Filtros : "IF-FGE" "Annual Meeting of the Biophysical Society" Removidos: "FÍSICA DE ALTA ENERGIA" "Department of Physics and Astronomy, Stony Brook University, New York, USA" Limpar

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  • Source: Biophysical Journal. Conference titles: Annual Meeting of the Biophysical Society. Unidade: IF

    Subjects: PEPTÍDEOS, PROTEÍNAS (ESTUDO)

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    • ABNT

      ENOKI, Thais Azevedo et al. The interaction between the antimicrobial peptide K-Hya1 and model membranes: distinct action in neutral or negatively charged bilayers. Biophysical Journal. Saint Louis: Cell Press. Disponível em: http://www.cell.com/biophysj/abstract/S0006-3495(13)01778-5. Acesso em: 12 jul. 2024. , 2014
    • APA

      Enoki, T. A., Riske, K. A., Perez, K. R., Lorenzon, E. N., Cilli, E. M., & Lamy, M. T. M. (2014). The interaction between the antimicrobial peptide K-Hya1 and model membranes: distinct action in neutral or negatively charged bilayers. Biophysical Journal. Saint Louis: Cell Press. Recuperado de http://www.cell.com/biophysj/abstract/S0006-3495(13)01778-5
    • NLM

      Enoki TA, Riske KA, Perez KR, Lorenzon EN, Cilli EM, Lamy MTM. The interaction between the antimicrobial peptide K-Hya1 and model membranes: distinct action in neutral or negatively charged bilayers [Internet]. Biophysical Journal. 2014 ; 106( ja 2014): 85A.[citado 2024 jul. 12 ] Available from: http://www.cell.com/biophysj/abstract/S0006-3495(13)01778-5
    • Vancouver

      Enoki TA, Riske KA, Perez KR, Lorenzon EN, Cilli EM, Lamy MTM. The interaction between the antimicrobial peptide K-Hya1 and model membranes: distinct action in neutral or negatively charged bilayers [Internet]. Biophysical Journal. 2014 ; 106( ja 2014): 85A.[citado 2024 jul. 12 ] Available from: http://www.cell.com/biophysj/abstract/S0006-3495(13)01778-5
  • Source: Biophysical Journal. Conference titles: Annual Meeting of the Biophysical Society. Unidade: IF

    Subjects: PEPTÍDEOS, PROTEÍNAS (ESTUDO)

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    • ABNT

      ITRI, Rosangela et al. Unraveling the heparin-induced protofibril structure of GAPDH. Biophysical Journal. Saint Louis: Cell Press. Disponível em: http://www.cell.com/biophysj/comments/S0006-3495(13)03434-6. Acesso em: 12 jul. 2024. , 2014
    • APA

      Itri, R., Torres-Bugeau, C. M., Avila, C. L., Chehin, R. N., Sales, E. M., & Barbosa, L. R. S. (2014). Unraveling the heparin-induced protofibril structure of GAPDH. Biophysical Journal. Saint Louis: Cell Press. Recuperado de http://www.cell.com/biophysj/comments/S0006-3495(13)03434-6
    • NLM

      Itri R, Torres-Bugeau CM, Avila CL, Chehin RN, Sales EM, Barbosa LRS. Unraveling the heparin-induced protofibril structure of GAPDH [Internet]. Biophysical Journal. 2014 ; 106( ja 2014): 385A.[citado 2024 jul. 12 ] Available from: http://www.cell.com/biophysj/comments/S0006-3495(13)03434-6
    • Vancouver

      Itri R, Torres-Bugeau CM, Avila CL, Chehin RN, Sales EM, Barbosa LRS. Unraveling the heparin-induced protofibril structure of GAPDH [Internet]. Biophysical Journal. 2014 ; 106( ja 2014): 385A.[citado 2024 jul. 12 ] Available from: http://www.cell.com/biophysj/comments/S0006-3495(13)03434-6
  • Source: Biophysical Journal. Conference titles: Annual Meeting of the Biophysical Society. Unidade: IF

