Filtros : "Gozzo, Fabio C." "ICB" Limpar

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  • Source: Journal of Proteome Research. Unidade: ICB

    Assunto: HISTOLOGIA

    Acesso à fonteDOIHow to cite
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    • ABNT

      FRICKER, Lloyd D. et al. Peptidomic analysis of HEK293T cells: effect of the proteasome inhibitor epoxomicin on intracellular peptides. Journal of Proteome Research, v. 11, n. 3, p. 1981-1990, 2012Tradução . . Disponível em: https://doi.org/10.1016/j.febslet.2012.07.002. Acesso em: 21 jun. 2024.
    • APA

      Fricker, L. D., Gelman, J. S., Castro, L. M. de, Gozzo, F. C., & Ferro, E. S. (2012). Peptidomic analysis of HEK293T cells: effect of the proteasome inhibitor epoxomicin on intracellular peptides. Journal of Proteome Research, 11( 3), 1981-1990. doi:10.1016/j.febslet.2012.07.002
    • NLM

      Fricker LD, Gelman JS, Castro LM de, Gozzo FC, Ferro ES. Peptidomic analysis of HEK293T cells: effect of the proteasome inhibitor epoxomicin on intracellular peptides [Internet]. Journal of Proteome Research. 2012 ; 11( 3): 1981-1990.[citado 2024 jun. 21 ] Available from: https://doi.org/10.1016/j.febslet.2012.07.002
    • Vancouver

      Fricker LD, Gelman JS, Castro LM de, Gozzo FC, Ferro ES. Peptidomic analysis of HEK293T cells: effect of the proteasome inhibitor epoxomicin on intracellular peptides [Internet]. Journal of Proteome Research. 2012 ; 11( 3): 1981-1990.[citado 2024 jun. 21 ] Available from: https://doi.org/10.1016/j.febslet.2012.07.002
  • Source: PLOS ONE. Unidades: ICB, IQ, FCF

    Assunto: HISTOLOGIA

    Acesso à fonteDOIHow to cite
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    • ABNT

      MALVEZZI, Alberto et al. The cysteine-rich protein thimet oligopeptidase as a model of the structural requirements for S-glutathiolation and oxidative oligomerization. PLOS ONE, v. 7, n. 6, p. 1-11, 2012Tradução . . Disponível em: https://doi.org/10.1371/journal.pone.0039408. Acesso em: 21 jun. 2024.
    • APA

      Malvezzi, A., Higa, P. M., Amaral, A. T. do, Silva, G. M., Gozzo, F. C., Ferro, E. S., et al. (2012). The cysteine-rich protein thimet oligopeptidase as a model of the structural requirements for S-glutathiolation and oxidative oligomerization. PLOS ONE, 7( 6), 1-11. doi:10.1371/journal.pone.0039408
    • NLM

      Malvezzi A, Higa PM, Amaral AT do, Silva GM, Gozzo FC, Ferro ES, Castro LM de, Rezende L de, Monteiro G, Demasi M, Turaça LT. The cysteine-rich protein thimet oligopeptidase as a model of the structural requirements for S-glutathiolation and oxidative oligomerization [Internet]. PLOS ONE. 2012 ; 7( 6): 1-11.[citado 2024 jun. 21 ] Available from: https://doi.org/10.1371/journal.pone.0039408
    • Vancouver

      Malvezzi A, Higa PM, Amaral AT do, Silva GM, Gozzo FC, Ferro ES, Castro LM de, Rezende L de, Monteiro G, Demasi M, Turaça LT. The cysteine-rich protein thimet oligopeptidase as a model of the structural requirements for S-glutathiolation and oxidative oligomerization [Internet]. PLOS ONE. 2012 ; 7( 6): 1-11.[citado 2024 jun. 21 ] Available from: https://doi.org/10.1371/journal.pone.0039408
  • Source: FEBS Letters. Unidade: ICB

    Assunto: HISTOLOGIA

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    • ABNT

      RUSSO, Lilian C. et al. Inhibition of thimet oligopeptidase by siRNA alters specific intracellular peptides and potentiates isoproterenol signal transduction. FEBS Letters, v. 586, n. 19, p. 3287-3292, 2012Tradução . . Disponível em: https://doi.org/10.1016/j.febslet.2012.07.002. Acesso em: 21 jun. 2024.
    • APA

      Russo, L. C., Castro, L. M. de, Gozzo, F. C., & Ferro, E. S. (2012). Inhibition of thimet oligopeptidase by siRNA alters specific intracellular peptides and potentiates isoproterenol signal transduction. FEBS Letters, 586( 19), 3287-3292. doi:10.1016/j.febslet.2012.07.002
    • NLM

