Filtros : "Oliveira, Marcos Antonio" Limpar

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  • Source: Abstracts. Conference titles: Annual Meeting of the Brazilian Society for Biochemistry and Molecular Biology/SBBq. Unidade: FCF

    Subjects: ESCHERICHIA COLI, FILOGENIA

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    • ABNT

      FERNANDES, Gabriella Costa et al. Expression of yeast Asp1 lacking N-terminal domain in strains of Escherichia coli. 2019, Anais.. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular/SBBq, 2019. Disponível em: http://www.sbbq.org.br/reuniao/2019/images/Livro_Resumos_2019.pdf. Acesso em: 05 out. 2024.
    • APA

      Fernandes, G. C., Silva, L. S. da, Pessoa Junior, A., Long, P., & Oliveira, M. A. (2019). Expression of yeast Asp1 lacking N-terminal domain in strains of Escherichia coli. In Abstracts. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular/SBBq. Recuperado de http://www.sbbq.org.br/reuniao/2019/images/Livro_Resumos_2019.pdf
    • NLM

      Fernandes GC, Silva LS da, Pessoa Junior A, Long P, Oliveira MA. Expression of yeast Asp1 lacking N-terminal domain in strains of Escherichia coli [Internet]. Abstracts. 2019 ;[citado 2024 out. 05 ] Available from: http://www.sbbq.org.br/reuniao/2019/images/Livro_Resumos_2019.pdf
    • Vancouver

      Fernandes GC, Silva LS da, Pessoa Junior A, Long P, Oliveira MA. Expression of yeast Asp1 lacking N-terminal domain in strains of Escherichia coli [Internet]. Abstracts. 2019 ;[citado 2024 out. 05 ] Available from: http://www.sbbq.org.br/reuniao/2019/images/Livro_Resumos_2019.pdf
  • Source: Directed mutageneis. Unidade: IB

    Subjects: PROTEÍNAS, ENZIMAS, ANTIOXIDANTES, METABOLISMO ENERGÉTICO, SACCHAROMYCES

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      NETTO, Luis Eduardo Soares e OLIVEIRA, Marcos Antonio. Site-directed mutagenesis as a tool to characterize specificity in thiol-based redox interactions between proteins and substrates. Directed mutageneis. Tradução . Columbia: InTech, 2013. . Disponível em: https://doi.org/10.5772/54183. Acesso em: 05 out. 2024.
    • APA

      Netto, L. E. S., & Oliveira, M. A. (2013). Site-directed mutagenesis as a tool to characterize specificity in thiol-based redox interactions between proteins and substrates. In Directed mutageneis. Columbia: InTech. doi:10.5772/54183
    • NLM

      Netto LES, Oliveira MA. Site-directed mutagenesis as a tool to characterize specificity in thiol-based redox interactions between proteins and substrates [Internet]. In: Directed mutageneis. Columbia: InTech; 2013. [citado 2024 out. 05 ] Available from: https://doi.org/10.5772/54183
    • Vancouver

      Netto LES, Oliveira MA. Site-directed mutagenesis as a tool to characterize specificity in thiol-based redox interactions between proteins and substrates [Internet]. In: Directed mutageneis. Columbia: InTech; 2013. [citado 2024 out. 05 ] Available from: https://doi.org/10.5772/54183
  • Source: Free Radical Biology and Medicine. Conference titles: Annual Meeting of the Society for Free Radical Biology and Medicine. Unidade: IB

    Assunto: PEROXIDASE

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      HORTA, Bruno Brasil et al. Peroxiredoxin Qβ is a bacterial Cys-based peroxidase that presents unique structural redox rearrangements and is highly reactive towards hydrogen peroxide and peroxynitrite. Free Radical Biology and Medicine. Philadelphia: Instituto de Biociências, Universidade de São Paulo. Disponível em: https://doi.org/10.1016/j.freeradbiomed.2010.10.554. Acesso em: 05 out. 2024. , 2010
    • APA

      Horta, B. B., Oliveira, M. A., Discola, K. F., Cussiol, J. R. R., & Netto, L. E. S. (2010). Peroxiredoxin Qβ is a bacterial Cys-based peroxidase that presents unique structural redox rearrangements and is highly reactive towards hydrogen peroxide and peroxynitrite. Free Radical Biology and Medicine. Philadelphia: Instituto de Biociências, Universidade de São Paulo. doi:10.1016/j.freeradbiomed.2010.10.554
    • NLM

      Horta BB, Oliveira MA, Discola KF, Cussiol JRR, Netto LES. Peroxiredoxin Qβ is a bacterial Cys-based peroxidase that presents unique structural redox rearrangements and is highly reactive towards hydrogen peroxide and peroxynitrite [Internet]. Free Radical Biology and Medicine. 2010 ; 49 S192.[citado 2024 out. 05 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2010.10.554
    • Vancouver

      Horta BB, Oliveira MA, Discola KF, Cussiol JRR, Netto LES. Peroxiredoxin Qβ is a bacterial Cys-based peroxidase that presents unique structural redox rearrangements and is highly reactive towards hydrogen peroxide and peroxynitrite [Internet]. Free Radical Biology and Medicine. 2010 ; 49 S192.[citado 2024 out. 05 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2010.10.554
  • Source: Journal of Molecular Biology. Unidade: IB

    Assunto: ENZIMAS OXIRREDUTORAS

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      DISCOLA, Karen Fulan et al. Structural aspects of the distinct biochemical properties of Glutaredoxin 1 and Glutaredoxin 2 from Saccharomyces cerevisiae. Journal of Molecular Biology, v. 385, n. 3, p. 889-901, 2009Tradução . . Disponível em: https://doi.org/10.1016/j.jmb.2008.10.055. Acesso em: 05 out. 2024.
    • APA

      Discola, K. F., Oliveira, M. A., Cussiol, J. R. R., Monteiro, G., Barcena, J. A., Porras, P., et al. (2009). Structural aspects of the distinct biochemical properties of Glutaredoxin 1 and Glutaredoxin 2 from Saccharomyces cerevisiae. Journal of Molecular Biology, 385( 3), 889-901. doi:10.1016/j.jmb.2008.10.055
    • NLM

      Discola KF, Oliveira MA, Cussiol JRR, Monteiro G, Barcena JA, Porras P, Padilla CA, Guimarães BG, Netto LES. Structural aspects of the distinct biochemical properties of Glutaredoxin 1 and Glutaredoxin 2 from Saccharomyces cerevisiae [Internet]. Journal of Molecular Biology. 2009 ; 385( 3): 889-901.[citado 2024 out. 05 ] Available from: https://doi.org/10.1016/j.jmb.2008.10.055
    • Vancouver

      Discola KF, Oliveira MA, Cussiol JRR, Monteiro G, Barcena JA, Porras P, Padilla CA, Guimarães BG, Netto LES. Structural aspects of the distinct biochemical properties of Glutaredoxin 1 and Glutaredoxin 2 from Saccharomyces cerevisiae [Internet]. Journal of Molecular Biology. 2009 ; 385( 3): 889-901.[citado 2024 out. 05 ] Available from: https://doi.org/10.1016/j.jmb.2008.10.055

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