    Subjects: PEPTÍDEOS, PROTEÍNAS (ESTUDO)

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      PELLEGRINA, Diogo V. S. e DUARTE, Evandro Luiz e LAMY, Maria Teresa Moura. Spin labels detect the coexistence of two lipid domains along the anomalous gel-fluid transition of anionic dmpg bilayers. Biophysical Journal. Saint Louis: Cell Press. Disponível em: http://www.cell.com/biophysj/fulltext/S0006-3495(13)04109-X. Acesso em: 12 jul. 2024. , 2014
    • APA

      Pellegrina, D. V. S., Duarte, E. L., & Lamy, M. T. M. (2014). Spin labels detect the coexistence of two lipid domains along the anomalous gel-fluid transition of anionic dmpg bilayers. Biophysical Journal. Saint Louis: Cell Press. Recuperado de http://www.cell.com/biophysj/fulltext/S0006-3495(13)04109-X
    • NLM

      Pellegrina DVS, Duarte EL, Lamy MTM. Spin labels detect the coexistence of two lipid domains along the anomalous gel-fluid transition of anionic dmpg bilayers [Internet]. Biophysical Journal. 2014 ; 106( ja 2014): 510A.[citado 2024 jul. 12 ] Available from: http://www.cell.com/biophysj/fulltext/S0006-3495(13)04109-X
    • Vancouver

      Pellegrina DVS, Duarte EL, Lamy MTM. Spin labels detect the coexistence of two lipid domains along the anomalous gel-fluid transition of anionic dmpg bilayers [Internet]. Biophysical Journal. 2014 ; 106( ja 2014): 510A.[citado 2024 jul. 12 ] Available from: http://www.cell.com/biophysj/fulltext/S0006-3495(13)04109-X
  • Source: Biophysical Journal. Conference titles: Annual Meeting of the Biophysical Society. Unidade: IF

    Subjects: PEPTÍDEOS, PROTEÍNAS (ESTUDO)

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      BARBOSA, Leandro Ramos Souza e BARBOSA, Leandro Ramos Souza. Urea, guanidine hydrocloride and 2,2,2-trifluoroethanol can change the amyloid fibril formation of model proteins: a spectroscopic study. Biophysical Journal. Saint Louis: Cell Press. Disponível em: http://www.cell.com/biophysj/pdf/S0006-3495(13)05028-5.pdf. Acesso em: 12 jul. 2024. , 2014
    • APA

      Barbosa, L. R. S., & Barbosa, L. R. S. (2014). Urea, guanidine hydrocloride and 2,2,2-trifluoroethanol can change the amyloid fibril formation of model proteins: a spectroscopic study. Biophysical Journal. Saint Louis: Cell Press. Recuperado de http://www.cell.com/biophysj/pdf/S0006-3495(13)05028-5.pdf
    • NLM

      Barbosa LRS, Barbosa LRS. Urea, guanidine hydrocloride and 2,2,2-trifluoroethanol can change the amyloid fibril formation of model proteins: a spectroscopic study [Internet]. Biophysical Journal. 2014 ; 106( ja 2014): 681A.[citado 2024 jul. 12 ] Available from: http://www.cell.com/biophysj/pdf/S0006-3495(13)05028-5.pdf
    • Vancouver

      Barbosa LRS, Barbosa LRS. Urea, guanidine hydrocloride and 2,2,2-trifluoroethanol can change the amyloid fibril formation of model proteins: a spectroscopic study [Internet]. Biophysical Journal. 2014 ; 106( ja 2014): 681A.[citado 2024 jul. 12 ] Available from: http://www.cell.com/biophysj/pdf/S0006-3495(13)05028-5.pdf
  • Source: Biophysical Journal. Conference titles: Annual Meeting of the Biophysical Society. Unidades: IF, IFSC

