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  • Source: International Journal of Biological Macromolecules. Unidade: IQSC

    Assunto: HEMOGLOBINAS

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      CARVALHO, Francisco A. O et al. Oligomeric stability of Glossoscolex paulistus hemoglobin as a function of the storage time. International Journal of Biological Macromolecules, v. 133, p. 30-36, 2019Tradução . . Disponível em: https://doi.org/10.1016/j.ijbiomac.2019.04.072. Acesso em: 05 nov. 2024.
    • APA

      Carvalho, F. A. O., Caruso, C. S., Nascimento, E. D., Oliveira, T. M. B. F., Bachega, J. F. R., & Tabak, M. (2019). Oligomeric stability of Glossoscolex paulistus hemoglobin as a function of the storage time. International Journal of Biological Macromolecules, 133, 30-36. doi:10.1016/j.ijbiomac.2019.04.072
    • NLM

      Carvalho FAO, Caruso CS, Nascimento ED, Oliveira TMBF, Bachega JFR, Tabak M. Oligomeric stability of Glossoscolex paulistus hemoglobin as a function of the storage time [Internet]. International Journal of Biological Macromolecules. 2019 ;133 30-36.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1016/j.ijbiomac.2019.04.072
    • Vancouver

      Carvalho FAO, Caruso CS, Nascimento ED, Oliveira TMBF, Bachega JFR, Tabak M. Oligomeric stability of Glossoscolex paulistus hemoglobin as a function of the storage time [Internet]. International Journal of Biological Macromolecules. 2019 ;133 30-36.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1016/j.ijbiomac.2019.04.072
  • Source: International Journal of Biological Macromolecules. Unidade: IQSC

    Subjects: HEMOGLOBINAS, ESPECTROSCOPIA ÓPTICA

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      LIBARDI, Silvia Helena e ALVES, Fernanda R. e TABAK, Marcel. Interaction of Glossoscolex paulistus extracellular hemoglobin with hydrogen peroxide: Formation and decay of ferryl-HbGp. International Journal of Biological Macromolecules, v. 111, p. 271-280, 2018Tradução . . Disponível em: https://doi.org/10.1016/j.ijbiomac.2017.12.147. Acesso em: 05 nov. 2024.
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      Libardi, S. H., Alves, F. R., & Tabak, M. (2018). Interaction of Glossoscolex paulistus extracellular hemoglobin with hydrogen peroxide: Formation and decay of ferryl-HbGp. International Journal of Biological Macromolecules, 111, 271-280. doi:10.1016/j.ijbiomac.2017.12.147
    • NLM

      Libardi SH, Alves FR, Tabak M. Interaction of Glossoscolex paulistus extracellular hemoglobin with hydrogen peroxide: Formation and decay of ferryl-HbGp [Internet]. International Journal of Biological Macromolecules. 2018 ; 111 271-280.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1016/j.ijbiomac.2017.12.147
    • Vancouver

      Libardi SH, Alves FR, Tabak M. Interaction of Glossoscolex paulistus extracellular hemoglobin with hydrogen peroxide: Formation and decay of ferryl-HbGp [Internet]. International Journal of Biological Macromolecules. 2018 ; 111 271-280.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1016/j.ijbiomac.2017.12.147
  • Source: International Journal of Biological Macromolecules. Unidades: FFCLRP, IQSC

    Assunto: HEMOGLOBINAS

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      BARROS, Ana Eliza Barbosa et al. Glossoscolex paulistus hemoglobin with fluorescein isothiocyanate: Steady-state and time-resolved fluorescence. International Journal of Biological Macromolecules, v. 98, p. 777-785, 2017Tradução . . Disponível em: https://doi.org/10.1016/j.ijbiomac.2017.02.035. Acesso em: 05 nov. 2024.
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      Barros, A. E. B., Barioni, M. B., Carvalho, F. A. de O., Ito, A. S., & Tabak, M. (2017). Glossoscolex paulistus hemoglobin with fluorescein isothiocyanate: Steady-state and time-resolved fluorescence. International Journal of Biological Macromolecules, 98, 777-785. doi:10.1016/j.ijbiomac.2017.02.035
    • NLM

