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  • Source: Biophysical Chemistry. Unidade: IF

    Subjects: BIOFÍSICA, ESPECTROSCOPIA, ESPECTROSCOPIA DE RESSONÂNCIA MAGNÉTICA NUCLEAR

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      CUNHA, Antonio R da et al. New insights into the interaction of emodin with lipid membranes. Biophysical Chemistry, p. 107233/1-107233/9, 2024Tradução . . Disponível em: https://doi.org/10.1016/j.bpc.2024.107233. Acesso em: 27 jun. 2025.
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      Cunha, A. R. da, Duarte, E. L., Muniz, G. S. V., Coutinho, K., & Lamy, T. (2024). New insights into the interaction of emodin with lipid membranes. Biophysical Chemistry, 107233/1-107233/9. doi:10.1016/j.bpc.2024.107233
    • NLM

      Cunha AR da, Duarte EL, Muniz GSV, Coutinho K, Lamy T. New insights into the interaction of emodin with lipid membranes [Internet]. Biophysical Chemistry. 2024 ; 107233/1-107233/9.[citado 2025 jun. 27 ] Available from: https://doi.org/10.1016/j.bpc.2024.107233
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      Cunha AR da, Duarte EL, Muniz GSV, Coutinho K, Lamy T. New insights into the interaction of emodin with lipid membranes [Internet]. Biophysical Chemistry. 2024 ; 107233/1-107233/9.[citado 2025 jun. 27 ] Available from: https://doi.org/10.1016/j.bpc.2024.107233
  • Source: Biophysical Chemistry. Unidade: IFSC

    Subjects: BIOFÍSICA, NANOPARTÍCULAS, NEOPLASIAS MAMÁRIAS, BIOQUÍMICA

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      KOBAL, Mirella Boaro et al. Unveiling the mechanisms underlying photothermal efficiency of gold shell-isolated nanoparticles (AuSHINs) on ductal mammary carcinoma cells (BT-474). Biophysical Chemistry, v. 300, p. 107077-1-107077-9 + supplementary data, 2023Tradução . . Disponível em: https://doi.org/10.1016/j.bpc.2023.107077. Acesso em: 27 jun. 2025.
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      Kobal, M. B., Camacho, S. A., Moreira, L. G., Toledo, K. A. de, Tada, D. B., & Aoki, P. H. B. (2023). Unveiling the mechanisms underlying photothermal efficiency of gold shell-isolated nanoparticles (AuSHINs) on ductal mammary carcinoma cells (BT-474). Biophysical Chemistry, 300, 107077-1-107077-9 + supplementary data. doi:10.1016/j.bpc.2023.107077
    • NLM

      Kobal MB, Camacho SA, Moreira LG, Toledo KA de, Tada DB, Aoki PHB. Unveiling the mechanisms underlying photothermal efficiency of gold shell-isolated nanoparticles (AuSHINs) on ductal mammary carcinoma cells (BT-474) [Internet]. Biophysical Chemistry. 2023 ; 300 107077-1-107077-9 + supplementary data.[citado 2025 jun. 27 ] Available from: https://doi.org/10.1016/j.bpc.2023.107077
    • Vancouver

      Kobal MB, Camacho SA, Moreira LG, Toledo KA de, Tada DB, Aoki PHB. Unveiling the mechanisms underlying photothermal efficiency of gold shell-isolated nanoparticles (AuSHINs) on ductal mammary carcinoma cells (BT-474) [Internet]. Biophysical Chemistry. 2023 ; 300 107077-1-107077-9 + supplementary data.[citado 2025 jun. 27 ] Available from: https://doi.org/10.1016/j.bpc.2023.107077
  • Source: Biophysical Chemistry. Unidade: IF

