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  • 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: 16 abr. 2024.
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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 2024 abr. 16 ] 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 2024 abr. 16 ] Available from: https://doi.org/10.1016/j.bpc.2023.107077
  • Source: Biophysical Chemistry. Unidades: FCFRP, IFSC, FFCLRP

    Subjects: BIOFÍSICA, ESPALHAMENTO DE RAIOS X A BAIXOS ÂNGULOS, PEPTÍDEOS, BIOQUÍMICA

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      PEDEZZI, Rafael et al. Biochemical and biophysical properties of a recombinant serine peptidase from Purpureocillium lilacinum. Biophysical Chemistry, v. 296, p. 106978-1-106978-9, 2023Tradução . . Disponível em: https://doi.org/10.1016/j.bpc.2023.106978. Acesso em: 16 abr. 2024.
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      Pedezzi, R., Evangelista, D. E., Garzon, N. G. da R., Simões, F. A. de O., Oliveira, A. H. C. de, Polikarpov, I., & Cabral, H. (2023). Biochemical and biophysical properties of a recombinant serine peptidase from Purpureocillium lilacinum. Biophysical Chemistry, 296, 106978-1-106978-9. doi:10.1016/j.bpc.2023.106978
    • NLM

      Pedezzi R, Evangelista DE, Garzon NG da R, Simões FA de O, Oliveira AHC de, Polikarpov I, Cabral H. Biochemical and biophysical properties of a recombinant serine peptidase from Purpureocillium lilacinum [Internet]. Biophysical Chemistry. 2023 ; 296 106978-1-106978-9.[citado 2024 abr. 16 ] Available from: https://doi.org/10.1016/j.bpc.2023.106978
    • Vancouver

      Pedezzi R, Evangelista DE, Garzon NG da R, Simões FA de O, Oliveira AHC de, Polikarpov I, Cabral H. Biochemical and biophysical properties of a recombinant serine peptidase from Purpureocillium lilacinum [Internet]. Biophysical Chemistry. 2023 ; 296 106978-1-106978-9.[citado 2024 abr. 16 ] Available from: https://doi.org/10.1016/j.bpc.2023.106978
  • 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: 16 abr. 2024.
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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 2024 abr. 16 ] 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 2024 abr. 16 ] 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: 16 abr. 2024.
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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 2024 abr. 16 ] 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 2024 abr. 16 ] 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: 16 abr. 2024.
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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
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      Yoshihara LMB, Arêas EPG. Protein/polyelectrolyte coacervation: investigating its occurrence in the lysozyme- carboxymethylcellulose system [Internet]. Biophysical Chemistry. 2018 ; 236 8-14.[citado 2024 abr. 16 ] Available from: https://doi.org/10.1016/j.bpc.2018.03.001
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      Yoshihara LMB, Arêas EPG. Protein/polyelectrolyte coacervation: investigating its occurrence in the lysozyme- carboxymethylcellulose system [Internet]. Biophysical Chemistry. 2018 ; 236 8-14.[citado 2024 abr. 16 ] Available from: https://doi.org/10.1016/j.bpc.2018.03.001
  • Source: Biophysical Chemistry. Unidade: FFCLRP

    Subjects: LIPÍDEOS, NANOPARTÍCULAS, LEISHMANIOSE VISCERAL, FÁRMACOS

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      BITENCOURT, José Jardes da Gama et al. Miltefosine-loaded lipid nanoparticles: improving miltefosine stability and reducing its hemolytic potential toward erythtocytes and its cytotoxic effect on macrophages. Biophysical Chemistry, v. 217, p. 20-31, 2016Tradução . . Disponível em: https://doi.org/10.1016/j.bpc.2016.07.005. Acesso em: 16 abr. 2024.
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      Bitencourt, J. J. da G., Pazin, W. M., Ito, A. S., Barioni, M. B., Pinto, C. de P., Santos, M. A. dos, et al. (2016). Miltefosine-loaded lipid nanoparticles: improving miltefosine stability and reducing its hemolytic potential toward erythtocytes and its cytotoxic effect on macrophages. Biophysical Chemistry, 217, 20-31. doi:10.1016/j.bpc.2016.07.005
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      Bitencourt JJ da G, Pazin WM, Ito AS, Barioni MB, Pinto C de P, Santos MA dos, Guimarães THS, Santos MRM dos, Valduga CJ. Miltefosine-loaded lipid nanoparticles: improving miltefosine stability and reducing its hemolytic potential toward erythtocytes and its cytotoxic effect on macrophages [Internet]. Biophysical Chemistry. 2016 ; 217 20-31.[citado 2024 abr. 16 ] Available from: https://doi.org/10.1016/j.bpc.2016.07.005
    • Vancouver