      Barros AEB, Barioni MB, Carvalho FA de O, Ito AS, Tabak M. Glossoscolex paulistus hemoglobin with fluorescein isothiocyanate: Steady-state and time-resolved fluorescence [Internet]. International Journal of Biological Macromolecules. 2017 ; 98 777-785.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1016/j.ijbiomac.2017.02.035
    • Vancouver

      Barros AEB, Barioni MB, Carvalho FA de O, Ito AS, Tabak M. Glossoscolex paulistus hemoglobin with fluorescein isothiocyanate: Steady-state and time-resolved fluorescence [Internet]. International Journal of Biological Macromolecules. 2017 ; 98 777-785.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1016/j.ijbiomac.2017.02.035
  • Source: International Journal of Biological Macromolecules. Unidade: IQSC

    Assunto: SURFACTANTES

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      CARVALHO, Francisco Adriano de Oliveira e ALVES, Fernanda Rosa e TABAK, Marcel. Ionic surfactants-Glossoscolex paulistus hemoglobin interactions: characterization of species in the solution. International Journal of Biological Macromolecules, v. 92, p. 670-681, 2016Tradução . . Disponível em: https://doi.org/10.1016/j.ijbiomac.2016.07.072. Acesso em: 05 nov. 2024.
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      Carvalho, F. A. de O., Alves, F. R., & Tabak, M. (2016). Ionic surfactants-Glossoscolex paulistus hemoglobin interactions: characterization of species in the solution. International Journal of Biological Macromolecules, 92, 670-681. doi:10.1016/j.ijbiomac.2016.07.072
    • NLM

      Carvalho FA de O, Alves FR, Tabak M. Ionic surfactants-Glossoscolex paulistus hemoglobin interactions: characterization of species in the solution [Internet]. International Journal of Biological Macromolecules. 2016 ; 92 670-681.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1016/j.ijbiomac.2016.07.072
    • Vancouver

      Carvalho FA de O, Alves FR, Tabak M. Ionic surfactants-Glossoscolex paulistus hemoglobin interactions: characterization of species in the solution [Internet]. International Journal of Biological Macromolecules. 2016 ; 92 670-681.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1016/j.ijbiomac.2016.07.072
  • Source: Colloids and Surfaces B: Biointerfaces. Unidade: IQSC

    Assunto: BIOFÍSICA

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      CARVALHO, José Wilson Pires et al. Cetyltrimethylammonium chloride (CTAC) effect on the thermal stability of oxy-HbGp: dynamic light scattering (DLS) and small angle X-ray scattering (SAXS) studies. Colloids and Surfaces B: Biointerfaces, v. 118, n. 1, p. 14-24, 2014Tradução . . Disponível em: https://doi.org/10.1016/j.colsurfb.2014.03.021. Acesso em: 05 nov. 2024.
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      Carvalho, J. W. P., Carvalho, F. A. de O., Batista, T., Santiago, P. S., & Tabak, M. (2014). Cetyltrimethylammonium chloride (CTAC) effect on the thermal stability of oxy-HbGp: dynamic light scattering (DLS) and small angle X-ray scattering (SAXS) studies. Colloids and Surfaces B: Biointerfaces, 118( 1), 14-24. doi:10.1016/j.colsurfb.2014.03.021
    • NLM

      Carvalho JWP, Carvalho FA de O, Batista T, Santiago PS, Tabak M. Cetyltrimethylammonium chloride (CTAC) effect on the thermal stability of oxy-HbGp: dynamic light scattering (DLS) and small angle X-ray scattering (SAXS) studies [Internet]. Colloids and Surfaces B: Biointerfaces. 2014 ; 118( 1): 14-24.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1016/j.colsurfb.2014.03.021
    • Vancouver

