Filtros : "Watanabe, Tatiana F." Limpar

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  • Source: FEBS Journal. Unidade: IFSC

    Subjects: CRISTALOGRAFIA, BIOFÍSICA, PROTEÍNAS

    Versão PublicadaAcesso à fonteDOIHow to cite
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    • ABNT

      SASAKI, Daisuke et al. Reverse protein engineering of a novel 4-domain copper nitrite reductase reveals functional regulation by protein-protein interaction. FEBS Journal, v. 288, n. Ja 2021, p. 262-280, 2021Tradução . . Disponível em: https://doi.org/10.1111/febs.15324. Acesso em: 03 jun. 2024.
    • APA

      Sasaki, D., Watanabe, T. F., Eady, R. R., Garratt, R. C., Antonyuk, S. V., & Hasnain, S. S. (2021). Reverse protein engineering of a novel 4-domain copper nitrite reductase reveals functional regulation by protein-protein interaction. FEBS Journal, 288( Ja 2021), 262-280. doi:10.1111/febs.15324
    • NLM

      Sasaki D, Watanabe TF, Eady RR, Garratt RC, Antonyuk SV, Hasnain SS. Reverse protein engineering of a novel 4-domain copper nitrite reductase reveals functional regulation by protein-protein interaction [Internet]. FEBS Journal. 2021 ; 288( Ja 2021): 262-280.[citado 2024 jun. 03 ] Available from: https://doi.org/10.1111/febs.15324
    • Vancouver

      Sasaki D, Watanabe TF, Eady RR, Garratt RC, Antonyuk SV, Hasnain SS. Reverse protein engineering of a novel 4-domain copper nitrite reductase reveals functional regulation by protein-protein interaction [Internet]. FEBS Journal. 2021 ; 288( Ja 2021): 262-280.[citado 2024 jun. 03 ] Available from: https://doi.org/10.1111/febs.15324
  • Source: IUCrJ. Unidade: IFSC

    Subjects: NITROGÊNIO, DESNITRIFICAÇÃO, CATÁLISE

    Versão PublicadaAcesso à fonteDOIHow to cite
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    • ABNT

      SASAKI, Daisuke et al. Structures of substrate- and product-bound forms of a multi-domain copper nitrite reductase shed light on the role of domain tethering in protein complexes. IUCrJ, v. 7, p. 557-565 + sup1-sup6, 2020Tradução . . Disponível em: https://doi.org/10.1107/S2052252520005230. Acesso em: 03 jun. 2024.
    • APA

      Sasaki, D., Watanabe, T. F., Eady, R. R., Garratt, R. C., Antonyuk, S. V., & Hasnain, S. S. (2020). Structures of substrate- and product-bound forms of a multi-domain copper nitrite reductase shed light on the role of domain tethering in protein complexes. IUCrJ, 7, 557-565 + sup1-sup6. doi:10.1107/S2052252520005230
    • NLM

      Sasaki D, Watanabe TF, Eady RR, Garratt RC, Antonyuk SV, Hasnain SS. Structures of substrate- and product-bound forms of a multi-domain copper nitrite reductase shed light on the role of domain tethering in protein complexes [Internet]. IUCrJ. 2020 ; 7 557-565 + sup1-sup6.[citado 2024 jun. 03 ] Available from: https://doi.org/10.1107/S2052252520005230
    • Vancouver

      Sasaki D, Watanabe TF, Eady RR, Garratt RC, Antonyuk SV, Hasnain SS. Structures of substrate- and product-bound forms of a multi-domain copper nitrite reductase shed light on the role of domain tethering in protein complexes [Internet]. IUCrJ. 2020 ; 7 557-565 + sup1-sup6.[citado 2024 jun. 03 ] Available from: https://doi.org/10.1107/S2052252520005230
  • Source: Scientific Reports. Unidades: FCFRP, IFSC

