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  • Source: Biophysical Journal. Unidade: IF

    Subjects: BIOFÍSICA, FÍSICO-QUÍMICA, MEMBRANAS CELULARES, LIPÍDEOS DA MEMBRANA, CURVATURA CONSTANTE, PROGRAMAÇÃO MATEMÁTICA, SIMULAÇÃO DE SISTEMAS

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      SANTOS, Denys e COUTINHO, Kaline Rabelo e SOARES, Thereza A. A look at membrane curvature and remodeling with SuAVE — Surface Assessment Via grid Evaluation. Biophysical Journal, v. 121, n. 3, p. 6-6, 2022Tradução . . Disponível em: https://doi.org/10.1016/j.bpj.2021.11.2674. Acesso em: 08 ago. 2024.
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      Santos, D., Coutinho, K. R., & Soares, T. A. (2022). A look at membrane curvature and remodeling with SuAVE — Surface Assessment Via grid Evaluation. Biophysical Journal, 121( 3), 6-6. doi:10.1016/j.bpj.2021.11.2674
    • NLM

      Santos D, Coutinho KR, Soares TA. A look at membrane curvature and remodeling with SuAVE — Surface Assessment Via grid Evaluation [Internet]. Biophysical Journal. 2022 ; 121( 3): 6-6.[citado 2024 ago. 08 ] Available from: https://doi.org/10.1016/j.bpj.2021.11.2674
    • Vancouver

      Santos D, Coutinho KR, Soares TA. A look at membrane curvature and remodeling with SuAVE — Surface Assessment Via grid Evaluation [Internet]. Biophysical Journal. 2022 ; 121( 3): 6-6.[citado 2024 ago. 08 ] Available from: https://doi.org/10.1016/j.bpj.2021.11.2674
  • Source: Biophysical Journal. Conference titles: Annual Meeting of the Biophysical Society. Unidade: IF

    Subjects: PEPTÍDEOS, PROTEÍNAS (ESTUDO)

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      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: 08 ago. 2024. , 2014
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      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 ago. 08 ] 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 ago. 08 ] 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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      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: 08 ago. 2024. , 2014
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      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 ago. 08 ] 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 ago. 08 ] 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: 08 ago. 2024. , 2014
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      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 ago. 08 ] 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 ago. 08 ] 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: 08 ago. 2024. , 2014
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      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 ago. 08 ] 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 ago. 08 ] 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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      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: 08 ago. 2024. , 2012
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      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 ago. 08 ] 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 ago. 08 ] Available from: https://doi.org/10.1016/j.bpj.2011.11.2087
  • Source: Biophysical Journal. Unidades: IF, FFCLRP

    Assunto: RAIOS X

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      BARBOSA, Leandro R. S. et al. On the Interaction of Large Amounts of C12E8 on 'NA',K-ATPase Alpha Subunits: A Small Angle X-Ray Scattering Study. Biophysical Journal, v. fe2011, n. 3, p. 382a, 2011Tradução . . Disponível em: https://doi.org/10.1016/j.bpj.2010.12.2276. Acesso em: 08 ago. 2024.
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      Barbosa, L. R. S., Rigos, C. F., Sakamoto, J. Y., Itri, R., & Ciancaglini, P. (2011). On the Interaction of Large Amounts of C12E8 on 'NA',K-ATPase Alpha Subunits: A Small Angle X-Ray Scattering Study. Biophysical Journal, fe2011( 3), 382a. doi:10.1016/j.bpj.2010.12.2276
    • NLM

      Barbosa LRS, Rigos CF, Sakamoto JY, Itri R, Ciancaglini P. On the Interaction of Large Amounts of C12E8 on 'NA',K-ATPase Alpha Subunits: A Small Angle X-Ray Scattering Study [Internet]. Biophysical Journal. 2011 ; fe2011( 3): 382a.[citado 2024 ago. 08 ] Available from: https://doi.org/10.1016/j.bpj.2010.12.2276
    • Vancouver