      Russo LC, Castro LM de, Gozzo FC, Ferro ES. Inhibition of thimet oligopeptidase by siRNA alters specific intracellular peptides and potentiates isoproterenol signal transduction [Internet]. FEBS Letters. 2012 ; 586( 19): 3287-3292.[citado 2024 jun. 21 ] Available from: https://doi.org/10.1016/j.febslet.2012.07.002
    • Vancouver

      Russo LC, Castro LM de, Gozzo FC, Ferro ES. Inhibition of thimet oligopeptidase by siRNA alters specific intracellular peptides and potentiates isoproterenol signal transduction [Internet]. FEBS Letters. 2012 ; 586( 19): 3287-3292.[citado 2024 jun. 21 ] Available from: https://doi.org/10.1016/j.febslet.2012.07.002
  • Source: Biochemical Journal. Unidades: ICB, IQ

    Assunto: PARASITOLOGIA

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    • ABNT

      TONHOSOLO, Renata et al. Identification, molecular cloning and functional characterization of an octaprenyl pyrophosphate synthase in intra-erythrocytic stages of Plasmodium falciparum. Biochemical Journal, v. 392, n. 1, p. 117-126, 2005Tradução . . Disponível em: https://doi.org/10.1042/bj20050441. Acesso em: 21 jun. 2024.
    • APA

      Tonhosolo, R., D'Alexandri, F. L., Genta, F. A., Wunderlich, G., Gozzo, F. C., Eberlin, M. N., et al. (2005). Identification, molecular cloning and functional characterization of an octaprenyl pyrophosphate synthase in intra-erythrocytic stages of Plasmodium falciparum. Biochemical Journal, 392( 1), 117-126. doi:10.1042/bj20050441
    • NLM

      Tonhosolo R, D'Alexandri FL, Genta FA, Wunderlich G, Gozzo FC, Eberlin MN, Peres VJ, Kimura EAS, Katzin AM. Identification, molecular cloning and functional characterization of an octaprenyl pyrophosphate synthase in intra-erythrocytic stages of Plasmodium falciparum [Internet]. Biochemical Journal. 2005 ; 392( 1): 117-126.[citado 2024 jun. 21 ] Available from: https://doi.org/10.1042/bj20050441
    • Vancouver

      Tonhosolo R, D'Alexandri FL, Genta FA, Wunderlich G, Gozzo FC, Eberlin MN, Peres VJ, Kimura EAS, Katzin AM. Identification, molecular cloning and functional characterization of an octaprenyl pyrophosphate synthase in intra-erythrocytic stages of Plasmodium falciparum [Internet]. Biochemical Journal. 2005 ; 392( 1): 117-126.[citado 2024 jun. 21 ] Available from: https://doi.org/10.1042/bj20050441
  • Source: The Journal of Biological Chemistry. Unidade: ICB

    Assunto: PARASITOLOGIA

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    • ABNT

      CASSERA, María B. et al. The methylerythritol phosphate pathway is functionally active in all intraerythrocytic stages of Plasmodium falciparum. The Journal of Biological Chemistry, v. 279, n. 50, p. 51749-51759, 2004Tradução . . Acesso em: 21 jun. 2024.
    • APA

      Cassera, M. B., Gozzo, F. C., D'Alexandri, F. L., Merino, E. F., del Portillo, H. A., Peres, V. J., et al. (2004). The methylerythritol phosphate pathway is functionally active in all intraerythrocytic stages of Plasmodium falciparum. The Journal of Biological Chemistry, 279( 50), 51749-51759.
    • NLM

      Cassera MB, Gozzo FC, D'Alexandri FL, Merino EF, del Portillo HA, Peres VJ, Almeida IC de, Eberlin MN, Wunderlich G, Wiesner J, Jomaa H, Kimura EA, Katzin AM. The methylerythritol phosphate pathway is functionally active in all intraerythrocytic stages of Plasmodium falciparum. The Journal of Biological Chemistry. 2004 ; 279( 50): 51749-51759.[citado 2024 jun. 21 ]
    • Vancouver

      Cassera MB, Gozzo FC, D'Alexandri FL, Merino EF, del Portillo HA, Peres VJ, Almeida IC de, Eberlin MN, Wunderlich G, Wiesner J, Jomaa H, Kimura EA, Katzin AM. The methylerythritol phosphate pathway is functionally active in all intraerythrocytic stages of Plasmodium falciparum. The Journal of Biological Chemistry. 2004 ; 279( 50): 51749-51759.[citado 2024 jun. 21 ]

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