      Carvalho JWP, Carvalho FA de O, Batista T, Santiago PS, Tabak M. Cetyltrimethylammonium chloride (CTAC) effect on the thermal stability of oxy-HbGp: dynamic light scattering (DLS) and small angle X-ray scattering (SAXS) studies [Internet]. Colloids and Surfaces B: Biointerfaces. 2014 ; 118( 1): 14-24.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1016/j.colsurfb.2014.03.021
  • Source: Biochimica et Biophysica Acta - Biomembranes. Unidades: IF, IQSC

    Subjects: LIPOPOLISSACARÍDEOS, BIOQUÍMICA

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      DOMINGUES, Marco M et al. rBPI21 interacts with negative membranes endothermically promoting the formation of rigid multilamellar structures. Biochimica et Biophysica Acta - Biomembranes, v. 1828, n. 11, p. 2419-2427, 2013Tradução . . Disponível em: https://doi.org/10.1016/j.bbamem.2013.06.009. Acesso em: 05 nov. 2024.
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      Domingues, M. M., Bianconi, M. L., Barbosa, L. R. S., Santiago, P. S., Tabak, M., Castanho, M. A. R. B., et al. (2013). rBPI21 interacts with negative membranes endothermically promoting the formation of rigid multilamellar structures. Biochimica et Biophysica Acta - Biomembranes, 1828( 11), 2419-2427. doi:10.1016/j.bbamem.2013.06.009
    • NLM

      Domingues MM, Bianconi ML, Barbosa LRS, Santiago PS, Tabak M, Castanho MARB, Itri R, Santos NC. rBPI21 interacts with negative membranes endothermically promoting the formation of rigid multilamellar structures [Internet]. Biochimica et Biophysica Acta - Biomembranes. 2013 ; 1828( 11): 2419-2427.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1016/j.bbamem.2013.06.009
    • Vancouver

      Domingues MM, Bianconi ML, Barbosa LRS, Santiago PS, Tabak M, Castanho MARB, Itri R, Santos NC. rBPI21 interacts with negative membranes endothermically promoting the formation of rigid multilamellar structures [Internet]. Biochimica et Biophysica Acta - Biomembranes. 2013 ; 1828( 11): 2419-2427.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1016/j.bbamem.2013.06.009
  • Source: Colloids and Surfaces B: Biointerfaces. Unidade: IQSC

    Assunto: BIOFÍSICA

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      CARVALHO, Jose Wilson Pires et al. Sodium dodecyl sulfate (SDS) effect on the thermal stability of oxy-HbGp: dynamic light scattering (DLS) and small angle X-ray scattering (SAXS) studies. Colloids and Surfaces B: Biointerfaces, v. 111, n. 1, p. 561-570, 2013Tradução . . Disponível em: https://doi.org/10.1016/j.colsurfb.2013.06.050. Acesso em: 05 nov. 2024.
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      Carvalho, J. W. P., Alves, F. R., Batista, T., Carvalho, F. A. de O., Santiago, P. S., & Tabak, M. (2013). Sodium dodecyl sulfate (SDS) effect on the thermal stability of oxy-HbGp: dynamic light scattering (DLS) and small angle X-ray scattering (SAXS) studies. Colloids and Surfaces B: Biointerfaces, 111( 1), 561-570. doi:10.1016/j.colsurfb.2013.06.050
    • NLM

      Carvalho JWP, Alves FR, Batista T, Carvalho FA de O, Santiago PS, Tabak M. Sodium dodecyl sulfate (SDS) effect on the thermal stability of oxy-HbGp: dynamic light scattering (DLS) and small angle X-ray scattering (SAXS) studies [Internet]. Colloids and Surfaces B: Biointerfaces. 2013 ; 111( 1): 561-570.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1016/j.colsurfb.2013.06.050
    • Vancouver

      Carvalho JWP, Alves FR, Batista T, Carvalho FA de O, Santiago PS, Tabak M. Sodium dodecyl sulfate (SDS) effect on the thermal stability of oxy-HbGp: dynamic light scattering (DLS) and small angle X-ray scattering (SAXS) studies [Internet]. Colloids and Surfaces B: Biointerfaces. 2013 ; 111( 1): 561-570.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1016/j.colsurfb.2013.06.050
  • Source: Biophysical Chemistry. Unidades: FFCLRP, IF, IQSC

