Filtros : "ENZIMAS (ESTUDO)" "Estados Unidos" Limpar

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  • Source: Journal of Inorganic Biochemistry. Unidades: IFSC, IQSC

    Subjects: ENZIMAS (ESTUDO), TUBERCULOSE, MANGANÊS

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    • ABNT

      OLIVEIRA, Carolina G. et al. Manganese(II) complexes with thiosemicarbazones as potential anti-Mycobacterium tuberculosis agents. Journal of Inorganic Biochemistry, v. 132, p. 21-29, 2014Tradução . . Disponível em: https://doi.org/10.1016/j.jinorgbio.2013.10.011. Acesso em: 09 ago. 2024.
    • APA

      Oliveira, C. G., Maia, P. I. da S., Souza, P. C., Pavan, F. R., Leite, C. Q. F., Viana, R. B., et al. (2014). Manganese(II) complexes with thiosemicarbazones as potential anti-Mycobacterium tuberculosis agents. Journal of Inorganic Biochemistry, 132, 21-29. doi:10.1016/j.jinorgbio.2013.10.011
    • NLM

      Oliveira CG, Maia PI da S, Souza PC, Pavan FR, Leite CQF, Viana RB, Batista AA, Nascimento OR, Deflon VM. Manganese(II) complexes with thiosemicarbazones as potential anti-Mycobacterium tuberculosis agents [Internet]. Journal of Inorganic Biochemistry. 2014 ; 132 21-29.[citado 2024 ago. 09 ] Available from: https://doi.org/10.1016/j.jinorgbio.2013.10.011
    • Vancouver

      Oliveira CG, Maia PI da S, Souza PC, Pavan FR, Leite CQF, Viana RB, Batista AA, Nascimento OR, Deflon VM. Manganese(II) complexes with thiosemicarbazones as potential anti-Mycobacterium tuberculosis agents [Internet]. Journal of Inorganic Biochemistry. 2014 ; 132 21-29.[citado 2024 ago. 09 ] Available from: https://doi.org/10.1016/j.jinorgbio.2013.10.011
  • Source: Journal of Biological Chemistry. Unidade: IFSC

    Subjects: ENZIMAS (ESTUDO), SCHISTOSOMA MANSONI

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      ZERAIK, Ana E. et al. Crystal structure of a Schistosoma mansoni septin reveals the phenomenon of strand slippage in septins dependent on the nature of the bound nucleotide. Journal of Biological Chemistry, v. 289, n. 11, p. 7799-7811, 2014Tradução . . Disponível em: https://doi.org/10.1074/jbc.M113.525352. Acesso em: 09 ago. 2024.
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      Zeraik, A. E., Pereira, H. d'M., Santos, Y. V., Brandão Neto, J., Spoerner, M., Santos, M. S., et al. (2014). Crystal structure of a Schistosoma mansoni septin reveals the phenomenon of strand slippage in septins dependent on the nature of the bound nucleotide. Journal of Biological Chemistry, 289( 11), 7799-7811. doi:10.1074/jbc.M113.525352
    • NLM

      Zeraik AE, Pereira H d'M, Santos YV, Brandão Neto J, Spoerner M, Santos MS, Colnago LA, Garratt RC, Araújo APU de, De Marco R. Crystal structure of a Schistosoma mansoni septin reveals the phenomenon of strand slippage in septins dependent on the nature of the bound nucleotide [Internet]. Journal of Biological Chemistry. 2014 ; 289( 11): 7799-7811.[citado 2024 ago. 09 ] Available from: https://doi.org/10.1074/jbc.M113.525352
    • Vancouver

      Zeraik AE, Pereira H d'M, Santos YV, Brandão Neto J, Spoerner M, Santos MS, Colnago LA, Garratt RC, Araújo APU de, De Marco R. Crystal structure of a Schistosoma mansoni septin reveals the phenomenon of strand slippage in septins dependent on the nature of the bound nucleotide [Internet]. Journal of Biological Chemistry. 2014 ; 289( 11): 7799-7811.[citado 2024 ago. 09 ] Available from: https://doi.org/10.1074/jbc.M113.525352
  • Source: PLOS ONE. Unidades: IFSC, IQ

    Subjects: ENZIMAS (ESTUDO), PROTEÍNAS, AMINOÁCIDOS

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      TAMAKI, Fábio K. et al. Sets of covariant residues modulate the activity and thermal stability of GH1 β-glucosidases. PLOS ONE, v. 9, n. 5, p. e96627-1-e96627-8, 2014Tradução . . Disponível em: https://doi.org/10.1371/journal.pone.0096627. Acesso em: 09 ago. 2024.
    • APA

      Tamaki, F. K., Textor, L. C., Polikarpov, I., & Marana, S. R. (2014). Sets of covariant residues modulate the activity and thermal stability of GH1 β-glucosidases. PLOS ONE, 9( 5), e96627-1-e96627-8. doi:10.1371/journal.pone.0096627
    • NLM

      Tamaki FK, Textor LC, Polikarpov I, Marana SR. Sets of covariant residues modulate the activity and thermal stability of GH1 β-glucosidases [Internet]. PLOS ONE. 2014 ; 9( 5): e96627-1-e96627-8.[citado 2024 ago. 09 ] Available from: https://doi.org/10.1371/journal.pone.0096627
    • Vancouver

      Tamaki FK, Textor LC, Polikarpov I, Marana SR. Sets of covariant residues modulate the activity and thermal stability of GH1 β-glucosidases [Internet]. PLOS ONE. 2014 ; 9( 5): e96627-1-e96627-8.[citado 2024 ago. 09 ] Available from: https://doi.org/10.1371/journal.pone.0096627
  • Source: PLOS ONE. Unidade: IFSC

