Filtros : "França" "Polikarpov, Igor" Removidos: " GRU015" "Bagnato, Vanderlei Salvador" "FE-EDF" "2007-2009" Limpar

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  • Fonte: Canadian Journal of Microbiology. Unidade: IFSC

    Assuntos: ENZIMAS, CELULOSE, GENOMAS

    Acesso à fonteDOIComo citar
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    • ABNT

      TOMAZINI JUNIOR, Atilio et al. Analysis of carbohydrate-active enzymes in Thermogemmatispora sp. strain T81 reveals carbohydrate degradation ability. Canadian Journal of Microbiology, v. 64, n. 12, p. 992-1003, 2018Tradução . . Disponível em: https://doi.org/10.1139/cjm-2018-0336. Acesso em: 12 out. 2024.
    • APA

      Tomazini Junior, A., Lal, S., Munir, R., Stott, M., Henrissat, B., Polikarpov, I., et al. (2018). Analysis of carbohydrate-active enzymes in Thermogemmatispora sp. strain T81 reveals carbohydrate degradation ability. Canadian Journal of Microbiology, 64( 12), 992-1003. doi:10.1139/cjm-2018-0336
    • NLM

      Tomazini Junior A, Lal S, Munir R, Stott M, Henrissat B, Polikarpov I, Sparling R, Levin DB. Analysis of carbohydrate-active enzymes in Thermogemmatispora sp. strain T81 reveals carbohydrate degradation ability [Internet]. Canadian Journal of Microbiology. 2018 ; 64( 12): 992-1003.[citado 2024 out. 12 ] Available from: https://doi.org/10.1139/cjm-2018-0336
    • Vancouver

      Tomazini Junior A, Lal S, Munir R, Stott M, Henrissat B, Polikarpov I, Sparling R, Levin DB. Analysis of carbohydrate-active enzymes in Thermogemmatispora sp. strain T81 reveals carbohydrate degradation ability [Internet]. Canadian Journal of Microbiology. 2018 ; 64( 12): 992-1003.[citado 2024 out. 12 ] Available from: https://doi.org/10.1139/cjm-2018-0336
  • Fonte: Abstracts. Nome do evento: Annual Meeting of the Brazilian Society for Biochemistry and Molecular Biology - SBBq. Unidade: IFSC

    Assuntos: ENZIMAS CELULOLÍTICAS, BIOMATERIAIS

    Acesso à fonteComo citar
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    • ABNT

      LIBERATO, M. V. et al. Molecular characterization of a trimodular family 5 glycoside hydrolase reveals a unique conformational selection mechanism. 2016, Anais.. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular - SBBq, 2016. Disponível em: http://www.sbbq.org.br/arquivos/2016/cd2016/listaresumos.htm. Acesso em: 12 out. 2024.
    • APA

      Liberato, M. V., Silveira, R. L., Prates, E. T., Araujo, E. A., Pellegrini, V. O. A., Camilo, C. M., et al. (2016). Molecular characterization of a trimodular family 5 glycoside hydrolase reveals a unique conformational selection mechanism. In Abstracts. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular - SBBq. Recuperado de http://www.sbbq.org.br/arquivos/2016/cd2016/listaresumos.htm
    • NLM

      Liberato MV, Silveira RL, Prates ET, Araujo EA, Pellegrini VOA, Camilo CM, Kadowaki MA, Neto MO, Popov A, Skaf MS, Polikarpov I. Molecular characterization of a trimodular family 5 glycoside hydrolase reveals a unique conformational selection mechanism [Internet]. Abstracts. 2016 ;[citado 2024 out. 12 ] Available from: http://www.sbbq.org.br/arquivos/2016/cd2016/listaresumos.htm
    • Vancouver

      Liberato MV, Silveira RL, Prates ET, Araujo EA, Pellegrini VOA, Camilo CM, Kadowaki MA, Neto MO, Popov A, Skaf MS, Polikarpov I. Molecular characterization of a trimodular family 5 glycoside hydrolase reveals a unique conformational selection mechanism [Internet]. Abstracts. 2016 ;[citado 2024 out. 12 ] Available from: http://www.sbbq.org.br/arquivos/2016/cd2016/listaresumos.htm
  • Fonte: Scientific Reports. Unidade: IFSC

    Assuntos: BIOTECNOLOGIA, MICROBIOLOGIA

    Acesso à fonteDOIComo citar
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    • ABNT

      LIBERATO, Marcelo V. et al. Molecular characterization of a family 5 glycoside hydrolase suggests an induced-fit enzymatic mechanism. Scientific Reports, v. 6, p. 23473-1-23473-15 + supplementary information, 2016Tradução . . Disponível em: https://doi.org/10.1038/srep23473. Acesso em: 12 out. 2024.
    • APA

      Liberato, M. V., Silveira, R. L., Prates, É. T., Araujo, E. A., Pellegrini, V. O. A., Camilo, C. M., et al. (2016). Molecular characterization of a family 5 glycoside hydrolase suggests an induced-fit enzymatic mechanism. Scientific Reports, 6, 23473-1-23473-15 + supplementary information. doi:10.1038/srep23473
    • NLM

      Liberato MV, Silveira RL, Prates ÉT, Araujo EA, Pellegrini VOA, Camilo CM, Kadowaki MA, Neto M de O, Popov A, Skaf MS, Polikarpov I. Molecular characterization of a family 5 glycoside hydrolase suggests an induced-fit enzymatic mechanism [Internet]. Scientific Reports. 2016 ; 6 23473-1-23473-15 + supplementary information.[citado 2024 out. 12 ] Available from: https://doi.org/10.1038/srep23473
    • Vancouver

      Liberato MV, Silveira RL, Prates ÉT, Araujo EA, Pellegrini VOA, Camilo CM, Kadowaki MA, Neto M de O, Popov A, Skaf MS, Polikarpov I. Molecular characterization of a family 5 glycoside hydrolase suggests an induced-fit enzymatic mechanism [Internet]. Scientific Reports. 2016 ; 6 23473-1-23473-15 + supplementary information.[citado 2024 out. 12 ] Available from: https://doi.org/10.1038/srep23473

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