    Subjects: BIOFÍSICA, BIOQUÍMICA

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      MARTINS, Leticia S. et al. DODAB vesicles containing lysophosphatidylcholines: the relevance of acyl chain saturation on the membrane structure and thermal properties. Biophysical Chemistry, v. 300, 2023Tradução . . Disponível em: https://doi.org/10.1016/j.bpc.2023.107075. Acesso em: 27 jun. 2025.
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      Martins, L. S., Rozenfeld, J. H. K., Duarte, E. L., & Lamy, M. T. M. (2023). DODAB vesicles containing lysophosphatidylcholines: the relevance of acyl chain saturation on the membrane structure and thermal properties. Biophysical Chemistry, 300. doi:10.1016/j.bpc.2023.107075
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      Martins LS, Rozenfeld JHK, Duarte EL, Lamy MTM. DODAB vesicles containing lysophosphatidylcholines: the relevance of acyl chain saturation on the membrane structure and thermal properties [Internet]. Biophysical Chemistry. 2023 ; 300[citado 2025 jun. 27 ] Available from: https://doi.org/10.1016/j.bpc.2023.107075
    • Vancouver

      Martins LS, Rozenfeld JHK, Duarte EL, Lamy MTM. DODAB vesicles containing lysophosphatidylcholines: the relevance of acyl chain saturation on the membrane structure and thermal properties [Internet]. Biophysical Chemistry. 2023 ; 300[citado 2025 jun. 27 ] Available from: https://doi.org/10.1016/j.bpc.2023.107075
  • Source: Biophysical Chemistry. Unidades: IF, IQ

    Subjects: FOTOBIOLOGIA, FOTOQUÍMICA, OXIDAÇÃO, LIPÍDEOS DA MEMBRANA, BIOFÍSICA, BIOQUÍMICA CELULAR, NANOPARTÍCULAS, PERMEABILIDADE DA MEMBRANA CELULAR, MEMBRANAS CELULARES

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      TSUBONE, Tayana Mazin e BAPTISTA, Mauricio da Silva e ITRI, Rosangela. Understanding membrane remodelling initiated by photosensitized lipid oxidation. Biophysical Chemistry, v. 254, 2019Tradução . . Disponível em: https://doi.org/10.1016/j.bpc.2019.106263. Acesso em: 27 jun. 2025.
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      Tsubone, T. M., Baptista, M. da S., & Itri, R. (2019). Understanding membrane remodelling initiated by photosensitized lipid oxidation. Biophysical Chemistry, 254. doi:10.1016/j.bpc.2019.106263
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      Tsubone TM, Baptista M da S, Itri R. Understanding membrane remodelling initiated by photosensitized lipid oxidation [Internet]. Biophysical Chemistry. 2019 ; 254[citado 2025 jun. 27 ] Available from: https://doi.org/10.1016/j.bpc.2019.106263
    • Vancouver

      Tsubone TM, Baptista M da S, Itri R. Understanding membrane remodelling initiated by photosensitized lipid oxidation [Internet]. Biophysical Chemistry. 2019 ; 254[citado 2025 jun. 27 ] Available from: https://doi.org/10.1016/j.bpc.2019.106263
  • Source: Biophysical Chemistry. Unidade: IFSC

    Subjects: POLÍMEROS (MATERIAIS), MEMBRANAS CELULARES

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      LEMMA, Tibebe et al. Disruption of giant unilamellar vesicles mimicking cell membranes induced by the pesticides glyphosate and picloram. Biophysical Chemistry, v. 250, p. 106176-1-106176-9, 2019Tradução . . Disponível em: https://doi.org/10.1016/j.bpc.2019.106176. Acesso em: 27 jun. 2025.
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      Lemma, T., Ruiz, G. C. M., Oliveira Junior, O. N. de, & Constantino, C. J. L. (2019). Disruption of giant unilamellar vesicles mimicking cell membranes induced by the pesticides glyphosate and picloram. Biophysical Chemistry, 250, 106176-1-106176-9. doi:10.1016/j.bpc.2019.106176
    • NLM

      Lemma T, Ruiz GCM, Oliveira Junior ON de, Constantino CJL. Disruption of giant unilamellar vesicles mimicking cell membranes induced by the pesticides glyphosate and picloram [Internet]. Biophysical Chemistry. 2019 ; 250 106176-1-106176-9.[citado 2025 jun. 27 ] Available from: https://doi.org/10.1016/j.bpc.2019.106176
    • Vancouver

      Lemma T, Ruiz GCM, Oliveira Junior ON de, Constantino CJL. Disruption of giant unilamellar vesicles mimicking cell membranes induced by the pesticides glyphosate and picloram [Internet]. Biophysical Chemistry. 2019 ; 250 106176-1-106176-9.[citado 2025 jun. 27 ] Available from: https://doi.org/10.1016/j.bpc.2019.106176
  • Source: Biophysical Chemistry. Unidade: IQ

