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  • Source: European Biophysics Journal. Conference titles: European Biophysics Congress - EBSA. Unidades: IFSC, IF

    Subjects: PROTEÍNAS, TERMODINÂMICA, CRISTALOGRAFIA

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    • ABNT

      KUMAGAI, Patricia Suemy et al. Physiological septin-septin interactions prevents amyloid filaments formation. European Biophysics Journal. Heidelberg: Springer. Disponível em: https://doi.org/10.1007/s00249-019-01373-4. Acesso em: 08 set. 2024. , 2019
    • APA

      Kumagai, P. S., Martins, C. S., Sales, E. M., Itri, R., & Araújo, A. P. U. de. (2019). Physiological septin-septin interactions prevents amyloid filaments formation. European Biophysics Journal. Heidelberg: Springer. doi:10.1007/s00249-019-01373-4
    • NLM

      Kumagai PS, Martins CS, Sales EM, Itri R, Araújo APU de. Physiological septin-septin interactions prevents amyloid filaments formation [Internet]. European Biophysics Journal. 2019 ; 48 S149.[citado 2024 set. 08 ] Available from: https://doi.org/10.1007/s00249-019-01373-4
    • Vancouver

      Kumagai PS, Martins CS, Sales EM, Itri R, Araújo APU de. Physiological septin-septin interactions prevents amyloid filaments formation [Internet]. European Biophysics Journal. 2019 ; 48 S149.[citado 2024 set. 08 ] Available from: https://doi.org/10.1007/s00249-019-01373-4
  • Source: European Biophysics Journal. Unidades: IF, IFSC

    Subjects: PEPTÍDEOS, AGENTES ANTIMICROBIANOS

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    • ABNT

      KUMAGAI, Patricia Suemy et al. Unveiling the binding and orientation of the antimicrobial peptide Plantaricin 149 in zwitterionic and negatively charged membranes. European Biophysics Journal, v. 48, n. 7, p. 621-633, 2019Tradução . . Disponível em: https://doi.org/10.1007/s00249-019-01387-y. Acesso em: 08 set. 2024.
    • APA

      Kumagai, P. S., Sousa, V. K. de, Donato, M., Itri, R., Beltramini, L. M., Araújo, A. P. U. de, et al. (2019). Unveiling the binding and orientation of the antimicrobial peptide Plantaricin 149 in zwitterionic and negatively charged membranes. European Biophysics Journal, 48( 7), 621-633. doi:10.1007/s00249-019-01387-y
    • NLM

      Kumagai PS, Sousa VK de, Donato M, Itri R, Beltramini LM, Araújo APU de, Buerck J, Wallace BA, Lopes JLS. Unveiling the binding and orientation of the antimicrobial peptide Plantaricin 149 in zwitterionic and negatively charged membranes [Internet]. European Biophysics Journal. 2019 ; 48( 7): 621-633.[citado 2024 set. 08 ] Available from: https://doi.org/10.1007/s00249-019-01387-y
    • Vancouver

      Kumagai PS, Sousa VK de, Donato M, Itri R, Beltramini LM, Araújo APU de, Buerck J, Wallace BA, Lopes JLS. Unveiling the binding and orientation of the antimicrobial peptide Plantaricin 149 in zwitterionic and negatively charged membranes [Internet]. European Biophysics Journal. 2019 ; 48( 7): 621-633.[citado 2024 set. 08 ] Available from: https://doi.org/10.1007/s00249-019-01387-y
  • Source: European Biophysics Journal. Unidades: IFSC, IF

    Subjects: PROTEÍNAS, CRISTALOGRAFIA, MEMBRANAS CELULARES

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    • ABNT

      KUMAGAI, Patricia S. e DE MARCO, Ricardo e LOPES, José luiz de Souza. Advantages of synchrotron radiation circular dichroism spectroscopy to study intrinsically disordered proteins. European Biophysics Journal, v. 46, n. 7, p. 599-606, 2017Tradução . . Disponível em: https://doi.org/10.1007/s00249-017-1202-1. Acesso em: 08 set. 2024.
    • APA

      Kumagai, P. S., De Marco, R., & Lopes, J. luiz de S. (2017). Advantages of synchrotron radiation circular dichroism spectroscopy to study intrinsically disordered proteins. European Biophysics Journal, 46( 7), 599-606. doi:10.1007/s00249-017-1202-1
    • NLM

      Kumagai PS, De Marco R, Lopes J luiz de S. Advantages of synchrotron radiation circular dichroism spectroscopy to study intrinsically disordered proteins [Internet]. European Biophysics Journal. 2017 ; 46( 7): 599-606.[citado 2024 set. 08 ] Available from: https://doi.org/10.1007/s00249-017-1202-1
    • Vancouver

      Kumagai PS, De Marco R, Lopes J luiz de S. Advantages of synchrotron radiation circular dichroism spectroscopy to study intrinsically disordered proteins [Internet]. European Biophysics Journal. 2017 ; 46( 7): 599-606.[citado 2024 set. 08 ] Available from: https://doi.org/10.1007/s00249-017-1202-1
  • Source: Biophysical Reviews. Unidades: IFSC, IF