      Barbosa LRS, Rigos CF, Sakamoto JY, Itri R, Ciancaglini P. On the Interaction of Large Amounts of C12E8 on 'NA',K-ATPase Alpha Subunits: A Small Angle X-Ray Scattering Study [Internet]. Biophysical Journal. 2011 ; fe2011( 3): 382a.[citado 2024 ago. 08 ] Available from: https://doi.org/10.1016/j.bpj.2010.12.2276
  • Source: Biophysical Journal. Unidades: FFCLRP, IF

    Assunto: BIOFÍSICA

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      FERNANDEZ, Roberto Morato et al. Peptide-lipid interaction minitored by spin labeled biologically active melanocortin peptides. Biophysical Journal. Bethesda: Biophysical Society. . Acesso em: 08 ago. 2024. , 2005
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      Fernandez, R. M., Vieira, R. de F. F., Nakaie, C. R., Ito, A. S., & Lamy, M. T. M. (2005). Peptide-lipid interaction minitored by spin labeled biologically active melanocortin peptides. Biophysical Journal. Bethesda: Biophysical Society.
    • NLM

      Fernandez RM, Vieira R de FF, Nakaie CR, Ito AS, Lamy MTM. Peptide-lipid interaction minitored by spin labeled biologically active melanocortin peptides. Biophysical Journal. 2005 ; 88( 1): 578A.[citado 2024 ago. 08 ]
    • Vancouver

      Fernandez RM, Vieira R de FF, Nakaie CR, Ito AS, Lamy MTM. Peptide-lipid interaction minitored by spin labeled biologically active melanocortin peptides. Biophysical Journal. 2005 ; 88( 1): 578A.[citado 2024 ago. 08 ]
  • Source: Biophysical Journal. Unidade: IF

    Subjects: BIOFÍSICA, ÁGUA

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      RISKE, Karin do Amaral et al. Mesoscopic structure in the chain-melting regime of anionic phospholipid vesicles: DMPG. Biophysical Journal, v. 86, n. 6, p. 3722-3733, 2004Tradução . . Disponível em: http://intl.biophysj.org/cgi/reprint/86/6/3722. Acesso em: 08 ago. 2024.
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      Riske, K. do A., Amaral, L. Q. do, Dobereiner, H. G., & Lamy, M. T. M. (2004). Mesoscopic structure in the chain-melting regime of anionic phospholipid vesicles: DMPG. Biophysical Journal, 86( 6), 3722-3733. Recuperado de http://intl.biophysj.org/cgi/reprint/86/6/3722
    • NLM

      Riske K do A, Amaral LQ do, Dobereiner HG, Lamy MTM. Mesoscopic structure in the chain-melting regime of anionic phospholipid vesicles: DMPG [Internet]. Biophysical Journal. 2004 ; 86( 6): 3722-3733.[citado 2024 ago. 08 ] Available from: http://intl.biophysj.org/cgi/reprint/86/6/3722
    • Vancouver

      Riske K do A, Amaral LQ do, Dobereiner HG, Lamy MTM. Mesoscopic structure in the chain-melting regime of anionic phospholipid vesicles: DMPG [Internet]. Biophysical Journal. 2004 ; 86( 6): 3722-3733.[citado 2024 ago. 08 ] Available from: http://intl.biophysj.org/cgi/reprint/86/6/3722
  • Source: Biophysical Journal. Unidade: IF

    Assunto: BIOFÍSICA

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      BENATTI, Carlos Roberto e RUYSSCHAERT, J M e LAMY, Maria Teresa Moura. Structural characterization of pH-sensitive cationic aggregates formed by the synthetic lipid diC(14)-amidine used for transfection. Biophysical Journal, 2004Tradução . . Acesso em: 08 ago. 2024.
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      Benatti, C. R., Ruysschaert, J. M., & Lamy, M. T. M. (2004). Structural characterization of pH-sensitive cationic aggregates formed by the synthetic lipid diC(14)-amidine used for transfection. Biophysical Journal.
    • NLM