    Assunto: LISOZIMAS

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      YOSHIHARA, Lucas M. B e ARÊAS, Elizabeth Pinheiro Gomes. Protein/polyelectrolyte coacervation: investigating its occurrence in the lysozyme- carboxymethylcellulose system. Biophysical Chemistry, v. 236, p. 8-14, 2018Tradução . . Disponível em: https://doi.org/10.1016/j.bpc.2018.03.001. Acesso em: 27 jun. 2025.
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      Yoshihara, L. M. B., & Arêas, E. P. G. (2018). Protein/polyelectrolyte coacervation: investigating its occurrence in the lysozyme- carboxymethylcellulose system. Biophysical Chemistry, 236, 8-14. doi:10.1016/j.bpc.2018.03.001
    • NLM

      Yoshihara LMB, Arêas EPG. Protein/polyelectrolyte coacervation: investigating its occurrence in the lysozyme- carboxymethylcellulose system [Internet]. Biophysical Chemistry. 2018 ; 236 8-14.[citado 2025 jun. 27 ] Available from: https://doi.org/10.1016/j.bpc.2018.03.001
    • Vancouver

      Yoshihara LMB, Arêas EPG. Protein/polyelectrolyte coacervation: investigating its occurrence in the lysozyme- carboxymethylcellulose system [Internet]. Biophysical Chemistry. 2018 ; 236 8-14.[citado 2025 jun. 27 ] Available from: https://doi.org/10.1016/j.bpc.2018.03.001
  • Source: Biophysical Chemistry. Unidade: IQ

    Subjects: ADSORÇÃO, PEPTÍDEOS

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      SALAY, Luiz C et al. Adsorption of the antimicrobial peptide tritrpticin onto solid and liquid surfaces: ion-specific effects. Biophysical Chemistry, v. 207, p. 128-134 , 2015Tradução . . Disponível em: https://doi.org/10.1016/j.bpc.2015.10.004. Acesso em: 27 jun. 2025.
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      Salay, L. C., Petri, D. F. S., Nakaie, C. R., & Schreier, S. (2015). Adsorption of the antimicrobial peptide tritrpticin onto solid and liquid surfaces: ion-specific effects. Biophysical Chemistry, 207, 128-134 . doi:10.1016/j.bpc.2015.10.004
    • NLM

      Salay LC, Petri DFS, Nakaie CR, Schreier S. Adsorption of the antimicrobial peptide tritrpticin onto solid and liquid surfaces: ion-specific effects [Internet]. Biophysical Chemistry. 2015 ; 207 128-134 .[citado 2025 jun. 27 ] Available from: https://doi.org/10.1016/j.bpc.2015.10.004
    • Vancouver

      Salay LC, Petri DFS, Nakaie CR, Schreier S. Adsorption of the antimicrobial peptide tritrpticin onto solid and liquid surfaces: ion-specific effects [Internet]. Biophysical Chemistry. 2015 ; 207 128-134 .[citado 2025 jun. 27 ] Available from: https://doi.org/10.1016/j.bpc.2015.10.004
  • Source: Biophysical Chemistry. Unidades: IQSC, IF, IFSC

    Subjects: TRYPANOSOMA CRUZI, CRISTALOGRAFIA

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      MURAKAMI, Mário Tyago et al. Structural studies of the Trypanosoma cruzi Old Yellow Enzyme: insights into enzyme dynamics and specificity. Biophysical Chemistry, v. 184, p. 44-53, 2013Tradução . . Disponível em: https://doi.org/10.1016/j.bpc.2013.08.004. Acesso em: 27 jun. 2025.
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      Murakami, M. T., Rodrigues, N. de C., Gava, L. M., Honorato, R. V., Canduri, F., Barbosa, L. R. S., et al. (2013). Structural studies of the Trypanosoma cruzi Old Yellow Enzyme: insights into enzyme dynamics and specificity. Biophysical Chemistry, 184, 44-53. doi:10.1016/j.bpc.2013.08.004
    • NLM

