oxidativo
- Yeast 20S proteasome glutathionylation and redox signaling
- A family of novel peroxidases, peroxiredoxins
- Regulation of mitochondrial thioredoxin peroxidase I expression by two different pathways: one dependent on cAMP and other on heme
- Cytosolic thioredoxin peroxidase I is essential for the antioxidant defense of yeast with dysfunctional mitochondria
- Selectively labeling the heterologous protein in Escherichia coli for NMR studies: a strategy to speed Up NMR spectroscopy
- Glucose repression of PRX1 expression is mediated by Tor1p and Ras2p through inhibition of Msn2/4p in Saccharomyces cerevisiae
- Catalases and thioredoxin peroxidase protect Saccharomyces cerevisiae against 'Ca POT.2+'-induced mitochondrial membrane permeabilization and cell death
- Uma chave para entrar na laranja
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