      Bitencourt JJ da G, Pazin WM, Ito AS, Barioni MB, Pinto C de P, Santos MA dos, Guimarães THS, Santos MRM dos, Valduga CJ. Miltefosine-loaded lipid nanoparticles: improving miltefosine stability and reducing its hemolytic potential toward erythtocytes and its cytotoxic effect on macrophages [Internet]. Biophysical Chemistry. 2016 ; 217 20-31.[citado 2024 abr. 16 ] Available from: https://doi.org/10.1016/j.bpc.2016.07.005
  • 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: 16 abr. 2024.
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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
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      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 2024 abr. 16 ] 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 2024 abr. 16 ] Available from: https://doi.org/10.1016/j.bpc.2015.10.004
  • Source: Biophysical Chemistry. Unidade: FFCLRP

    Subjects: LEISHMANIA, FÁRMACOS

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      BARIONI, Marina Berardi et al. Miltefosine and BODIPY-labeled alkylphosphocholine with leishmanicidal activity: aggregation properties and interaction with model membranes. Biophysical Chemistry, v. 196, p. 92-99, 2015Tradução . . Disponível em: https://doi.org/10.1016/j.bpc.2014.10.002. Acesso em: 16 abr. 2024.
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      Barioni, M. B., Ramos, A. P., Zaniquelli, M. E. D., Acuña, A. U., & Ito, A. S. (2015). Miltefosine and BODIPY-labeled alkylphosphocholine with leishmanicidal activity: aggregation properties and interaction with model membranes. Biophysical Chemistry, 196, 92-99. doi:10.1016/j.bpc.2014.10.002
    • NLM

      Barioni MB, Ramos AP, Zaniquelli MED, Acuña AU, Ito AS. Miltefosine and BODIPY-labeled alkylphosphocholine with leishmanicidal activity: aggregation properties and interaction with model membranes [Internet]. Biophysical Chemistry. 2015 ; 196 92-99.[citado 2024 abr. 16 ] Available from: https://doi.org/10.1016/j.bpc.2014.10.002
    • Vancouver

      Barioni MB, Ramos AP, Zaniquelli MED, Acuña AU, Ito AS. Miltefosine and BODIPY-labeled alkylphosphocholine with leishmanicidal activity: aggregation properties and interaction with model membranes [Internet]. Biophysical Chemistry. 2015 ; 196 92-99.[citado 2024 abr. 16 ] Available from: https://doi.org/10.1016/j.bpc.2014.10.002
  • 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: 16 abr. 2024.
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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 2024 abr. 16 ] 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 2024 abr. 16 ] Available from: https://doi.org/10.1016/j.bpc.2013.08.004
  • 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: 16 abr. 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 abr. 16 ] 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 abr. 16 ] Available from: https://doi.org/10.1016/j.bpc.2012.02.004
  • 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: 16 abr. 2024.
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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 2024 abr. 16 ] 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 2024 abr. 16 ] Available from: https://doi.org/10.1016/j.bpc.2010.10.010
  • Source: Biophysical Chemistry. Unidade: FFCLRP

