Filtros : "WARD, RICHARD JOHN" "2013" Removido: "BIOQUÍMICA" Limpar

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  • Source: Abstracts. Conference titles: Conference Protein Engineering: new approaches and applications. Unidade: FFCLRP

    Subjects: ENZIMAS, BIOENGENHARIA

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      PINHEIRO, Matheus Pinto e REIS, Renata Almeida Garcia e WARD, Richard John. Design of a left-handed β-3-solenoid as a scaffold for multifunctional biocatalyst development. 2013, Anais.. Chester: Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto, Universidade de São Paulo, 2013. Disponível em: http://www.biochemistry.org/Portals/0/Conferences/abstracts/SA143/SA143P022.pdf. Acesso em: 14 ago. 2024.
    • APA

      Pinheiro, M. P., Reis, R. A. G., & Ward, R. J. (2013). Design of a left-handed β-3-solenoid as a scaffold for multifunctional biocatalyst development. In Abstracts. Chester: Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto, Universidade de São Paulo. Recuperado de http://www.biochemistry.org/Portals/0/Conferences/abstracts/SA143/SA143P022.pdf
    • NLM

      Pinheiro MP, Reis RAG, Ward RJ. Design of a left-handed β-3-solenoid as a scaffold for multifunctional biocatalyst development [Internet]. Abstracts. 2013 ;[citado 2024 ago. 14 ] Available from: http://www.biochemistry.org/Portals/0/Conferences/abstracts/SA143/SA143P022.pdf
    • Vancouver

      Pinheiro MP, Reis RAG, Ward RJ. Design of a left-handed β-3-solenoid as a scaffold for multifunctional biocatalyst development [Internet]. Abstracts. 2013 ;[citado 2024 ago. 14 ] Available from: http://www.biochemistry.org/Portals/0/Conferences/abstracts/SA143/SA143P022.pdf
  • Source: Abstracts. Conference titles: Protein-Protein Interactions : Emerging Science and Therapeutic Potential. Unidade: FFCLRP

    Subjects: PROTEÍNAS (INTERAÇÃO), ENZIMAS

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      WARD, Richard John et al. Creation of protein/protein interfaces modulates catalytic activity in multifunctional chimeric enzymes. 2013, Anais.. London: Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto, Universidade de São Paulo, 2013. . Acesso em: 14 ago. 2024.
    • APA

      Ward, R. J., Ribeiro, L. F., Furtado, G. P., & Lourenzoni, M. R. (2013). Creation of protein/protein interfaces modulates catalytic activity in multifunctional chimeric enzymes. In Abstracts. London: Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto, Universidade de São Paulo.
    • NLM

      Ward RJ, Ribeiro LF, Furtado GP, Lourenzoni MR. Creation of protein/protein interfaces modulates catalytic activity in multifunctional chimeric enzymes. Abstracts. 2013 ;[citado 2024 ago. 14 ]
    • Vancouver

      Ward RJ, Ribeiro LF, Furtado GP, Lourenzoni MR. Creation of protein/protein interfaces modulates catalytic activity in multifunctional chimeric enzymes. Abstracts. 2013 ;[citado 2024 ago. 14 ]
  • Source: Protein Engineering Design and Selection. Unidade: FFCLRP

    Subjects: BACTÉRIAS, ENZIMAS, CATÁLISE, ESPECTROSCOPIA

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      FURTADO, G. P. et al. A designed bifunctional laccase/β-I,3-I,4-glucanase enzyme shows synergistic sugar release from milled sugarcane bagasse. Protein Engineering Design and Selection, v. 26, n. 1, p. 15-23, 2013Tradução . . Disponível em: https://doi.org/10.1093/protein/gzs057. Acesso em: 14 ago. 2024.
    • APA

      Furtado, G. P., Ribeiro, L. F., Lourenzoni, M. R., & Ward, R. J. (2013). A designed bifunctional laccase/β-I,3-I,4-glucanase enzyme shows synergistic sugar release from milled sugarcane bagasse. Protein Engineering Design and Selection, 26( 1), 15-23. doi:10.1093/protein/gzs057
    • NLM