    Subjects: ESPECTROSCOPIA, PROTEÍNAS

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    • ABNT

      KUMAGAI, Patricia S. e ARAÚJO, Ana Paula Ulian de e LOPES, José Luiz de Souza. Going deep into protein secondary structure with synchrotron radiation circular dichroism spectroscopy. Biophysical Reviews, v. 9, n. 5, p. 517-527, 2017Tradução . . Disponível em: https://doi.org/10.1007/s12551-017-0314-2. Acesso em: 08 set. 2024.
    • APA

      Kumagai, P. S., Araújo, A. P. U. de, & Lopes, J. L. de S. (2017). Going deep into protein secondary structure with synchrotron radiation circular dichroism spectroscopy. Biophysical Reviews, 9( 5), 517-527. doi:10.1007/s12551-017-0314-2
    • NLM

      Kumagai PS, Araújo APU de, Lopes JL de S. Going deep into protein secondary structure with synchrotron radiation circular dichroism spectroscopy [Internet]. Biophysical Reviews. 2017 ; 9( 5): 517-527.[citado 2024 set. 08 ] Available from: https://doi.org/10.1007/s12551-017-0314-2
    • Vancouver

      Kumagai PS, Araújo APU de, Lopes JL de S. Going deep into protein secondary structure with synchrotron radiation circular dichroism spectroscopy [Internet]. Biophysical Reviews. 2017 ; 9( 5): 517-527.[citado 2024 set. 08 ] Available from: https://doi.org/10.1007/s12551-017-0314-2
  • Source: European Biophysics Journal. Conference titles: European Biophysics Congress - EBSA. Unidades: IFSC, IF

    Subjects: PROTEÍNAS, TERMODINÂMICA, CRISTALOGRAFIA

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    • ABNT

      ORTORE, M. G. et al. Septin 3 aggregation in solution: thermodynamic and structural characterization. European Biophysics Journal. Heidelberg: Springer. Disponível em: https://doi.org/10.1007/s00249-015-1045-6. Acesso em: 08 set. 2024. , 2015
    • APA

      Ortore, M. G., Macedo, J. N. A., Araújo, A. P. U. de, Ferrero, C., Mariani, P., Spinozzi, F., & Itri, R. (2015). Septin 3 aggregation in solution: thermodynamic and structural characterization. European Biophysics Journal. Heidelberg: Springer. doi:10.1007/s00249-015-1045-6
    • NLM

      Ortore MG, Macedo JNA, Araújo APU de, Ferrero C, Mariani P, Spinozzi F, Itri R. Septin 3 aggregation in solution: thermodynamic and structural characterization [Internet]. European Biophysics Journal. 2015 ; 44 S208.[citado 2024 set. 08 ] Available from: https://doi.org/10.1007/s00249-015-1045-6
    • Vancouver

      Ortore MG, Macedo JNA, Araújo APU de, Ferrero C, Mariani P, Spinozzi F, Itri R. Septin 3 aggregation in solution: thermodynamic and structural characterization [Internet]. European Biophysics Journal. 2015 ; 44 S208.[citado 2024 set. 08 ] Available from: https://doi.org/10.1007/s00249-015-1045-6
  • Source: European Biophysics Journal. Conference titles: European Biophysics Congress. Unidades: IFSC, IF

    Subjects: BIOFÍSICA, DIFRAÇÃO POR RAIOS X

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    • ABNT

      CAMARGO, A I et al. Structural analysis of two centrins from fungi B. Emersoni by AMF and SAXS. European Biophysics Journal. Berlin: Springer. Disponível em: http://www.springerlink.com/content/tut763t6375w/?p=fcc06efe22c34885b71b856c23249384&pi=14. Acesso em: 08 set. 2024. , 2009
    • APA

      Camargo, A. I., Barbosa, L. R. S., Itri, R., & Beltramini, L. M. (2009). Structural analysis of two centrins from fungi B. Emersoni by AMF and SAXS. European Biophysics Journal. Berlin: Springer. Recuperado de http://www.springerlink.com/content/tut763t6375w/?p=fcc06efe22c34885b71b856c23249384&pi=14
    • NLM

      Camargo AI, Barbosa LRS, Itri R, Beltramini LM. Structural analysis of two centrins from fungi B. Emersoni by AMF and SAXS [Internet]. European Biophysics Journal. 2009 ; 39 1.[citado 2024 set. 08 ] Available from: http://www.springerlink.com/content/tut763t6375w/?p=fcc06efe22c34885b71b856c23249384&pi=14
    • Vancouver

      Camargo AI, Barbosa LRS, Itri R, Beltramini LM. Structural analysis of two centrins from fungi B. Emersoni by AMF and SAXS [Internet]. European Biophysics Journal. 2009 ; 39 1.[citado 2024 set. 08 ] Available from: http://www.springerlink.com/content/tut763t6375w/?p=fcc06efe22c34885b71b856c23249384&pi=14

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