      Murakami MT, Rodrigues N de C, Gava LM, Honorato RV, Canduri F, Barbosa LRS, Oliva G, Borges JC. Structural studies of the Trypanosoma cruzi Old Yellow Enzyme: insights into enzyme dynamics and specificity [Internet]. Biophysical Chemistry. 2013 ; 184 44-53.[citado 2025 jun. 27 ] Available from: https://doi.org/10.1016/j.bpc.2013.08.004
    • Vancouver

      Murakami MT, Rodrigues N de C, Gava LM, Honorato RV, Canduri F, Barbosa LRS, Oliva G, Borges JC. Structural studies of the Trypanosoma cruzi Old Yellow Enzyme: insights into enzyme dynamics and specificity [Internet]. Biophysical Chemistry. 2013 ; 184 44-53.[citado 2025 jun. 27 ] Available from: https://doi.org/10.1016/j.bpc.2013.08.004
  • Source: Biophysical Chemistry. Unidade: IFSC

    Subjects: BIOTECNOLOGIA, NANOTECNOLOGIA, MEMBRANAS (BIOLOGIA), FILMES FINOS

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      MONTANHA, E. A. et al. Comparative study and liponucleosides in Langmuir monolayers as cell membrane models. Biophysical Chemistry, v. 153, n. Ja 2011, p. 154-158, 2011Tradução . . Disponível em: https://doi.org/10.1016/j.bpc.2010.10.010. Acesso em: 27 jun. 2025.
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      Montanha, E. A., Caseli, L., Kaczmarek, O., Liebscher, J., Huster, D., & Oliveira Junior, O. N. de. (2011). Comparative study and liponucleosides in Langmuir monolayers as cell membrane models. Biophysical Chemistry, 153( Ja 2011), 154-158. doi:10.1016/j.bpc.2010.10.010
    • NLM

      Montanha EA, Caseli L, Kaczmarek O, Liebscher J, Huster D, Oliveira Junior ON de. Comparative study and liponucleosides in Langmuir monolayers as cell membrane models [Internet]. Biophysical Chemistry. 2011 ; 153( Ja 2011): 154-158.[citado 2025 jun. 27 ] Available from: https://doi.org/10.1016/j.bpc.2010.10.010
    • Vancouver

      Montanha EA, Caseli L, Kaczmarek O, Liebscher J, Huster D, Oliveira Junior ON de. Comparative study and liponucleosides in Langmuir monolayers as cell membrane models [Internet]. Biophysical Chemistry. 2011 ; 153( Ja 2011): 154-158.[citado 2025 jun. 27 ] Available from: https://doi.org/10.1016/j.bpc.2010.10.010
  • Source: Biophysical Chemistry. Unidade: IQSC

    Assunto: PROTEÍNAS

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      SANTIAGO, Patricia Soares et al. Thermal stability of extracellular hemoglobin of glossocolex paulistus: determination of activation parameters by optical spectroscopic and differential scanning calorimetric studies. Biophysical Chemistry, v. 152, n. 1-3, p. 128-138, 2010Tradução . . Disponível em: https://doi.org/10.1016/j.bpc.2010.08.010. Acesso em: 27 jun. 2025.
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      Santiago, P. S., Carvalho, J. W. P., Domingues, M. A., Santos, N. C., & Tabak, M. (2010). Thermal stability of extracellular hemoglobin of glossocolex paulistus: determination of activation parameters by optical spectroscopic and differential scanning calorimetric studies. Biophysical Chemistry, 152( 1-3), 128-138. doi:10.1016/j.bpc.2010.08.010
    • NLM

      Santiago PS, Carvalho JWP, Domingues MA, Santos NC, Tabak M. Thermal stability of extracellular hemoglobin of glossocolex paulistus: determination of activation parameters by optical spectroscopic and differential scanning calorimetric studies [Internet]. Biophysical Chemistry. 2010 ; 152( 1-3): 128-138.[citado 2025 jun. 27 ] Available from: https://doi.org/10.1016/j.bpc.2010.08.010
    • Vancouver

      Santiago PS, Carvalho JWP, Domingues MA, Santos NC, Tabak M. Thermal stability of extracellular hemoglobin of glossocolex paulistus: determination of activation parameters by optical spectroscopic and differential scanning calorimetric studies [Internet]. Biophysical Chemistry. 2010 ; 152( 1-3): 128-138.[citado 2025 jun. 27 ] Available from: https://doi.org/10.1016/j.bpc.2010.08.010
  • Source: Biophysical Chemistry. Unidade: IFSC