    Subjects: ENZIMAS (ESTUDO), BIOMASSA, BIOCOMBUSTÍVEIS

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      MIOTTO, Lis Schwartz et al. The characterization of the endoglucanase Cel12A from Gloeophyllum trabeum reveals an enzyme highly active on β-glucan. PLOS ONE, v. 9, n. 9, p. e108393-1-e108393-9, 2014Tradução . . Disponível em: https://doi.org/10.1371/journal.pone.0108393. Acesso em: 09 ago. 2024.
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      Miotto, L. S., Rezende, C. A. de, Bernardes, A., Serpa, V. I., Tsang, A., & Polikarpov, I. (2014). The characterization of the endoglucanase Cel12A from Gloeophyllum trabeum reveals an enzyme highly active on β-glucan. PLOS ONE, 9( 9), e108393-1-e108393-9. doi:10.1371/journal.pone.0108393
    • NLM

      Miotto LS, Rezende CA de, Bernardes A, Serpa VI, Tsang A, Polikarpov I. The characterization of the endoglucanase Cel12A from Gloeophyllum trabeum reveals an enzyme highly active on β-glucan [Internet]. PLOS ONE. 2014 ; 9( 9): e108393-1-e108393-9.[citado 2024 ago. 09 ] Available from: https://doi.org/10.1371/journal.pone.0108393
    • Vancouver

      Miotto LS, Rezende CA de, Bernardes A, Serpa VI, Tsang A, Polikarpov I. The characterization of the endoglucanase Cel12A from Gloeophyllum trabeum reveals an enzyme highly active on β-glucan [Internet]. PLOS ONE. 2014 ; 9( 9): e108393-1-e108393-9.[citado 2024 ago. 09 ] Available from: https://doi.org/10.1371/journal.pone.0108393
  • Source: PLOS ONE. Unidade: IFSC

    Subjects: ENZIMAS (ESTUDO), OLIGOPEPTÍDEOS

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      FERREIRA, Juliana C. et al. Recycling of the high valence states of heme proteins by cysteine residues of thimet-oligopeptidase. PLOS ONE, v. No 2013, n. 11, p. e79102-1-e79102-16, 2013Tradução . . Disponível em: https://doi.org/10.1371/journal.pone.0079102. Acesso em: 09 ago. 2024.
    • APA

      Ferreira, J. C., Icimoto, M. Y., Marcondes, M. F., Oliveira, V., Nascimento, O. R., & Nantes, I. L. (2013). Recycling of the high valence states of heme proteins by cysteine residues of thimet-oligopeptidase. PLOS ONE, No 2013( 11), e79102-1-e79102-16. doi:10.1371/journal.pone.0079102
    • NLM

      Ferreira JC, Icimoto MY, Marcondes MF, Oliveira V, Nascimento OR, Nantes IL. Recycling of the high valence states of heme proteins by cysteine residues of thimet-oligopeptidase [Internet]. PLOS ONE. 2013 ; No 2013( 11): e79102-1-e79102-16.[citado 2024 ago. 09 ] Available from: https://doi.org/10.1371/journal.pone.0079102
    • Vancouver

      Ferreira JC, Icimoto MY, Marcondes MF, Oliveira V, Nascimento OR, Nantes IL. Recycling of the high valence states of heme proteins by cysteine residues of thimet-oligopeptidase [Internet]. PLOS ONE. 2013 ; No 2013( 11): e79102-1-e79102-16.[citado 2024 ago. 09 ] Available from: https://doi.org/10.1371/journal.pone.0079102
  • Source: Acta Crystallographica F. Unidade: IFSC

    Subjects: DOENÇA DE CHAGAS (CONTROLE), PROTEÍNAS (PREPARO), RAIOS X (ANÁLISE), ENZIMAS (ESTUDO), TRYPANOSOMA CRUZI, FÁRMACOS (DESENVOLVIMENTO)

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      GÓMEZ BARROSO, J. A. et al. Protein preparation, crystallization and preliminary X-ray analysis of Trypanosoma cruzi nucleoside diphosphate kinase 1. Acta Crystallographica F, v. 66, p. 862-865, 2010Tradução . . Disponível em: https://doi.org/10.1107/S1744309110013886. Acesso em: 09 ago. 2024.
    • APA

      Gómez Barroso, J. A., Pereira, H., Miranda, M., Pereira, C., Garratt, R. C., & Aguilar, C. F. (2010). Protein preparation, crystallization and preliminary X-ray analysis of Trypanosoma cruzi nucleoside diphosphate kinase 1. Acta Crystallographica F, 66, 862-865. doi:10.1107/S1744309110013886
    • NLM

      Gómez Barroso JA, Pereira H, Miranda M, Pereira C, Garratt RC, Aguilar CF. Protein preparation, crystallization and preliminary X-ray analysis of Trypanosoma cruzi nucleoside diphosphate kinase 1 [Internet]. Acta Crystallographica F. 2010 ; 66 862-865.[citado 2024 ago. 09 ] Available from: https://doi.org/10.1107/S1744309110013886
    • Vancouver

      Gómez Barroso JA, Pereira H, Miranda M, Pereira C, Garratt RC, Aguilar CF. Protein preparation, crystallization and preliminary X-ray analysis of Trypanosoma cruzi nucleoside diphosphate kinase 1 [Internet]. Acta Crystallographica F. 2010 ; 66 862-865.[citado 2024 ago. 09 ] Available from: https://doi.org/10.1107/S1744309110013886

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