    Subjects: QUÍMICA MÉDICA, PLANTAS MEDICINAIS

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    • ABNT

      SOUZA-MOREIRA, Tatiana M. et al. Friedelin synthase from maytenus ilicifolia: leucine 482 plays an essential role in the production of the most rearranged pentacyclic triterpene. Scientific Reports, v. No 2016, p. 36858-1-36858-13, 2016Tradução . . Disponível em: https://doi.org/10.1038/srep36858. Acesso em: 03 jun. 2024.
    • APA

      Souza-Moreira, T. M., Alves, T. B., Pinheiro, K. A., Felippe, L. G., Lima, G. M. A., Watanabe, T. F., et al. (2016). Friedelin synthase from maytenus ilicifolia: leucine 482 plays an essential role in the production of the most rearranged pentacyclic triterpene. Scientific Reports, No 2016, 36858-1-36858-13. doi:10.1038/srep36858
    • NLM

      Souza-Moreira TM, Alves TB, Pinheiro KA, Felippe LG, Lima GMA, Watanabe TF, Barbosa CC, Santos VAFFM, Lopes NP, Valentini SR, Guido RVC, Furlan M, Zanelli CF. Friedelin synthase from maytenus ilicifolia: leucine 482 plays an essential role in the production of the most rearranged pentacyclic triterpene [Internet]. Scientific Reports. 2016 ; No 2016 36858-1-36858-13.[citado 2024 jun. 03 ] Available from: https://doi.org/10.1038/srep36858
    • Vancouver

      Souza-Moreira TM, Alves TB, Pinheiro KA, Felippe LG, Lima GMA, Watanabe TF, Barbosa CC, Santos VAFFM, Lopes NP, Valentini SR, Guido RVC, Furlan M, Zanelli CF. Friedelin synthase from maytenus ilicifolia: leucine 482 plays an essential role in the production of the most rearranged pentacyclic triterpene [Internet]. Scientific Reports. 2016 ; No 2016 36858-1-36858-13.[citado 2024 jun. 03 ] Available from: https://doi.org/10.1038/srep36858
  • Source: Memórias do Instituto Oswaldo Cruz. Unidade: FMRP

    Assunto: TRYPANOSOMA CRUZI

    Acesso à fonteDOIHow to cite
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    • ABNT

      SILVA, Marco Túlio A. da et al. New insights into trypanosomatid U5 small nuclear ribonucleoproteins. Memórias do Instituto Oswaldo Cruz, v. 106, n. 2, p. 130-138, 2011Tradução . . Disponível em: https://doi.org/10.1590/s0074-02762011000200003. Acesso em: 03 jun. 2024.
    • APA

      Silva, M. T. A. da, Ambrósio, D. L., Trevelin, C. C., Watanabe, T. F., Laure, H. J., Greene, L. J., et al. (2011). New insights into trypanosomatid U5 small nuclear ribonucleoproteins. Memórias do Instituto Oswaldo Cruz, 106( 2), 130-138. doi:10.1590/s0074-02762011000200003
    • NLM

      Silva MTA da, Ambrósio DL, Trevelin CC, Watanabe TF, Laure HJ, Greene LJ, Rosa JC, Valentini SR, Cicarelli RMB. New insights into trypanosomatid U5 small nuclear ribonucleoproteins [Internet]. Memórias do Instituto Oswaldo Cruz. 2011 ; 106( 2): 130-138.[citado 2024 jun. 03 ] Available from: https://doi.org/10.1590/s0074-02762011000200003
    • Vancouver

      Silva MTA da, Ambrósio DL, Trevelin CC, Watanabe TF, Laure HJ, Greene LJ, Rosa JC, Valentini SR, Cicarelli RMB. New insights into trypanosomatid U5 small nuclear ribonucleoproteins [Internet]. Memórias do Instituto Oswaldo Cruz. 2011 ; 106( 2): 130-138.[citado 2024 jun. 03 ] Available from: https://doi.org/10.1590/s0074-02762011000200003

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