    Subjects: RECEPTORES, LIGANTES, ESPALHAMENTO, DIFRAÇÃO POR RAIOS X, GLÂNDULA TIREOIDE, HORMÔNIOS, ESTRÓGENOS, EXPRESSÃO GÊNICA, APOPTOSE

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      GARCIA, Wanius et al. Probing conformational changes in orphan nuclear receptor: the NGFI-B intermediate is a partially unfolded dimer. Biophysical Chemistry, v. 137, p. 2-3, 2008Tradução . . Disponível em: https://doi.org/10.1016/j.bpc.2008.07.005. Acesso em: 27 jun. 2025.
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      Garcia, W., Figueira, A. C. M., Oliveira Neto, M. de, Guzzi, C. A., Buzzá, H. H., Portugal, R. V., et al. (2008). Probing conformational changes in orphan nuclear receptor: the NGFI-B intermediate is a partially unfolded dimer. Biophysical Chemistry, 137, 2-3. doi:10.1016/j.bpc.2008.07.005
    • NLM

      Garcia W, Figueira ACM, Oliveira Neto M de, Guzzi CA, Buzzá HH, Portugal RV, Calgaro MR, Polikarpov I. Probing conformational changes in orphan nuclear receptor: the NGFI-B intermediate is a partially unfolded dimer [Internet]. Biophysical Chemistry. 2008 ; 137 2-3.[citado 2025 jun. 27 ] Available from: https://doi.org/10.1016/j.bpc.2008.07.005
    • Vancouver

      Garcia W, Figueira ACM, Oliveira Neto M de, Guzzi CA, Buzzá HH, Portugal RV, Calgaro MR, Polikarpov I. Probing conformational changes in orphan nuclear receptor: the NGFI-B intermediate is a partially unfolded dimer [Internet]. Biophysical Chemistry. 2008 ; 137 2-3.[citado 2025 jun. 27 ] Available from: https://doi.org/10.1016/j.bpc.2008.07.005
  • Source: Biophysical Chemistry. Unidade: IQ

    Subjects: LIPOSSOMOS, RESSONÂNCIA MAGNÉTICA, FLUORESCÊNCIA

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      PAULA, Eneida de et al. Preferential location of lidocaine and etidocaine in lecithin bilayers as determined by EPR, fluorescence and `ANTPOT. 2H'NMR. Biophysical Chemistry, v. 132, n. 1, p. 47-54, 2008Tradução . . Disponível em: https://doi.org/10.1016/j.bpc.2007.10.004. Acesso em: 27 jun. 2025.
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      Paula, E. de, Schreier, S., Jarrell, H. C., & Fraceto, L. F. (2008). Preferential location of lidocaine and etidocaine in lecithin bilayers as determined by EPR, fluorescence and `ANTPOT. 2H'NMR. Biophysical Chemistry, 132( 1), 47-54. doi:10.1016/j.bpc.2007.10.004
    • NLM

      Paula E de, Schreier S, Jarrell HC, Fraceto LF. Preferential location of lidocaine and etidocaine in lecithin bilayers as determined by EPR, fluorescence and `ANTPOT. 2H'NMR [Internet]. Biophysical Chemistry. 2008 ; 132( 1): 47-54.[citado 2025 jun. 27 ] Available from: https://doi.org/10.1016/j.bpc.2007.10.004
    • Vancouver

      Paula E de, Schreier S, Jarrell HC, Fraceto LF. Preferential location of lidocaine and etidocaine in lecithin bilayers as determined by EPR, fluorescence and `ANTPOT. 2H'NMR [Internet]. Biophysical Chemistry. 2008 ; 132( 1): 47-54.[citado 2025 jun. 27 ] Available from: https://doi.org/10.1016/j.bpc.2007.10.004
  • Source: Biophysical Chemistry. Unidades: FCFRP, IFSC