      Benatti CR, Ruysschaert JM, Lamy MTM. Structural characterization of pH-sensitive cationic aggregates formed by the synthetic lipid diC(14)-amidine used for transfection. Biophysical Journal. 2004 ;[citado 2024 ago. 08 ]
    • Vancouver

      Benatti CR, Ruysschaert JM, Lamy MTM. Structural characterization of pH-sensitive cationic aggregates formed by the synthetic lipid diC(14)-amidine used for transfection. Biophysical Journal. 2004 ;[citado 2024 ago. 08 ]
  • Source: Biophysical Journal. Unidade: IF

    Subjects: BIOFÍSICA, HORMÔNIOS, MOLÉCULA, ÁCIDOS

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      ITO, Amando S. et al. Fluorescence study of conformational properties of melanotropins labeled with aminobenzoic acid. Biophysical Journal, v. 81, n. 2, p. 1180-1189, 2001Tradução . . Disponível em: http://www.biophysj.org/cgi/reprint/81/2/1180.pdf. Acesso em: 08 ago. 2024.
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      Ito, A. S., Souza, E. S. de, Barbosa, S. dos R., & Nakaie, C. R. (2001). Fluorescence study of conformational properties of melanotropins labeled with aminobenzoic acid. Biophysical Journal, 81( 2), 1180-1189. Recuperado de http://www.biophysj.org/cgi/reprint/81/2/1180.pdf
    • NLM

      Ito AS, Souza ES de, Barbosa S dos R, Nakaie CR. Fluorescence study of conformational properties of melanotropins labeled with aminobenzoic acid [Internet]. Biophysical Journal. 2001 ; 81( 2): 1180-1189.[citado 2024 ago. 08 ] Available from: http://www.biophysj.org/cgi/reprint/81/2/1180.pdf
    • Vancouver

      Ito AS, Souza ES de, Barbosa S dos R, Nakaie CR. Fluorescence study of conformational properties of melanotropins labeled with aminobenzoic acid [Internet]. Biophysical Journal. 2001 ; 81( 2): 1180-1189.[citado 2024 ago. 08 ] Available from: http://www.biophysj.org/cgi/reprint/81/2/1180.pdf
  • Source: Biophysical Journal. Unidade: IF

    Assunto: BIOFÍSICA

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      TURCHIELLO, R. F. et al. A spin label comparative study of the interaction of bradykinin and related peptides with lipid vesicles. Biophysical Journal, v. 76, n. 1, p. A217, 1999Tradução . . Acesso em: 08 ago. 2024.
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      Turchiello, R. F., Riske, K. do A., Juliano, L., Ito, A. S., & Lamy, M. T. M. (1999). A spin label comparative study of the interaction of bradykinin and related peptides with lipid vesicles. Biophysical Journal, 76( 1), A217.
    • NLM

      Turchiello RF, Riske K do A, Juliano L, Ito AS, Lamy MTM. A spin label comparative study of the interaction of bradykinin and related peptides with lipid vesicles. Biophysical Journal. 1999 ; 76( 1): A217.[citado 2024 ago. 08 ]
    • Vancouver

      Turchiello RF, Riske K do A, Juliano L, Ito AS, Lamy MTM. A spin label comparative study of the interaction of bradykinin and related peptides with lipid vesicles. Biophysical Journal. 1999 ; 76( 1): A217.[citado 2024 ago. 08 ]
  • 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: 08 ago. 2024. , 1998
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      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 ago. 08 ]
    • 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 ago. 08 ]
  • Source: Biophysical Journal. Unidades: IQ, IF

    Assunto: BIOQUÍMICA

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      RISKE, K A et al. Temperature and ionic strength dependent suface ionization in DMPG liposomes. Biophysical Journal, v. 72, p. TH223-33, 1997Tradução . . Acesso em: 08 ago. 2024.
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      Riske, K. A., Politi, M. J., Reed, W. F., & Lamy, M. T. M. (1997). Temperature and ionic strength dependent suface ionization in DMPG liposomes. Biophysical Journal, 72, TH223-33.
    • NLM

