Filtros : "2011" "Journal of Molecular Biology" Removidos: "CORONAVIRUS" "Fischer, Hannes" Limpar

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  • Source: Journal of Molecular Biology. Unidade: ESALQ

    Subjects: BICHOS-DA-SEDA, FEROMÔNIOS, OLFATO, PROTEÍNAS

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    • ABNT

      MICHEL, Erich et al. Dynamic Conformational Equilibria in the Physiological Function of the Bombyx mori Pheromone-Binding Protein. Journal of Molecular Biology, v. 408, p. 922-931, 2011Tradução . . Disponível em: https://doi.org/10.1016/j.jmb.2011.03.008. Acesso em: 29 set. 2024.
    • APA

      Michel, E., Damberger, F. F., Ishida, Y., Fiorito, F., Lee, D., Leal, W. S., & Wüthrich, K. (2011). Dynamic Conformational Equilibria in the Physiological Function of the Bombyx mori Pheromone-Binding Protein. Journal of Molecular Biology, 408, 922-931. doi:10.1016/j.jmb.2011.03.008
    • NLM

      Michel E, Damberger FF, Ishida Y, Fiorito F, Lee D, Leal WS, Wüthrich K. Dynamic Conformational Equilibria in the Physiological Function of the Bombyx mori Pheromone-Binding Protein [Internet]. Journal of Molecular Biology. 2011 ; 408 922-931.[citado 2024 set. 29 ] Available from: https://doi.org/10.1016/j.jmb.2011.03.008
    • Vancouver

      Michel E, Damberger FF, Ishida Y, Fiorito F, Lee D, Leal WS, Wüthrich K. Dynamic Conformational Equilibria in the Physiological Function of the Bombyx mori Pheromone-Binding Protein [Internet]. Journal of Molecular Biology. 2011 ; 408 922-931.[citado 2024 set. 29 ] Available from: https://doi.org/10.1016/j.jmb.2011.03.008
  • Source: Journal of Molecular Biology. Unidade: IF

    Assunto: RAIOS X

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    • ABNT

      BASAIAWMOIT, R V e OLIVEIRA, C L P. SAXS models of TGFBIp reveal a trimeric structure and show that the overall shape is not affected by the arg124His mutation. Journal of Molecular Biology, v. 408, n. 3, p. 503-513, 2011Tradução . . Disponível em: https://doi.org/10.1016/j.jmb.2011.02.052. Acesso em: 29 set. 2024.
    • APA

      Basaiawmoit, R. V., & Oliveira, C. L. P. (2011). SAXS models of TGFBIp reveal a trimeric structure and show that the overall shape is not affected by the arg124His mutation. Journal of Molecular Biology, 408( 3), 503-513. doi:10.1016/j.jmb.2011.02.052
    • NLM

      Basaiawmoit RV, Oliveira CLP. SAXS models of TGFBIp reveal a trimeric structure and show that the overall shape is not affected by the arg124His mutation [Internet]. Journal of Molecular Biology. 2011 ;408( 3): 503-513.[citado 2024 set. 29 ] Available from: https://doi.org/10.1016/j.jmb.2011.02.052
    • Vancouver

      Basaiawmoit RV, Oliveira CLP. SAXS models of TGFBIp reveal a trimeric structure and show that the overall shape is not affected by the arg124His mutation [Internet]. Journal of Molecular Biology. 2011 ;408( 3): 503-513.[citado 2024 set. 29 ] Available from: https://doi.org/10.1016/j.jmb.2011.02.052
  • Source: Journal of Molecular Biology. Unidade: IF

    Assunto: RAIOS X

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    • ABNT

      BEHRENS, Manja A e OLIVEIRA, C L P. Activation of the zymogen to urokinase-type plasminogen activator is associated with increased interdomain flexibility. Journal of Molecular Biology, v. 411, n. 2, p. 417-429, 2011Tradução . . Disponível em: https://doi.org/10.1016/j.jmb.2011.05.026. Acesso em: 29 set. 2024.
    • APA

      Behrens, M. A., & Oliveira, C. L. P. (2011). Activation of the zymogen to urokinase-type plasminogen activator is associated with increased interdomain flexibility. Journal of Molecular Biology, 411( 2), 417-429. doi:10.1016/j.jmb.2011.05.026
    • NLM

      Behrens MA, Oliveira CLP. Activation of the zymogen to urokinase-type plasminogen activator is associated with increased interdomain flexibility [Internet]. Journal of Molecular Biology. 2011 ;411( 2): 417-429.[citado 2024 set. 29 ] Available from: https://doi.org/10.1016/j.jmb.2011.05.026
    • Vancouver

      Behrens MA, Oliveira CLP. Activation of the zymogen to urokinase-type plasminogen activator is associated with increased interdomain flexibility [Internet]. Journal of Molecular Biology. 2011 ;411( 2): 417-429.[citado 2024 set. 29 ] Available from: https://doi.org/10.1016/j.jmb.2011.05.026
  • Source: Journal of Molecular Biology. Unidade: IFSC

    Subjects: HORMÔNIOS TIREOIDIANOS, RECEPTORES, LIGANTES

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    • ABNT

      SOUZA, Paulo C. T. et al. Helix 12 dynamics and thyroid hormone receptor activity: experimental and molecular dynamics studies of Ile280 mutants. Journal of Molecular Biology, v. 412, n. 5, p. 882-893, 2011Tradução . . Disponível em: https://doi.org/10.1016/j.jmb.2011.04.014. Acesso em: 29 set. 2024.
    • APA

      Souza, P. C. T., Barra, G. B., Velasco, L. F. R., Ribeiro, I. C. J., Simeoni, L. A., Togashi, M., et al. (2011). Helix 12 dynamics and thyroid hormone receptor activity: experimental and molecular dynamics studies of Ile280 mutants. Journal of Molecular Biology, 412( 5), 882-893. doi:10.1016/j.jmb.2011.04.014
    • NLM

      Souza PCT, Barra GB, Velasco LFR, Ribeiro ICJ, Simeoni LA, Togashi M, Webb P, Neves FAR, Skaf MS, Martínez L, Polikarpov I. Helix 12 dynamics and thyroid hormone receptor activity: experimental and molecular dynamics studies of Ile280 mutants [Internet]. Journal of Molecular Biology. 2011 ; 412( 5): 882-893.[citado 2024 set. 29 ] Available from: https://doi.org/10.1016/j.jmb.2011.04.014
    • Vancouver

      Souza PCT, Barra GB, Velasco LFR, Ribeiro ICJ, Simeoni LA, Togashi M, Webb P, Neves FAR, Skaf MS, Martínez L, Polikarpov I. Helix 12 dynamics and thyroid hormone receptor activity: experimental and molecular dynamics studies of Ile280 mutants [Internet]. Journal of Molecular Biology. 2011 ; 412( 5): 882-893.[citado 2024 set. 29 ] Available from: https://doi.org/10.1016/j.jmb.2011.04.014

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