    Subjects: ESPECTROFLUOROMETRIA, POLIMERIZAÇÃO, PROTEÍNAS RECOMBINANTES, ESPECTROSCOPIA, FLUORESCÊNCIA

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      GARCIA, A. F. et al. Structural stability and reversible unfolding of recombinant porcine S100A12. Biophysical Chemistry, v. 134, p. 246-253, 2008Tradução . . Disponível em: https://doi.org/10.1016/j.bpc.2008.02.013. Acesso em: 27 jun. 2025.
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      Garcia, A. F., Garcia, W., Nonato, M. C., & Araújo, A. P. U. de. (2008). Structural stability and reversible unfolding of recombinant porcine S100A12. Biophysical Chemistry, 134, 246-253. doi:10.1016/j.bpc.2008.02.013
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      Garcia AF, Garcia W, Nonato MC, Araújo APU de. Structural stability and reversible unfolding of recombinant porcine S100A12 [Internet]. Biophysical Chemistry. 2008 ; 134 246-253.[citado 2025 jun. 27 ] Available from: https://doi.org/10.1016/j.bpc.2008.02.013
    • Vancouver

      Garcia AF, Garcia W, Nonato MC, Araújo APU de. Structural stability and reversible unfolding of recombinant porcine S100A12 [Internet]. Biophysical Chemistry. 2008 ; 134 246-253.[citado 2025 jun. 27 ] Available from: https://doi.org/10.1016/j.bpc.2008.02.013
  • Source: Biophysical Chemistry. Unidade: IFSC

    Assunto: FILMES FINOS

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      PICKHOLZ, Mónica e OLIVEIRA JUNIOR, Osvaldo Novais de e SKAF, Munir S. Interactions of chlorpromazine with phospholipid monolayers: effects of the ionization state of the drug. Biophysical Chemistry, v. 125, n. 2-3, p. 425-434, 2007Tradução . . Disponível em: https://doi.org/10.1016/j.bpc.2006.10.010. Acesso em: 27 jun. 2025.
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      Pickholz, M., Oliveira Junior, O. N. de, & Skaf, M. S. (2007). Interactions of chlorpromazine with phospholipid monolayers: effects of the ionization state of the drug. Biophysical Chemistry, 125( 2-3), 425-434. doi:10.1016/j.bpc.2006.10.010
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      Pickholz M, Oliveira Junior ON de, Skaf MS. Interactions of chlorpromazine with phospholipid monolayers: effects of the ionization state of the drug [Internet]. Biophysical Chemistry. 2007 ; 125( 2-3): 425-434.[citado 2025 jun. 27 ] Available from: https://doi.org/10.1016/j.bpc.2006.10.010
    • Vancouver

      Pickholz M, Oliveira Junior ON de, Skaf MS. Interactions of chlorpromazine with phospholipid monolayers: effects of the ionization state of the drug [Internet]. Biophysical Chemistry. 2007 ; 125( 2-3): 425-434.[citado 2025 jun. 27 ] Available from: https://doi.org/10.1016/j.bpc.2006.10.010
  • Source: Biophysical Chemistry. Unidades: IFSC, IQSC

    Assunto: BIOQUÍMICA

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      MOREIRA, Leonardo Marmo et al. Pentacoordinate and hexacoordinate ferric hemes in acid medium:: EPR, UV-Vis and CD studies of the giant extracellular hemoglobin of Glossoscolex paulistus. Biophysical Chemistry, v. 124, n. 1, p. 62-72, 2006Tradução . . Disponível em: https://doi.org/10.1016/j.bpc.2006.05.030. Acesso em: 27 jun. 2025.
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      Moreira, L. M., Poli, A. L., Costa Filho, A. J. da, & Imasato, H. (2006). Pentacoordinate and hexacoordinate ferric hemes in acid medium:: EPR, UV-Vis and CD studies of the giant extracellular hemoglobin of Glossoscolex paulistus. Biophysical Chemistry, 124( 1), 62-72. doi:10.1016/j.bpc.2006.05.030
    • NLM

      Moreira LM, Poli AL, Costa Filho AJ da, Imasato H. Pentacoordinate and hexacoordinate ferric hemes in acid medium:: EPR, UV-Vis and CD studies of the giant extracellular hemoglobin of Glossoscolex paulistus [Internet]. Biophysical Chemistry. 2006 ; 124( 1): 62-72.[citado 2025 jun. 27 ] Available from: https://doi.org/10.1016/j.bpc.2006.05.030
    • Vancouver