    Subjects: LIPÍDEOS, CALORÍMETROS, MEMBRANA PLASMÁTICA

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      BOLEAN, M. et al. Thermodynamic properties and characterization of proteoliposomes rich in microdomains carrying alkaline phosphatase. Biophysical Chemistry, v. 158, n. 2/3, p. 111-118, 2011Tradução . . Disponível em: https://doi.org/10.1016/j.bpc.2011.05.019. Acesso em: 16 abr. 2024.
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      Bolean, M., Simão, A. M. S., Favarin, B. Z., Millán, J. L., & Ciancaglini, P. (2011). Thermodynamic properties and characterization of proteoliposomes rich in microdomains carrying alkaline phosphatase. Biophysical Chemistry, 158( 2/3), 111-118. doi:10.1016/j.bpc.2011.05.019
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      Bolean M, Simão AMS, Favarin BZ, Millán JL, Ciancaglini P. Thermodynamic properties and characterization of proteoliposomes rich in microdomains carrying alkaline phosphatase [Internet]. Biophysical Chemistry. 2011 ; 158( 2/3): 111-118.[citado 2024 abr. 16 ] Available from: https://doi.org/10.1016/j.bpc.2011.05.019
    • Vancouver

      Bolean M, Simão AMS, Favarin BZ, Millán JL, Ciancaglini P. Thermodynamic properties and characterization of proteoliposomes rich in microdomains carrying alkaline phosphatase [Internet]. Biophysical Chemistry. 2011 ; 158( 2/3): 111-118.[citado 2024 abr. 16 ] Available from: https://doi.org/10.1016/j.bpc.2011.05.019
  • Source: Biophysical Chemistry. Unidade: FFCLRP

    Subjects: ENZIMAS, PROTEÍNAS, ESPECTROSCOPIA

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      RIGOS, Carolina Fortes et al. Cytoplasmatic domain of Na,K-ATPase 'alfa'-subunit is responsible for the aggregation of the enzyme in proteoliposomes. Biophysical Chemistry, v. 146, n. 1, p. 36-41, 2010Tradução . . Disponível em: https://doi.org/10.1016/j.bpc.2009.10.002. Acesso em: 16 abr. 2024.
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      Rigos, C. F., Santos, H. de L., Yoneda, J. S., Montich, G., Maggio, B., & Ciancaglini, P. (2010). Cytoplasmatic domain of Na,K-ATPase 'alfa'-subunit is responsible for the aggregation of the enzyme in proteoliposomes. Biophysical Chemistry, 146( 1), 36-41. doi:10.1016/j.bpc.2009.10.002
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      Rigos CF, Santos H de L, Yoneda JS, Montich G, Maggio B, Ciancaglini P. Cytoplasmatic domain of Na,K-ATPase 'alfa'-subunit is responsible for the aggregation of the enzyme in proteoliposomes [Internet]. Biophysical Chemistry. 2010 ; 146( 1): 36-41.[citado 2024 abr. 16 ] Available from: https://doi.org/10.1016/j.bpc.2009.10.002
    • Vancouver

      Rigos CF, Santos H de L, Yoneda JS, Montich G, Maggio B, Ciancaglini P. Cytoplasmatic domain of Na,K-ATPase 'alfa'-subunit is responsible for the aggregation of the enzyme in proteoliposomes [Internet]. Biophysical Chemistry. 2010 ; 146( 1): 36-41.[citado 2024 abr. 16 ] Available from: https://doi.org/10.1016/j.bpc.2009.10.002
  • Source: Biophysical Chemistry. Unidade: FFCLRP

    Subjects: COLESTEROL, OSTEOBLASTO, CALORÍMETROS

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      BOLEAN, Maytê et al. The effect of cholesterol on the reconstitution of alkaline phosphatase into liposomes. Biophysical Chemistry, v. 152, n. 1/3, p. 74-79, 2010Tradução . . Disponível em: https://doi.org/10.1016/j.bpc.2010.08.002. Acesso em: 16 abr. 2024.
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      Bolean, M., Simão, A. M. S., Millán, J. L., & Ciancaglini, P. (2010). The effect of cholesterol on the reconstitution of alkaline phosphatase into liposomes. Biophysical Chemistry, 152( 1/3), 74-79. doi:10.1016/j.bpc.2010.08.002
    • NLM

