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  • Source: Colloids and Surfaces B: Biointerfaces. Unidades: IQSC, IFSC

    Assunto: QUITOSANA

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    • ABNT

      JOCHELAVICIUS, Karen et al. Chitosan effects on monolayers of zwitterionic, anionic and a natural lipid extract from E. coli at physiological pH. Colloids and Surfaces B: Biointerfaces, v. 209, n. Ja 2022, p. 112146-1-112146-8, 2022Tradução . . Disponível em: https://doi.org/10.1016/j.colsurfb.2021.112146. Acesso em: 27 jun. 2024.
    • APA

      Jochelavicius, K., Pereira, A. R., Fiamingo, A., Nobre, T. M., Campana Filho, S. P., & Oliveira Junior, O. N. de. (2022). Chitosan effects on monolayers of zwitterionic, anionic and a natural lipid extract from E. coli at physiological pH. Colloids and Surfaces B: Biointerfaces, 209( Ja 2022), 112146-1-112146-8. doi:10.1016/j.colsurfb.2021.112146
    • NLM

      Jochelavicius K, Pereira AR, Fiamingo A, Nobre TM, Campana Filho SP, Oliveira Junior ON de. Chitosan effects on monolayers of zwitterionic, anionic and a natural lipid extract from E. coli at physiological pH [Internet]. Colloids and Surfaces B: Biointerfaces. 2022 ; 209( Ja 2022): 112146-1-112146-8.[citado 2024 jun. 27 ] Available from: https://doi.org/10.1016/j.colsurfb.2021.112146
    • Vancouver

      Jochelavicius K, Pereira AR, Fiamingo A, Nobre TM, Campana Filho SP, Oliveira Junior ON de. Chitosan effects on monolayers of zwitterionic, anionic and a natural lipid extract from E. coli at physiological pH [Internet]. Colloids and Surfaces B: Biointerfaces. 2022 ; 209( Ja 2022): 112146-1-112146-8.[citado 2024 jun. 27 ] Available from: https://doi.org/10.1016/j.colsurfb.2021.112146
  • Source: Virology. Unidade: IFSC

    Subjects: DENGUE, FILMES FINOS, SENSORES BIOMÉDICOS, NANOTECNOLOGIA

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    • ABNT

      CESPEDES, Graziely F. et al. On the role of surrounding regions in the fusion peptide in dengue virus infection. Virology, v. 557, p. 62-69, 2021Tradução . . Disponível em: https://doi.org/10.1016/j.virol.2021.02.012. Acesso em: 27 jun. 2024.
    • APA

      Cespedes, G. F., Nobre, T. M., Oliveira Junior, O. N. de, Bong, D., & Cilli, E. M. (2021). On the role of surrounding regions in the fusion peptide in dengue virus infection. Virology, 557, 62-69. doi:10.1016/j.virol.2021.02.012
    • NLM

      Cespedes GF, Nobre TM, Oliveira Junior ON de, Bong D, Cilli EM. On the role of surrounding regions in the fusion peptide in dengue virus infection [Internet]. Virology. 2021 ; 557 62-69.[citado 2024 jun. 27 ] Available from: https://doi.org/10.1016/j.virol.2021.02.012
    • Vancouver

      Cespedes GF, Nobre TM, Oliveira Junior ON de, Bong D, Cilli EM. On the role of surrounding regions in the fusion peptide in dengue virus infection [Internet]. Virology. 2021 ; 557 62-69.[citado 2024 jun. 27 ] Available from: https://doi.org/10.1016/j.virol.2021.02.012
  • Source: Chemistry and Physics of Lipids. Unidade: IFSC

    Subjects: FILMES FINOS, NEOPLASIAS, NANOTECNOLOGIA, MEMBRANA PLASMÁTICA

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    • ABNT

      SANDRINO, Bianca et al. The prion fragment PrP106-127 adopts a secondary structure typical of aggregated fibrils in langmuir monolayers of brain lipid extract. Chemistry and Physics of Lipids, v. 230, p. 104930-1-104930-7, 2020Tradução . . Disponível em: https://doi.org/10.1016/j.chemphyslip.2020.104930. Acesso em: 27 jun. 2024.
    • APA

      Sandrino, B., Jochelavicius, K., Volpati, D., Barbosa, S. C., Nobre, T. M., & Oliveira Junior, O. N. de. (2020). The prion fragment PrP106-127 adopts a secondary structure typical of aggregated fibrils in langmuir monolayers of brain lipid extract. Chemistry and Physics of Lipids, 230, 104930-1-104930-7. doi:10.1016/j.chemphyslip.2020.104930
    • NLM

      Sandrino B, Jochelavicius K, Volpati D, Barbosa SC, Nobre TM, Oliveira Junior ON de. The prion fragment PrP106-127 adopts a secondary structure typical of aggregated fibrils in langmuir monolayers of brain lipid extract [Internet]. Chemistry and Physics of Lipids. 2020 ; 230 104930-1-104930-7.[citado 2024 jun. 27 ] Available from: https://doi.org/10.1016/j.chemphyslip.2020.104930
    • Vancouver

      Sandrino B, Jochelavicius K, Volpati D, Barbosa SC, Nobre TM, Oliveira Junior ON de. The prion fragment PrP106-127 adopts a secondary structure typical of aggregated fibrils in langmuir monolayers of brain lipid extract [Internet]. Chemistry and Physics of Lipids. 2020 ; 230 104930-1-104930-7.[citado 2024 jun. 27 ] Available from: https://doi.org/10.1016/j.chemphyslip.2020.104930
  • Source: ACS Infectious Diseases. Unidade: IFSC

    Subjects: BACTÉRIAS GRAM-NEGATIVAS, RESISTÊNCIA MICROBIANA ÀS DROGAS, PEPTÍDEOS

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    • ABNT

      MARTYNOWYCZ, Michael W. et al. Salmonella membrane structural remodeling increases resistance to antimicrobial peptide LL-37. ACS Infectious Diseases, v. 5, n. 7, p. 1214-1222, 2019Tradução . . Disponível em: https://doi.org/10.1021/acsinfecdis.9b00066. Acesso em: 27 jun. 2024.
    • APA

      Martynowycz, M. W., Rice, A., Andreev, K., Nobre, T. M., Kuzmenko, I., Wereszczynski, J., & Gidalevitz, D. (2019). Salmonella membrane structural remodeling increases resistance to antimicrobial peptide LL-37. ACS Infectious Diseases, 5( 7), 1214-1222. doi:10.1021/acsinfecdis.9b00066
    • NLM

      Martynowycz MW, Rice A, Andreev K, Nobre TM, Kuzmenko I, Wereszczynski J, Gidalevitz D. Salmonella membrane structural remodeling increases resistance to antimicrobial peptide LL-37 [Internet]. ACS Infectious Diseases. 2019 ; 5( 7): 1214-1222.[citado 2024 jun. 27 ] Available from: https://doi.org/10.1021/acsinfecdis.9b00066
    • Vancouver

      Martynowycz MW, Rice A, Andreev K, Nobre TM, Kuzmenko I, Wereszczynski J, Gidalevitz D. Salmonella membrane structural remodeling increases resistance to antimicrobial peptide LL-37 [Internet]. ACS Infectious Diseases. 2019 ; 5( 7): 1214-1222.[citado 2024 jun. 27 ] Available from: https://doi.org/10.1021/acsinfecdis.9b00066

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