      Moreira LM, Poli AL, Costa Filho AJ da, Imasato H. Pentacoordinate and hexacoordinate ferric hemes in acid medium:: EPR, UV-Vis and CD studies of the giant extracellular hemoglobin of Glossoscolex paulistus [Internet]. Biophysical Chemistry. 2006 ; 124( 1): 62-72.[citado 2025 jun. 27 ] Available from: https://doi.org/10.1016/j.bpc.2006.05.030
  • Source: Biophysical Chemistry. Unidade: IQ

    Subjects: LIPOSSOMOS, RESSONÂNCIA MAGNÉTICA NUCLEAR, ANESTESIA LOCAL

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      FRACETO, Leonardo Fernandes et al. Differential effects of uncharged aminoamide local anesthetics on phospholipid bilayers, as monitored by 'ANTPOT 1 H'-NMR measurements. Biophysical Chemistry, v. 115, n. 1, p. 11-18, 2005Tradução . . Disponível em: https://doi.org/10.1016/j.bpc.2004.12.003. Acesso em: 27 jun. 2025.
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      Fraceto, L. F., Spisni, A., Schreier, S., & Paula, E. de. (2005). Differential effects of uncharged aminoamide local anesthetics on phospholipid bilayers, as monitored by 'ANTPOT 1 H'-NMR measurements. Biophysical Chemistry, 115( 1), 11-18. doi:10.1016/j.bpc.2004.12.003
    • NLM

      Fraceto LF, Spisni A, Schreier S, Paula E de. Differential effects of uncharged aminoamide local anesthetics on phospholipid bilayers, as monitored by 'ANTPOT 1 H'-NMR measurements [Internet]. Biophysical Chemistry. 2005 ; 115( 1): 11-18.[citado 2025 jun. 27 ] Available from: https://doi.org/10.1016/j.bpc.2004.12.003
    • Vancouver

      Fraceto LF, Spisni A, Schreier S, Paula E de. Differential effects of uncharged aminoamide local anesthetics on phospholipid bilayers, as monitored by 'ANTPOT 1 H'-NMR measurements [Internet]. Biophysical Chemistry. 2005 ; 115( 1): 11-18.[citado 2025 jun. 27 ] Available from: https://doi.org/10.1016/j.bpc.2004.12.003
  • Source: Biophysical Chemistry. Unidade: IFSC

    Subjects: BIOFÍSICA, PROTEÍNAS, PEPTÍDEOS

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      CAMPANA, Patrícia Targon et al. Conformation of a synthetic antigenic peptide from HIV-1 p24 protein induced by ionic micelles. Biophysical Chemistry, v. 113, n. 2, p. 175-182, 2005Tradução . . Disponível em: https://doi.org/10.1016/j.bpc.2004.08.006. Acesso em: 27 jun. 2025.
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      Campana, P. T., Beltramini, L. M., Costa Filho, A. J. da, Tonarelli, G., Lottersberger, J., & Bianconi, M. L. (2005). Conformation of a synthetic antigenic peptide from HIV-1 p24 protein induced by ionic micelles. Biophysical Chemistry, 113( 2), 175-182. doi:10.1016/j.bpc.2004.08.006
    • NLM

      Campana PT, Beltramini LM, Costa Filho AJ da, Tonarelli G, Lottersberger J, Bianconi ML. Conformation of a synthetic antigenic peptide from HIV-1 p24 protein induced by ionic micelles [Internet]. Biophysical Chemistry. 2005 ; 113( 2): 175-182.[citado 2025 jun. 27 ] Available from: https://doi.org/10.1016/j.bpc.2004.08.006
    • Vancouver

      Campana PT, Beltramini LM, Costa Filho AJ da, Tonarelli G, Lottersberger J, Bianconi ML. Conformation of a synthetic antigenic peptide from HIV-1 p24 protein induced by ionic micelles [Internet]. Biophysical Chemistry. 2005 ; 113( 2): 175-182.[citado 2025 jun. 27 ] Available from: https://doi.org/10.1016/j.bpc.2004.08.006
  • Source: Biophysical Chemistry. Unidade: IQSC