      Bolean M, Simão AMS, Millán JL, Ciancaglini P. The effect of cholesterol on the reconstitution of alkaline phosphatase into liposomes [Internet]. Biophysical Chemistry. 2010 ; 152( 1/3): 74-79.[citado 2024 abr. 16 ] Available from: https://doi.org/10.1016/j.bpc.2010.08.002
    • Vancouver

      Bolean M, Simão AMS, Millán JL, Ciancaglini P. The effect of cholesterol on the reconstitution of alkaline phosphatase into liposomes [Internet]. Biophysical Chemistry. 2010 ; 152( 1/3): 74-79.[citado 2024 abr. 16 ] Available from: https://doi.org/10.1016/j.bpc.2010.08.002
  • 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: 16 abr. 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 abr. 16 ] 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 abr. 16 ] Available from: https://doi.org/10.1016/j.bpc.2010.08.010
  • Source: Biophysical Chemistry. Unidade: FFCLRP

    Subjects: ANESTESIA LOCAL, LIPÍDEOS DA MEMBRANA, MICROSCOPIA

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      LORITE, Gabriela S. et al. Dibucaine effects on structural and elastic properties of lipid bilayers. Biophysical Chemistry, v. 139, p. 75-83, 2009Tradução . . Disponível em: https://doi.org/10.1016/j.bpc.2008.10.006. Acesso em: 16 abr. 2024.
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      Lorite, G. S., Nobre, T. M., Zaniquelli, M. E. D., Paula, E. de, & Cotta, M. A. (2009). Dibucaine effects on structural and elastic properties of lipid bilayers. Biophysical Chemistry, 139, 75-83. doi:10.1016/j.bpc.2008.10.006
    • NLM

      Lorite GS, Nobre TM, Zaniquelli MED, Paula E de, Cotta MA. Dibucaine effects on structural and elastic properties of lipid bilayers [Internet]. Biophysical Chemistry. 2009 ; 139 75-83.[citado 2024 abr. 16 ] Available from: https://doi.org/10.1016/j.bpc.2008.10.006
    • Vancouver

      Lorite GS, Nobre TM, Zaniquelli MED, Paula E de, Cotta MA. Dibucaine effects on structural and elastic properties of lipid bilayers [Internet]. Biophysical Chemistry. 2009 ; 139 75-83.[citado 2024 abr. 16 ] Available from: https://doi.org/10.1016/j.bpc.2008.10.006
  • Source: Biophysical Chemistry. Unidade: FFCLRP

    Subjects: FLUORESCÊNCIA, PEPTÍDEOS

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      ROMANI, Ana Paula e ITO, Amando S. Interaction of adrenocorticotropin peptides with microheterogeneous systems: a fluorescence study. Biophysical Chemistry, v. 139, n. 2-3, p. 92-98, 2009Tradução . . Disponível em: https://doi.org/10.1016/j.bpc.2008.10.009. Acesso em: 16 abr. 2024.
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      Romani, A. P., & Ito, A. S. (2009). Interaction of adrenocorticotropin peptides with microheterogeneous systems: a fluorescence study. Biophysical Chemistry, 139( 2-3), 92-98. doi:10.1016/j.bpc.2008.10.009
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      Romani AP, Ito AS. Interaction of adrenocorticotropin peptides with microheterogeneous systems: a fluorescence study [Internet]. Biophysical Chemistry. 2009 ; 139( 2-3): 92-98.[citado 2024 abr. 16 ] Available from: https://doi.org/10.1016/j.bpc.2008.10.009
    • Vancouver

      Romani AP, Ito AS. Interaction of adrenocorticotropin peptides with microheterogeneous systems: a fluorescence study [Internet]. Biophysical Chemistry. 2009 ; 139( 2-3): 92-98.[citado 2024 abr. 16 ] Available from: https://doi.org/10.1016/j.bpc.2008.10.009
  • 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: 16 abr. 2024.
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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
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      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 2024 abr. 16 ] 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 2024 abr. 16 ] 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: 16 abr. 2024.
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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 2024 abr. 16 ] 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 2024 abr. 16 ] 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: 16 abr. 2024.
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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 2024 abr. 16 ] 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 2024 abr. 16 ] Available from: https://doi.org/10.1016/j.bpc.2008.02.013

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