    Assunto: BIOQUÍMICA

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      CARVALHO, José Wilson Pires et al. On the temperature stability of extracellular hemoglobin of Glossoscolex paulistus, at different oxidation states: SAXS and DLS studies. Biophysical Chemistry, v. 163-164, p. 44-55, 2012Tradução . . Disponível em: https://doi.org/10.1016/j.bpc.2012.02.004. Acesso em: 05 nov. 2024.
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      Carvalho, J. W. P., Santiago, P. S., Batista, T., Salmon, C. E. G., Barbosa, L. R. S., Itri, R., & Tabak, M. (2012). On the temperature stability of extracellular hemoglobin of Glossoscolex paulistus, at different oxidation states: SAXS and DLS studies. Biophysical Chemistry, 163-164, 44-55. doi:10.1016/j.bpc.2012.02.004
    • NLM

      Carvalho JWP, Santiago PS, Batista T, Salmon CEG, Barbosa LRS, Itri R, Tabak M. On the temperature stability of extracellular hemoglobin of Glossoscolex paulistus, at different oxidation states: SAXS and DLS studies [Internet]. Biophysical Chemistry. 2012 ; 163-164 44-55.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1016/j.bpc.2012.02.004
    • Vancouver

      Carvalho JWP, Santiago PS, Batista T, Salmon CEG, Barbosa LRS, Itri R, Tabak M. On the temperature stability of extracellular hemoglobin of Glossoscolex paulistus, at different oxidation states: SAXS and DLS studies [Internet]. Biophysical Chemistry. 2012 ; 163-164 44-55.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1016/j.bpc.2012.02.004
  • Source: Colloids and Surfaces B: Biointerfaces. Unidade: IQSC

    Assunto: BIOFÍSICA

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      ANJOS, Jorge Luiz Vieira et al. On the interaction of bovine serum albumin with ionic surfactants:: temperature induced EPR changes of a maleimide nitroxide reflect local protein dynamics and probe solvent accessibility. Colloids and Surfaces B: Biointerfaces, v. 88, n. 1, p. 463-470, 2011Tradução . . Disponível em: https://doi.org/10.1016/j.colsurfb.2011.07.030. Acesso em: 05 nov. 2024.
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      Anjos, J. L. V., Santiago, P. S., Tabak, M., & Alonso, A. (2011). On the interaction of bovine serum albumin with ionic surfactants:: temperature induced EPR changes of a maleimide nitroxide reflect local protein dynamics and probe solvent accessibility. Colloids and Surfaces B: Biointerfaces, 88( 1), 463-470. doi:10.1016/j.colsurfb.2011.07.030
    • NLM

      Anjos JLV, Santiago PS, Tabak M, Alonso A. On the interaction of bovine serum albumin with ionic surfactants:: temperature induced EPR changes of a maleimide nitroxide reflect local protein dynamics and probe solvent accessibility [Internet]. Colloids and Surfaces B: Biointerfaces. 2011 ; 88( 1): 463-470.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1016/j.colsurfb.2011.07.030
    • Vancouver

      Anjos JLV, Santiago PS, Tabak M, Alonso A. On the interaction of bovine serum albumin with ionic surfactants:: temperature induced EPR changes of a maleimide nitroxide reflect local protein dynamics and probe solvent accessibility [Internet]. Colloids and Surfaces B: Biointerfaces. 2011 ; 88( 1): 463-470.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1016/j.colsurfb.2011.07.030
  • 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: 05 nov. 2024.
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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 2024 nov. 05 ] 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 2024 nov. 05 ] Available from: https://doi.org/10.1016/j.bpc.2010.08.010
  • Source: Colloids and Surfaces B: Biointerfaces. Unidades: IQSC, FFCLRP