    Subjects: PROTEÍNAS, BIOFÍSICA

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    • ABNT

      ITRI, Rosangela et al. Structural studies of Septin2G amyloid fibrils. Biophysical Journal. Saint Louis: Cell Press. Disponível em: https://doi.org/10.1016/j.bpj.2011.11.2087. Acesso em: 12 jul. 2024. , 2012
    • APA

      Itri, R., Sales, E. M., Damascio, J., Barbosa, L. R. S., Spinozzi, F., Mariani, P., & Araújo, A. P. U. de. (2012). Structural studies of Septin2G amyloid fibrils. Biophysical Journal. Saint Louis: Cell Press. doi:10.1016/j.bpj.2011.11.2087
    • NLM

      Itri R, Sales EM, Damascio J, Barbosa LRS, Spinozzi F, Mariani P, Araújo APU de. Structural studies of Septin2G amyloid fibrils [Internet]. Biophysical Journal. 2012 ; 102( Ja 2012): 381a-382a.[citado 2024 jul. 12 ] Available from: https://doi.org/10.1016/j.bpj.2011.11.2087
    • Vancouver

      Itri R, Sales EM, Damascio J, Barbosa LRS, Spinozzi F, Mariani P, Araújo APU de. Structural studies of Septin2G amyloid fibrils [Internet]. Biophysical Journal. 2012 ; 102( Ja 2012): 381a-382a.[citado 2024 jul. 12 ] Available from: https://doi.org/10.1016/j.bpj.2011.11.2087
  • Source: Biophysical Journal. Conference titles: Annual Meeting of the Biophysical Society. Unidades: IFSC, IF

    Assunto: BIOFÍSICA

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      AMARAL-RISKE, K et al. Characterization of DMPG vesicle surface potential by a charged water soluble spin label. Biophysical Journal. New York: Instituto de Física de São Carlos, Universidade de São Paulo. . Acesso em: 12 jul. 2024. , 1998
    • APA

      Amaral-Riske, K., Nascimento, O. R., Bales, B., & Lamy, M. T. M. (1998). Characterization of DMPG vesicle surface potential by a charged water soluble spin label. Biophysical Journal. New York: Instituto de Física de São Carlos, Universidade de São Paulo.
    • NLM

      Amaral-Riske K, Nascimento OR, Bales B, Lamy MTM. Characterization of DMPG vesicle surface potential by a charged water soluble spin label. Biophysical Journal. 1998 ; 74( 2): A310.[citado 2024 jul. 12 ]
    • Vancouver

      Amaral-Riske K, Nascimento OR, Bales B, Lamy MTM. Characterization of DMPG vesicle surface potential by a charged water soluble spin label. Biophysical Journal. 1998 ; 74( 2): A310.[citado 2024 jul. 12 ]
  • Source: Biophysics. Conference titles: Annual Meeting of the Biophysical Society. Unidade: IF

    Assunto: BIOFÍSICA

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      SHIDA, C S et al. Interaction of the aromatic hormone melatonin with lipid membranes. Biophysics. New Orleans: Instituto de Física, Universidade de São Paulo. . Acesso em: 12 jul. 2024. , 1994
    • APA

      Shida, C. S., Costa, E. X., Ito, A. S., & Lamy, M. T. M. (1994). Interaction of the aromatic hormone melatonin with lipid membranes. Biophysics. New Orleans: Instituto de Física, Universidade de São Paulo.
    • NLM

      Shida CS, Costa EX, Ito AS, Lamy MTM. Interaction of the aromatic hormone melatonin with lipid membranes. Biophysics. 1994 ;66 a57.[citado 2024 jul. 12 ]
    • Vancouver

      Shida CS, Costa EX, Ito AS, Lamy MTM. Interaction of the aromatic hormone melatonin with lipid membranes. Biophysics. 1994 ;66 a57.[citado 2024 jul. 12 ]

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