      Riske KA, Politi MJ, Reed WF, Lamy MTM. Temperature and ionic strength dependent suface ionization in DMPG liposomes. Biophysical Journal. 1997 ; 72 TH223-33.[citado 2024 ago. 08 ]
    • Vancouver

      Riske KA, Politi MJ, Reed WF, Lamy MTM. Temperature and ionic strength dependent suface ionization in DMPG liposomes. Biophysical Journal. 1997 ; 72 TH223-33.[citado 2024 ago. 08 ]
  • Source: Biophysical Journal. Conference titles: Annual Meeting Biophysical Society. Unidade: IF

    Assunto: BIOFÍSICA

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      RISKE, K A et al. Localizing melanotropic peptides in phospholipid bilayers , spin label and fluorescence studies. Biophysical Journal. New York: Instituto de Física, Universidade de São Paulo. . Acesso em: 08 ago. 2024. , 1995
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      Riske, K. A., Macedo, Z. S., Biaggi, M. H., Furquim, M. H., Ito, A. S., & Lamy, M. T. M. (1995). Localizing melanotropic peptides in phospholipid bilayers , spin label and fluorescence studies. Biophysical Journal. New York: Instituto de Física, Universidade de São Paulo.
    • NLM

      Riske KA, Macedo ZS, Biaggi MH, Furquim MH, Ito AS, Lamy MTM. Localizing melanotropic peptides in phospholipid bilayers , spin label and fluorescence studies. Biophysical Journal. 1995 ;a433 68.[citado 2024 ago. 08 ]
    • Vancouver

      Riske KA, Macedo ZS, Biaggi MH, Furquim MH, Ito AS, Lamy MTM. Localizing melanotropic peptides in phospholipid bilayers , spin label and fluorescence studies. Biophysical Journal. 1995 ;a433 68.[citado 2024 ago. 08 ]
  • Source: Biophysical Journal. Unidade: IF

    Assunto: BIOFÍSICA

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      GOLDMAN, C et al. Contribution of electron transfer reaction to the quenching of tryptophan fluorescence. Biophysical Journal, v. 68, n. 2 , p. a191, 1995Tradução . . Acesso em: 08 ago. 2024.
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      Goldman, C., Pascutti, P. G., Piquini, P., & Ito, A. S. (1995). Contribution of electron transfer reaction to the quenching of tryptophan fluorescence. Biophysical Journal, 68( 2 ), a191.
    • NLM

      Goldman C, Pascutti PG, Piquini P, Ito AS. Contribution of electron transfer reaction to the quenching of tryptophan fluorescence. Biophysical Journal. 1995 ;68( 2 ): a191.[citado 2024 ago. 08 ]
    • Vancouver

      Goldman C, Pascutti PG, Piquini P, Ito AS. Contribution of electron transfer reaction to the quenching of tryptophan fluorescence. Biophysical Journal. 1995 ;68( 2 ): a191.[citado 2024 ago. 08 ]
  • Source: Biophysical Journal. Unidade: IF

    Assunto: BIOFÍSICA

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      ITO, Amando S. e SZABO, A G. Structures of melanotropin peptides in model lipid by tryptophan fluorescence. Biophysical Journal, v. 64, n. 2 , p. a161, 1993Tradução . . Acesso em: 08 ago. 2024.
    • APA

      Ito, A. S., & Szabo, A. G. (1993). Structures of melanotropin peptides in model lipid by tryptophan fluorescence. Biophysical Journal, 64( 2 ), a161.
    • NLM

      Ito AS, Szabo AG. Structures of melanotropin peptides in model lipid by tryptophan fluorescence. Biophysical Journal. 1993 ;64( 2 ): a161.[citado 2024 ago. 08 ]
    • Vancouver

      Ito AS, Szabo AG. Structures of melanotropin peptides in model lipid by tryptophan fluorescence. Biophysical Journal. 1993 ;64( 2 ): a161.[citado 2024 ago. 08 ]

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