    Subjects: BIOQUÍMICA, BIORESSONÂNCIA PARAMAGNÉTICA DE SPIN

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      SOUSA NETO, Diógenes de et al. Interaction of bovine serum albumin (BSA) with ionic surfactants evaluated by electron paramagnetic resonance (EPR) spectroscopy. Colloids and Surfaces B: Biointerfaces, v. 70, n. 1, p. 147-156, 2009Tradução . . Disponível em: https://doi.org/10.1016/j.colsurfb.2008.12.026. Acesso em: 05 nov. 2024.
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      Sousa Neto, D. de, Salmon, C. E. G., Alonso, A., & Tabak, M. (2009). Interaction of bovine serum albumin (BSA) with ionic surfactants evaluated by electron paramagnetic resonance (EPR) spectroscopy. Colloids and Surfaces B: Biointerfaces, 70( 1), 147-156. doi:10.1016/j.colsurfb.2008.12.026
    • NLM

      Sousa Neto D de, Salmon CEG, Alonso A, Tabak M. Interaction of bovine serum albumin (BSA) with ionic surfactants evaluated by electron paramagnetic resonance (EPR) spectroscopy [Internet]. Colloids and Surfaces B: Biointerfaces. 2009 ; 70( 1): 147-156.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1016/j.colsurfb.2008.12.026
    • Vancouver

      Sousa Neto D de, Salmon CEG, Alonso A, Tabak M. Interaction of bovine serum albumin (BSA) with ionic surfactants evaluated by electron paramagnetic resonance (EPR) spectroscopy [Internet]. Colloids and Surfaces B: Biointerfaces. 2009 ; 70( 1): 147-156.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1016/j.colsurfb.2008.12.026
  • Source: Colloids and Surfaces B: Biointerfaces. Unidade: IQSC

    Subjects: BIOQUÍMICA, BIOFÍSICA

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      SANTIAGO, Patricia Soares et al. On the localization of water-soluble porphyrins in micellar systems evaluated by static and time-resolved frequency-domanin fluorescence techniques. Colloids and Surfaces B: Biointerfaces, v. 65, n. 2, p. 247-256, 2008Tradução . . Disponível em: https://doi.org/10.1016/j.colsurfb.2008.04.010. Acesso em: 05 nov. 2024.
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      Santiago, P. S., Sousa Neto, D. de, Gandini, S. de C. M., & Tabak, M. (2008). On the localization of water-soluble porphyrins in micellar systems evaluated by static and time-resolved frequency-domanin fluorescence techniques. Colloids and Surfaces B: Biointerfaces, 65( 2), 247-256. doi:10.1016/j.colsurfb.2008.04.010
    • NLM

      Santiago PS, Sousa Neto D de, Gandini S de CM, Tabak M. On the localization of water-soluble porphyrins in micellar systems evaluated by static and time-resolved frequency-domanin fluorescence techniques [Internet]. Colloids and Surfaces B: Biointerfaces. 2008 ; 65( 2): 247-256.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1016/j.colsurfb.2008.04.010
    • Vancouver

      Santiago PS, Sousa Neto D de, Gandini S de CM, Tabak M. On the localization of water-soluble porphyrins in micellar systems evaluated by static and time-resolved frequency-domanin fluorescence techniques [Internet]. Colloids and Surfaces B: Biointerfaces. 2008 ; 65( 2): 247-256.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1016/j.colsurfb.2008.04.010
  • Source: Colloids and Surfaces B: Biointerfaces. Unidade: IQSC

    Subjects: BIOQUÍMICA, BIOFÍSICA

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      MOREIRA, Leonardo Marmo et al. Interaction of giant extracellular glossoscolex paulistus hemoglobin (HbGp) with zwitterionic surfactant N-hexadecyl-N,N-dimethyl-3-ammonio-1-propanesulfonate (HPS): effects of oligomeric dissociation. Colloids and Surfaces B: Biointerfaces, v. 61, n. 2, p. 153-163, 2008Tradução . . Disponível em: https://doi.org/10.1016/j.colsurfb.2007.07.010. Acesso em: 05 nov. 2024.
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      Moreira, L. M., Santiago, P. S., Almeida, Ë. V. de, & Tabak, M. (2008). Interaction of giant extracellular glossoscolex paulistus hemoglobin (HbGp) with zwitterionic surfactant N-hexadecyl-N,N-dimethyl-3-ammonio-1-propanesulfonate (HPS): effects of oligomeric dissociation. Colloids and Surfaces B: Biointerfaces, 61( 2), 153-163. doi:10.1016/j.colsurfb.2007.07.010
    • NLM

