Filtros : "Antonyuk, Svetlana V." 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: 20 maio 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 maio 20 ] 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 maio 20 ] Available from: https://doi.org/10.1111/febs.15324
  • Source: European Journal of Medicinal Chemistry Reports. Unidades: ICB, IFSC

    Subjects: ANTIMALÁRICOS, ANTIPARASITÁRIOS, MALÁRIA, PLASMODIUM FALCIPARUM

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    • ABNT

      SOUZA, Juliana Oliveira de et al. Parasitological profiling shows 4(1H)-quinolone derivatives as new lead candidates for malaria. European Journal of Medicinal Chemistry Reports, v. 3, p. 100012-1-100012-16 + supplementary data, 2021Tradução . . Disponível em: https://doi.org/10.1016/j.ejmcr.2021.100012. Acesso em: 20 maio 2024.
    • APA

      Souza, J. O. de, Almeida, S. M., Souza, G. E. de, Zanini, C. L., Silva, E. M. da, Paim, J. C., et al. (2021). Parasitological profiling shows 4(1H)-quinolone derivatives as new lead candidates for malaria. European Journal of Medicinal Chemistry Reports, 3, 100012-1-100012-16 + supplementary data. doi:10.1016/j.ejmcr.2021.100012
    • NLM

      Souza JO de, Almeida SM, Souza GE de, Zanini CL, Silva EM da, Paim JC, Bargieri DY, Amporndanai K, Antonyuk SV, Hasnain SS, Cruz FC, Pereira DB, Oliva G, Corrêa AG, Aguiar ACC, Guido RVC. Parasitological profiling shows 4(1H)-quinolone derivatives as new lead candidates for malaria [Internet]. European Journal of Medicinal Chemistry Reports. 2021 ; 3 100012-1-100012-16 + supplementary data.[citado 2024 maio 20 ] Available from: https://doi.org/10.1016/j.ejmcr.2021.100012
    • Vancouver

      Souza JO de, Almeida SM, Souza GE de, Zanini CL, Silva EM da, Paim JC, Bargieri DY, Amporndanai K, Antonyuk SV, Hasnain SS, Cruz FC, Pereira DB, Oliva G, Corrêa AG, Aguiar ACC, Guido RVC. Parasitological profiling shows 4(1H)-quinolone derivatives as new lead candidates for malaria [Internet]. European Journal of Medicinal Chemistry Reports. 2021 ; 3 100012-1-100012-16 + supplementary data.[citado 2024 maio 20 ] Available from: https://doi.org/10.1016/j.ejmcr.2021.100012
  • Source: IUCrJ. Unidade: IFSC

    Subjects: NITROGÊNIO, DESNITRIFICAÇÃO, CATÁLISE

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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: 20 maio 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 maio 20 ] 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 maio 20 ] Available from: https://doi.org/10.1107/S2052252520005230
  • Source: PLOS Biology. Unidade: IFSC

    Subjects: CRISTALIZAÇÃO, PROTEÍNAS

    Versão PublicadaAcesso à fonteDOIHow to cite
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    • ABNT

      SALA, Fernanda A. et al. Molecular recognition and maturation of SOD1 by its evolutionarily destabilised cognate chaperone hCCS. PLOS Biology, v. 17, n. 2, p. e3000141-1-e3000141-22, 2019Tradução . . Disponível em: https://doi.org/10.1371/journal.pbio.3000141. Acesso em: 20 maio 2024.
    • APA

      Sala, F. A., Wright, G. S. A., Antonyuk, S. V., Garratt, R. C., & Hasnain, S. S. (2019). Molecular recognition and maturation of SOD1 by its evolutionarily destabilised cognate chaperone hCCS. PLOS Biology, 17( 2), e3000141-1-e3000141-22. doi:10.1371/journal.pbio.3000141
    • NLM

      Sala FA, Wright GSA, Antonyuk SV, Garratt RC, Hasnain SS. Molecular recognition and maturation of SOD1 by its evolutionarily destabilised cognate chaperone hCCS [Internet]. PLOS Biology. 2019 ; 17( 2): e3000141-1-e3000141-22.[citado 2024 maio 20 ] Available from: https://doi.org/10.1371/journal.pbio.3000141
    • Vancouver

      Sala FA, Wright GSA, Antonyuk SV, Garratt RC, Hasnain SS. Molecular recognition and maturation of SOD1 by its evolutionarily destabilised cognate chaperone hCCS [Internet]. PLOS Biology. 2019 ; 17( 2): e3000141-1-e3000141-22.[citado 2024 maio 20 ] Available from: https://doi.org/10.1371/journal.pbio.3000141

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