    Assunto: BIOQUÍMICA

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      POLI, Alessandra Lima et al. Autoxidation studies of extracellular hemoglobin of glossoscolex paulistus at pH 9 :: Cyanide and hydroxyl effect. Biophysical Chemistry, v. 114, n. 2-3, p. 253-260, 2005Tradução . . Disponível em: https://doi.org/10.1016/j.bpc.2004.12.041. Acesso em: 27 jun. 2025.
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      Poli, A. L., Moreira, L. M., Hidalgo, Á. A., & Imasato, H. (2005). Autoxidation studies of extracellular hemoglobin of glossoscolex paulistus at pH 9 :: Cyanide and hydroxyl effect. Biophysical Chemistry, 114( 2-3), 253-260. doi:10.1016/j.bpc.2004.12.041
    • NLM

      Poli AL, Moreira LM, Hidalgo ÁA, Imasato H. Autoxidation studies of extracellular hemoglobin of glossoscolex paulistus at pH 9 :: Cyanide and hydroxyl effect [Internet]. Biophysical Chemistry. 2005 ;114( 2-3): 253-260.[citado 2025 jun. 27 ] Available from: https://doi.org/10.1016/j.bpc.2004.12.041
    • Vancouver

      Poli AL, Moreira LM, Hidalgo ÁA, Imasato H. Autoxidation studies of extracellular hemoglobin of glossoscolex paulistus at pH 9 :: Cyanide and hydroxyl effect [Internet]. Biophysical Chemistry. 2005 ;114( 2-3): 253-260.[citado 2025 jun. 27 ] Available from: https://doi.org/10.1016/j.bpc.2004.12.041
  • Source: Biophysical Chemistry. Unidades: IQSC, IFSC

    Subjects: BIOFÍSICA, QUÍMICA, LIPÍDEOS

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      HIDALGO, A. A. et al. Interaction of two phenothiazine derivatives with phospholipid monolayers. Biophysical Chemistry, v. 109, n. 1, p. 85-104, 2004Tradução . . Disponível em: https://doi.org/10.1016/j.bpc.2003.10.020. Acesso em: 27 jun. 2025.
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      Hidalgo, A. A., Caetano, W., Tabak, M., & Oliveira Junior, O. N. de. (2004). Interaction of two phenothiazine derivatives with phospholipid monolayers. Biophysical Chemistry, 109( 1), 85-104. doi:10.1016/j.bpc.2003.10.020
    • NLM

      Hidalgo AA, Caetano W, Tabak M, Oliveira Junior ON de. Interaction of two phenothiazine derivatives with phospholipid monolayers [Internet]. Biophysical Chemistry. 2004 ; 109( 1): 85-104.[citado 2025 jun. 27 ] Available from: https://doi.org/10.1016/j.bpc.2003.10.020
    • Vancouver

      Hidalgo AA, Caetano W, Tabak M, Oliveira Junior ON de. Interaction of two phenothiazine derivatives with phospholipid monolayers [Internet]. Biophysical Chemistry. 2004 ; 109( 1): 85-104.[citado 2025 jun. 27 ] Available from: https://doi.org/10.1016/j.bpc.2003.10.020
  • Source: Biophysical Chemistry. Unidade: IQ

    Subjects: REOLOGIA, LISOZIMAS, FÍSICO-QUÍMICA

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      SILVA, Marcelo A. da e ARÊAS, Elizabeth Pinheiro Gomes. Rheological study on lysozyme/tetramethylurea viscoelastic matrices. Biophysical Chemistry, v. 99, n. 2, p. 129-141, 2002Tradução . . Disponível em: https://doi.org/10.1016/s0301-4622(02)00142-4. Acesso em: 27 jun. 2025.
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      Silva, M. A. da, & Arêas, E. P. G. (2002). Rheological study on lysozyme/tetramethylurea viscoelastic matrices. Biophysical Chemistry, 99( 2), 129-141. doi:10.1016/s0301-4622(02)00142-4
    • NLM

      Silva MA da, Arêas EPG. Rheological study on lysozyme/tetramethylurea viscoelastic matrices [Internet]. Biophysical Chemistry. 2002 ; 99( 2): 129-141.[citado 2025 jun. 27 ] Available from: https://doi.org/10.1016/s0301-4622(02)00142-4
    • Vancouver

      Silva MA da, Arêas EPG. Rheological study on lysozyme/tetramethylurea viscoelastic matrices [Internet]. Biophysical Chemistry. 2002 ; 99( 2): 129-141.[citado 2025 jun. 27 ] Available from: https://doi.org/10.1016/s0301-4622(02)00142-4

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