Filtros : "MUNIZ, JOÃO RENATO CARVALHO" "Squina, Fabio M." Removido: "Financiado pelo LNLS" Limpar

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  • Source: Biochimica et Biophysica Acta: Proteins and Proteomics. Unidade: IFSC

    Subjects: IMUNOGLOBULINAS, BIOMASSA, MONOSSACARÍDEOS

    PrivadoAcesso à fonteDOIHow to cite
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    • ABNT

      SILVA, Viviam M. et al. High-resolution structure of a modular hyperthermostable endo-β-1,4-mannanase from Thermotoga petrophila: the ancillary immunoglobulin-like module is a thermostabilizing domain. Biochimica et Biophysica Acta: Proteins and Proteomics, v. 1868, n. 8, p. 140437-1-140437-8, 2020Tradução . . Disponível em: https://doi.org/10.1016/j.bbapap.2020.140437. Acesso em: 22 ago. 2024.
    • APA

      Silva, V. M., Cabral, A. D., Sperança, M. A., Squina, F. M., Muniz, J. R. C., Martin, L., et al. (2020). High-resolution structure of a modular hyperthermostable endo-β-1,4-mannanase from Thermotoga petrophila: the ancillary immunoglobulin-like module is a thermostabilizing domain. Biochimica et Biophysica Acta: Proteins and Proteomics, 1868( 8), 140437-1-140437-8. doi:10.1016/j.bbapap.2020.140437
    • NLM

      Silva VM, Cabral AD, Sperança MA, Squina FM, Muniz JRC, Martin L, Nicolet Y, Garcia W. High-resolution structure of a modular hyperthermostable endo-β-1,4-mannanase from Thermotoga petrophila: the ancillary immunoglobulin-like module is a thermostabilizing domain [Internet]. Biochimica et Biophysica Acta: Proteins and Proteomics. 2020 ; 1868( 8): 140437-1-140437-8.[citado 2024 ago. 22 ] Available from: https://doi.org/10.1016/j.bbapap.2020.140437
    • Vancouver

      Silva VM, Cabral AD, Sperança MA, Squina FM, Muniz JRC, Martin L, Nicolet Y, Garcia W. High-resolution structure of a modular hyperthermostable endo-β-1,4-mannanase from Thermotoga petrophila: the ancillary immunoglobulin-like module is a thermostabilizing domain [Internet]. Biochimica et Biophysica Acta: Proteins and Proteomics. 2020 ; 1868( 8): 140437-1-140437-8.[citado 2024 ago. 22 ] Available from: https://doi.org/10.1016/j.bbapap.2020.140437
  • Source: PLOS ONE. Unidade: IFSC

    Subjects: BIOTECNOLOGIA, LIGNINA

    Versão PublicadaAcesso à fonteDOIHow to cite
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    • ABNT

      SILVA, Viviam M. et al. Systematic studies of the interactions between a model polyphenol compound and microbial β-glucosidases. PLOS ONE, v. 12, n. 7, p. e0181629-1-e0181629-15, 2017Tradução . . Disponível em: https://doi.org/10.1371/journal.pone.0181629. Acesso em: 22 ago. 2024.
    • APA

      Silva, V. M., Sato, J. A. P., Araujo, J. N., Squina, F. M., Muniz, J. R. C., Riske, K. A., & Garcia, W. (2017). Systematic studies of the interactions between a model polyphenol compound and microbial β-glucosidases. PLOS ONE, 12( 7), e0181629-1-e0181629-15. doi:10.1371/journal.pone.0181629
    • NLM

      Silva VM, Sato JAP, Araujo JN, Squina FM, Muniz JRC, Riske KA, Garcia W. Systematic studies of the interactions between a model polyphenol compound and microbial β-glucosidases [Internet]. PLOS ONE. 2017 ; 12( 7): e0181629-1-e0181629-15.[citado 2024 ago. 22 ] Available from: https://doi.org/10.1371/journal.pone.0181629
    • Vancouver

      Silva VM, Sato JAP, Araujo JN, Squina FM, Muniz JRC, Riske KA, Garcia W. Systematic studies of the interactions between a model polyphenol compound and microbial β-glucosidases [Internet]. PLOS ONE. 2017 ; 12( 7): e0181629-1-e0181629-15.[citado 2024 ago. 22 ] Available from: https://doi.org/10.1371/journal.pone.0181629
  • Source: Enzyme and Microbial Technology. Unidade: IFSC

    Subjects: ENZIMAS, HIDRÓLISE, ENZIMAS HIDROLÍTICAS

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    • ABNT

      SILVA, Viviam M. et al. Non-productive adsorption of bacterial β-glucosidases on lignins is electrostatically modulated and depends on the presence offibronection type III-like domain. Enzyme and Microbial Technology, v. 87-88, p. 1-8, 2016Tradução . . Disponível em: https://doi.org/10.1016/j.enzmictec.2016.02.007. Acesso em: 22 ago. 2024.
    • APA

      Silva, V. M., Souza, A. S., Negrão, D. R., Polikarpov, I., Squina, F. M., Oliveira Neto, M. de, et al. (2016). Non-productive adsorption of bacterial β-glucosidases on lignins is electrostatically modulated and depends on the presence offibronection type III-like domain. Enzyme and Microbial Technology, 87-88, 1-8. doi:10.1016/j.enzmictec.2016.02.007
    • NLM

      Silva VM, Souza AS, Negrão DR, Polikarpov I, Squina FM, Oliveira Neto M de, Muniz JRC, Garcia W. Non-productive adsorption of bacterial β-glucosidases on lignins is electrostatically modulated and depends on the presence offibronection type III-like domain [Internet]. Enzyme and Microbial Technology. 2016 ; 87-88 1-8.[citado 2024 ago. 22 ] Available from: https://doi.org/10.1016/j.enzmictec.2016.02.007
    • Vancouver

      Silva VM, Souza AS, Negrão DR, Polikarpov I, Squina FM, Oliveira Neto M de, Muniz JRC, Garcia W. Non-productive adsorption of bacterial β-glucosidases on lignins is electrostatically modulated and depends on the presence offibronection type III-like domain [Internet]. Enzyme and Microbial Technology. 2016 ; 87-88 1-8.[citado 2024 ago. 22 ] Available from: https://doi.org/10.1016/j.enzmictec.2016.02.007

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