      Moreira LM, Santiago PS, Almeida ËV de, Tabak M. Interaction of giant extracellular glossoscolex paulistus hemoglobin (HbGp) with zwitterionic surfactant N-hexadecyl-N,N-dimethyl-3-ammonio-1-propanesulfonate (HPS): effects of oligomeric dissociation [Internet]. Colloids and Surfaces B: Biointerfaces. 2008 ; 61( 2): 153-163.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1016/j.colsurfb.2007.07.010
    • Vancouver

      Moreira LM, Santiago PS, Almeida ËV de, Tabak M. Interaction of giant extracellular glossoscolex paulistus hemoglobin (HbGp) with zwitterionic surfactant N-hexadecyl-N,N-dimethyl-3-ammonio-1-propanesulfonate (HPS): effects of oligomeric dissociation [Internet]. Colloids and Surfaces B: Biointerfaces. 2008 ; 61( 2): 153-163.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1016/j.colsurfb.2007.07.010
  • Source: Biochimica et Biophysica Acta - General Subjects. Unidade: IQSC

    Assunto: BIOFÍSICA

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      SANTIAGO, Patricia Soares et al. Giant extracellular glossoscolex paulistus hemoglobin (HbGp) upon interaction with cethyltrilammonium chloride (CTAC) and sodium dodecyl sulphate (SDS) surfactants: dissociation of oligomeric structure ad autoxidation. Biochimica et Biophysica Acta - General Subjects, v. 1770, n. 4, p. 506-517, 2007Tradução . . Disponível em: https://doi.org/10.1016/j.bbagen.2006.11.005. Acesso em: 05 nov. 2024.
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      Santiago, P. S., Moreira, L. M., Almeida, E. V. R. de, & Tabak, M. (2007). Giant extracellular glossoscolex paulistus hemoglobin (HbGp) upon interaction with cethyltrilammonium chloride (CTAC) and sodium dodecyl sulphate (SDS) surfactants: dissociation of oligomeric structure ad autoxidation. Biochimica et Biophysica Acta - General Subjects, 1770( 4), 506-517. doi:10.1016/j.bbagen.2006.11.005
    • NLM

      Santiago PS, Moreira LM, Almeida EVR de, Tabak M. Giant extracellular glossoscolex paulistus hemoglobin (HbGp) upon interaction with cethyltrilammonium chloride (CTAC) and sodium dodecyl sulphate (SDS) surfactants: dissociation of oligomeric structure ad autoxidation [Internet]. Biochimica et Biophysica Acta - General Subjects. 2007 ; 1770( 4): 506-517.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1016/j.bbagen.2006.11.005
    • Vancouver

      Santiago PS, Moreira LM, Almeida EVR de, Tabak M. Giant extracellular glossoscolex paulistus hemoglobin (HbGp) upon interaction with cethyltrilammonium chloride (CTAC) and sodium dodecyl sulphate (SDS) surfactants: dissociation of oligomeric structure ad autoxidation [Internet]. Biochimica et Biophysica Acta - General Subjects. 2007 ; 1770( 4): 506-517.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1016/j.bbagen.2006.11.005
  • Source: Biochimica et Biophysica Acta. Unidade: IQSC

    Assunto: BIOFÍSICA

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      ALMEIDA, Luís Eduardo e IMASATO, Hidetake e TABAK, Marcel. Enzymatic oxidation of dipyridamole in homogeneous and micellar solutions in the horseradish peroxidase-hydrogen peroxide system. Biochimica et Biophysica Acta, v. 1760, n. 2, p. 216-226, 2006Tradução . . Disponível em: http://www.sciencedirect.com/science/journal/03044165. Acesso em: 05 nov. 2024.
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      Almeida, L. E., Imasato, H., & Tabak, M. (2006). Enzymatic oxidation of dipyridamole in homogeneous and micellar solutions in the horseradish peroxidase-hydrogen peroxide system. Biochimica et Biophysica Acta, 1760( 2), 216-226. Recuperado de http://www.sciencedirect.com/science/journal/03044165
    • NLM