      Furtado GP, Ribeiro LF, Lourenzoni MR, Ward RJ. A designed bifunctional laccase/β-I,3-I,4-glucanase enzyme shows synergistic sugar release from milled sugarcane bagasse [Internet]. Protein Engineering Design and Selection. 2013 ; 26( 1): 15-23.[citado 2024 ago. 14 ] Available from: https://doi.org/10.1093/protein/gzs057
    • Vancouver

      Furtado GP, Ribeiro LF, Lourenzoni MR, Ward RJ. A designed bifunctional laccase/β-I,3-I,4-glucanase enzyme shows synergistic sugar release from milled sugarcane bagasse [Internet]. Protein Engineering Design and Selection. 2013 ; 26( 1): 15-23.[citado 2024 ago. 14 ] Available from: https://doi.org/10.1093/protein/gzs057
  • Source: Journal of Molecular Catalysis B: Enzymatic. Unidade: FFCLRP

    Subjects: GLUTAMATOS, CELULOSE, HIDRÓLISE (PROCESSOS)

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      SOUZA, Flávio Henrique Moreira et al. Glucose and xylose stimulation of a β-glucosidase from the thermophilic fungus Humicola insolens: a kinetic and biophysical study. Journal of Molecular Catalysis B: Enzymatic, v. 94, p. 119-128, 2013Tradução . . Disponível em: https://doi.org/10.1016/j.molcatb.2013.05.012. Acesso em: 14 ago. 2024.
    • APA

      Souza, F. H. M., Inocentes, R. F., Ward, R. J., Jorge, J. A., & Furriel, R. dos P. M. (2013). Glucose and xylose stimulation of a β-glucosidase from the thermophilic fungus Humicola insolens: a kinetic and biophysical study. Journal of Molecular Catalysis B: Enzymatic, 94, 119-128. doi:10.1016/j.molcatb.2013.05.012
    • NLM

      Souza FHM, Inocentes RF, Ward RJ, Jorge JA, Furriel R dos PM. Glucose and xylose stimulation of a β-glucosidase from the thermophilic fungus Humicola insolens: a kinetic and biophysical study [Internet]. Journal of Molecular Catalysis B: Enzymatic. 2013 ; 94 119-128.[citado 2024 ago. 14 ] Available from: https://doi.org/10.1016/j.molcatb.2013.05.012
    • Vancouver

      Souza FHM, Inocentes RF, Ward RJ, Jorge JA, Furriel R dos PM. Glucose and xylose stimulation of a β-glucosidase from the thermophilic fungus Humicola insolens: a kinetic and biophysical study [Internet]. Journal of Molecular Catalysis B: Enzymatic. 2013 ; 94 119-128.[citado 2024 ago. 14 ] Available from: https://doi.org/10.1016/j.molcatb.2013.05.012
  • Source: Abstracts. Conference titles: Conference Protein Engineering: new approaches and applications. Unidade: FFCLRP

    Subjects: ENZIMAS, BIOENGENHARIA

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      RIBEIRO, Lucas Ferreira et al. Creation of allosteric bifunctional xylanase-XBP chimeras by in vitro recombination of nonhomologous genes. 2013, Anais.. Chester: Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto, Universidade de São Paulo, 2013. Disponível em: http://www.biochemistry.org/Portals/0/Conferences/abstracts/SA143/SA143P021.pdf. Acesso em: 14 ago. 2024.
    • APA

      Ribeiro, L. F., Tullman, J., Nicholes, N., Ostermeier, M., & Ward, R. J. (2013). Creation of allosteric bifunctional xylanase-XBP chimeras by in vitro recombination of nonhomologous genes. In Abstracts. Chester: Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto, Universidade de São Paulo. Recuperado de http://www.biochemistry.org/Portals/0/Conferences/abstracts/SA143/SA143P021.pdf
    • NLM

      Ribeiro LF, Tullman J, Nicholes N, Ostermeier M, Ward RJ. Creation of allosteric bifunctional xylanase-XBP chimeras by in vitro recombination of nonhomologous genes [Internet]. Abstracts. 2013 ;[citado 2024 ago. 14 ] Available from: http://www.biochemistry.org/Portals/0/Conferences/abstracts/SA143/SA143P021.pdf
    • Vancouver

      Ribeiro LF, Tullman J, Nicholes N, Ostermeier M, Ward RJ. Creation of allosteric bifunctional xylanase-XBP chimeras by in vitro recombination of nonhomologous genes [Internet]. Abstracts. 2013 ;[citado 2024 ago. 14 ] Available from: http://www.biochemistry.org/Portals/0/Conferences/abstracts/SA143/SA143P021.pdf
  • Source: Journal of Biotechnology. Unidades: FZEA, FFCLRP

    Subjects: CITOMETRIA DE FLUXO, PROTEÍNAS DE FLUORESCÊNCIA VERDE, ESCHERICHIA

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      RIBEIRO, Lucas F. et al. d-Xylose detection in Escherichia coli by a xylose binding protein-dependent response. Journal of Biotechnology, v. 168, n. 4, p. 440-445, 2013Tradução . . Disponível em: https://doi.org/10.1016/j.jbiotec.2013.10.019. Acesso em: 14 ago. 2024.
    • APA

      Ribeiro, L. F., Bressan, F. F., Furtado, G. P., Meirelles, F. V., & Ward, R. J. (2013). d-Xylose detection in Escherichia coli by a xylose binding protein-dependent response. Journal of Biotechnology, 168( 4), 440-445. doi:10.1016/j.jbiotec.2013.10.019
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      Ribeiro LF, Bressan FF, Furtado GP, Meirelles FV, Ward RJ. d-Xylose detection in Escherichia coli by a xylose binding protein-dependent response [Internet]. Journal of Biotechnology. 2013 ; 168( 4): 440-445.[citado 2024 ago. 14 ] Available from: https://doi.org/10.1016/j.jbiotec.2013.10.019
    • Vancouver

      Ribeiro LF, Bressan FF, Furtado GP, Meirelles FV, Ward RJ. d-Xylose detection in Escherichia coli by a xylose binding protein-dependent response [Internet]. Journal of Biotechnology. 2013 ; 168( 4): 440-445.[citado 2024 ago. 14 ] Available from: https://doi.org/10.1016/j.jbiotec.2013.10.019
  • Source: Journal of Biological Chemistry. Unidade: FFCLRP

    Subjects: ESCHERICHIA COLI (ENZIMOLOGIA), BACILOS GRAM-NEGATIVOS FACULTATIVAMENTE ANAERÓBICOS, MUTAGÊNESE, PROTEÍNAS

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      MALDONADO, Raquel Fonseca et al. Engineering the pattern of protein glycosylation modulates the thermostability of a GH11 xylanase. Journal of Biological Chemistry, v. 288, n. 35, p. 25522- 25534, 2013Tradução . . Disponível em: https://doi.org/10.1074/jbc.M113.485953. Acesso em: 14 ago. 2024.
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      Maldonado, R. F., Vieira, D., Alponti, J. S., Bonneil, E., Thibault, P., & Ward, R. J. (2013). Engineering the pattern of protein glycosylation modulates the thermostability of a GH11 xylanase. Journal of Biological Chemistry, 288( 35), 25522- 25534. doi:10.1074/jbc.M113.485953
    • NLM

      Maldonado RF, Vieira D, Alponti JS, Bonneil E, Thibault P, Ward RJ. Engineering the pattern of protein glycosylation modulates the thermostability of a GH11 xylanase [Internet]. Journal of Biological Chemistry. 2013 ; 288( 35): 25522- 25534.[citado 2024 ago. 14 ] Available from: https://doi.org/10.1074/jbc.M113.485953
    • Vancouver

      Maldonado RF, Vieira D, Alponti JS, Bonneil E, Thibault P, Ward RJ. Engineering the pattern of protein glycosylation modulates the thermostability of a GH11 xylanase [Internet]. Journal of Biological Chemistry. 2013 ; 288( 35): 25522- 25534.[citado 2024 ago. 14 ] Available from: https://doi.org/10.1074/jbc.M113.485953

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