      Almeida LE, Imasato H, Tabak M. Enzymatic oxidation of dipyridamole in homogeneous and micellar solutions in the horseradish peroxidase-hydrogen peroxide system [Internet]. Biochimica et Biophysica Acta. 2006 ; 1760( 2): 216-226.[citado 2024 nov. 05 ] Available from: http://www.sciencedirect.com/science/journal/03044165
    • Vancouver

      Almeida LE, Imasato H, Tabak M. Enzymatic oxidation of dipyridamole in homogeneous and micellar solutions in the horseradish peroxidase-hydrogen peroxide system [Internet]. Biochimica et Biophysica Acta. 2006 ; 1760( 2): 216-226.[citado 2024 nov. 05 ] Available from: http://www.sciencedirect.com/science/journal/03044165
  • Source: Colloids and Surfaces B: Biointerfaces. Unidade: IQSC

    Subjects: BIOQUÍMICA, BIOFÍSICA

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      POLI, Alessandra Lima et al. SDS (sodium dodecyl sulfate) effect on the autoxidation of the glossoscolex paulistus giant extracellular hemoglobin:: Kinetic studies at pH 7.0 and 9.0. Colloids and Surfaces B: Biointerfaces, v. 52, n. 1, p. 96-104, 2006Tradução . . Disponível em: https://doi.org/10.1016/j.colsurfb.2006.07.010. Acesso em: 05 nov. 2024.
    • APA

      Poli, A. L., Moreira, L. M., Tabak, M., & Imasato, H. (2006). SDS (sodium dodecyl sulfate) effect on the autoxidation of the glossoscolex paulistus giant extracellular hemoglobin:: Kinetic studies at pH 7.0 and 9.0. Colloids and Surfaces B: Biointerfaces, 52( 1), 96-104. doi:10.1016/j.colsurfb.2006.07.010
    • NLM

      Poli AL, Moreira LM, Tabak M, Imasato H. SDS (sodium dodecyl sulfate) effect on the autoxidation of the glossoscolex paulistus giant extracellular hemoglobin:: Kinetic studies at pH 7.0 and 9.0 [Internet]. Colloids and Surfaces B: Biointerfaces. 2006 ; 52( 1): 96-104.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1016/j.colsurfb.2006.07.010
    • Vancouver

      Poli AL, Moreira LM, Tabak M, Imasato H. SDS (sodium dodecyl sulfate) effect on the autoxidation of the glossoscolex paulistus giant extracellular hemoglobin:: Kinetic studies at pH 7.0 and 9.0 [Internet]. Colloids and Surfaces B: Biointerfaces. 2006 ; 52( 1): 96-104.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1016/j.colsurfb.2006.07.010
  • 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: 05 nov. 2024.
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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 2024 nov. 05 ] 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 2024 nov. 05 ] Available from: https://doi.org/10.1016/j.bpc.2003.10.020
  • Source: Biochimica et Biophysica Acta. Unidade: IQSC

    Subjects: BIOQUÍMICA, BIOFÍSICA

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      ALONSO, Antonio e SILVA, Junaine Vasques da e TABAK, Marcel. Hydration effects on the protein dynamics in stratum corneum as evaluated by EPR spectroscopy. Biochimica et Biophysica Acta, v. 1646, p. 32-41, 2003Tradução . . Disponível em: https://doi.org/10.1016/s1570-9639(02)00545-9. Acesso em: 05 nov. 2024.
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      Alonso, A., Silva, J. V. da, & Tabak, M. (2003). Hydration effects on the protein dynamics in stratum corneum as evaluated by EPR spectroscopy. Biochimica et Biophysica Acta, 1646, 32-41. doi:10.1016/s1570-9639(02)00545-9
    • NLM

      Alonso A, Silva JV da, Tabak M. Hydration effects on the protein dynamics in stratum corneum as evaluated by EPR spectroscopy [Internet]. Biochimica et Biophysica Acta. 2003 ; 1646 32-41.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1016/s1570-9639(02)00545-9
    • Vancouver

      Alonso A, Silva JV da, Tabak M. Hydration effects on the protein dynamics in stratum corneum as evaluated by EPR spectroscopy [Internet]. Biochimica et Biophysica Acta. 2003 ; 1646 32-41.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1016/s1570-9639(02)00545-9
  • Source: Biochimica et Biophysica Acta. Unidade: IQSC

    Subjects: BIOQUÍMICA, BIOFÍSICA

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    • ABNT

      GELAMO, Emerson Luiz et al. Interaction of bovine (BSA) and human (HSA) serum albumins with ionic surfactants: spectroscopy and modelling. Biochimica et Biophysica Acta, v. 1594, n. 1, p. 84-99, 2002Tradução . . Disponível em: https://doi.org/10.1016/s0167-4838(01)00287-4. Acesso em: 05 nov. 2024.
    • APA

      Gelamo, E. L., Silva, C. H. T. P., Imasato, H., & Tabak, M. (2002). Interaction of bovine (BSA) and human (HSA) serum albumins with ionic surfactants: spectroscopy and modelling. Biochimica et Biophysica Acta, 1594( 1), 84-99. doi:10.1016/s0167-4838(01)00287-4
    • NLM

      Gelamo EL, Silva CHTP, Imasato H, Tabak M. Interaction of bovine (BSA) and human (HSA) serum albumins with ionic surfactants: spectroscopy and modelling [Internet]. Biochimica et Biophysica Acta. 2002 ; 1594( 1): 84-99.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1016/s0167-4838(01)00287-4
    • Vancouver

      Gelamo EL, Silva CHTP, Imasato H, Tabak M. Interaction of bovine (BSA) and human (HSA) serum albumins with ionic surfactants: spectroscopy and modelling [Internet]. Biochimica et Biophysica Acta. 2002 ; 1594( 1): 84-99.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1016/s0167-4838(01)00287-4
  • Source: Biophysical Chemistry. Unidades: IQSC, FMRP, IFSC

    Assunto: BIOFÍSICA

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      CABRAL, Carolina Bosch et al. Fluorescence properties of tryptophan residues in the monomeric d-chain Glossoscolex paulistus hemoglobin: an interpretation based on a comparative molecular model. Biophysical Chemistry, v. 97, p. 139-157, 2002Tradução . . Disponível em: https://doi.org/10.1016/s0301-4622(02)00046-7. Acesso em: 05 nov. 2024.
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      Cabral, C. B., Imasato, H., Rosa, J. C., Laure, H. J., Silva, C. H. T. de P. da, Tabak, M., et al. (2002). Fluorescence properties of tryptophan residues in the monomeric d-chain Glossoscolex paulistus hemoglobin: an interpretation based on a comparative molecular model. Biophysical Chemistry, 97, 139-157. doi:10.1016/s0301-4622(02)00046-7
    • NLM

      Cabral CB, Imasato H, Rosa JC, Laure HJ, Silva CHT de P da, Tabak M, Garratt RC, Greene LJ. Fluorescence properties of tryptophan residues in the monomeric d-chain Glossoscolex paulistus hemoglobin: an interpretation based on a comparative molecular model [Internet]. Biophysical Chemistry. 2002 ; 97 139-157.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1016/s0301-4622(02)00046-7
    • Vancouver

      Cabral CB, Imasato H, Rosa JC, Laure HJ, Silva CHT de P da, Tabak M, Garratt RC, Greene LJ. Fluorescence properties of tryptophan residues in the monomeric d-chain Glossoscolex paulistus hemoglobin: an interpretation based on a comparative molecular model [Internet]. Biophysical Chemistry. 2002 ; 97 139-157.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1016/s0301-4622(02)00046-7

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