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

    Subjects: LEISHMANIA BRASILIENSIS, PROTOZOA

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    • ABNT

      COTO, Amanda Laís de Souza et al. Structural and functional studies of the Leishmania braziliensis SGT co-chaperone indicate that it shares structural features with HIP and can interact with both Hsp90 and Hsp70 with similar affinities. International Journal of Biological Macromolecules, v. 118, p. 693-706, 2018Tradução . . Disponível em: https://doi.org/10.1016/j.ijbiomac.2018.06.123. Acesso em: 09 maio 2024.
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      Coto, A. L. de S., Seraphim, T. V., Batista, F. A. H., Dores-Silva, P. R., Barranco, A. B. F., Teixeira, F. R., et al. (2018). Structural and functional studies of the Leishmania braziliensis SGT co-chaperone indicate that it shares structural features with HIP and can interact with both Hsp90 and Hsp70 with similar affinities. International Journal of Biological Macromolecules, 118, 693-706. doi:10.1016/j.ijbiomac.2018.06.123
    • NLM

      Coto AL de S, Seraphim TV, Batista FAH, Dores-Silva PR, Barranco ABF, Teixeira FR, Lisandra M. Gava, Borges JC. Structural and functional studies of the Leishmania braziliensis SGT co-chaperone indicate that it shares structural features with HIP and can interact with both Hsp90 and Hsp70 with similar affinities [Internet]. International Journal of Biological Macromolecules. 2018 ;118 693-706.[citado 2024 maio 09 ] Available from: https://doi.org/10.1016/j.ijbiomac.2018.06.123
    • Vancouver

      Coto AL de S, Seraphim TV, Batista FAH, Dores-Silva PR, Barranco ABF, Teixeira FR, Lisandra M. Gava, Borges JC. Structural and functional studies of the Leishmania braziliensis SGT co-chaperone indicate that it shares structural features with HIP and can interact with both Hsp90 and Hsp70 with similar affinities [Internet]. International Journal of Biological Macromolecules. 2018 ;118 693-706.[citado 2024 maio 09 ] Available from: https://doi.org/10.1016/j.ijbiomac.2018.06.123
  • Source: International Journal of Biological Macromolecules. Unidades: IF, IQSC

    Assunto: LEISHMANIA

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      SERAPHIM, Thiago Vargas et al. Insights on the structural dynamics of Leishmania braziliensis Hsp90 molecular chaperone by small angle X-ray scattering. International Journal of Biological Macromolecules, v. 97, p. 503–512, 2017Tradução . . Disponível em: https://doi.org/10.1016/j.ijbiomac.2017.01.058. Acesso em: 09 maio 2024.
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      Seraphim, T. V., Silva, K. P. da, Dores-Silva, P. R. das, Barbosa, L. R. S., & Borges, J. C. (2017). Insights on the structural dynamics of Leishmania braziliensis Hsp90 molecular chaperone by small angle X-ray scattering. International Journal of Biological Macromolecules, 97, 503–512. doi:10.1016/j.ijbiomac.2017.01.058
    • NLM

      Seraphim TV, Silva KP da, Dores-Silva PR das, Barbosa LRS, Borges JC. Insights on the structural dynamics of Leishmania braziliensis Hsp90 molecular chaperone by small angle X-ray scattering [Internet]. International Journal of Biological Macromolecules. 2017 ; 97 503–512.[citado 2024 maio 09 ] Available from: https://doi.org/10.1016/j.ijbiomac.2017.01.058
    • Vancouver

      Seraphim TV, Silva KP da, Dores-Silva PR das, Barbosa LRS, Borges JC. Insights on the structural dynamics of Leishmania braziliensis Hsp90 molecular chaperone by small angle X-ray scattering [Internet]. International Journal of Biological Macromolecules. 2017 ; 97 503–512.[citado 2024 maio 09 ] Available from: https://doi.org/10.1016/j.ijbiomac.2017.01.058
  • Source: European Journal of Pharmaceutics and Biopharmaceutics. Unidade: IQSC

    Subjects: BIOLOGIA CELULAR, PROTEÍNAS

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      FERREIRA, Natália N. et al. Alginate hydrogel improves anti-angiogenic bevacizumab activity in cancer therapy. European Journal of Pharmaceutics and Biopharmaceutics, v. 119, p. 271-282, 2017Tradução . . Disponível em: https://doi.org/10.1016/j.ejpb.2017.06.028. Acesso em: 09 maio 2024.
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      Ferreira, N. N., Ferreira, L. M. N., Miranda-Gonçalves, V., Reis, R. M., Seraphim, T. V., Borges, J. C., et al. (2017). Alginate hydrogel improves anti-angiogenic bevacizumab activity in cancer therapy. European Journal of Pharmaceutics and Biopharmaceutics, 119, 271-282. doi:10.1016/j.ejpb.2017.06.028
    • NLM

      Ferreira NN, Ferreira LMN, Miranda-Gonçalves V, Reis RM, Seraphim TV, Borges JC, Baltazar F, Gremiao MPD. Alginate hydrogel improves anti-angiogenic bevacizumab activity in cancer therapy [Internet]. European Journal of Pharmaceutics and Biopharmaceutics. 2017 ; 119 271-282.[citado 2024 maio 09 ] Available from: https://doi.org/10.1016/j.ejpb.2017.06.028
    • Vancouver

      Ferreira NN, Ferreira LMN, Miranda-Gonçalves V, Reis RM, Seraphim TV, Borges JC, Baltazar F, Gremiao MPD. Alginate hydrogel improves anti-angiogenic bevacizumab activity in cancer therapy [Internet]. European Journal of Pharmaceutics and Biopharmaceutics. 2017 ; 119 271-282.[citado 2024 maio 09 ] Available from: https://doi.org/10.1016/j.ejpb.2017.06.028
  • Source: Current Protein and Peptide Science. Unidade: IQSC

    Assunto: PROTEÍNAS

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      BATISTA, Fernanda Aparecida Heleno et al. From Conformation to Interaction: Techniques to Explore the Hsp70/ Hsp90 Network. Current Protein and Peptide Science, v. 16, p. 735-753, 2015Tradução . . Disponível em: https://doi.org/10.2174/1389203716666150505225744. Acesso em: 09 maio 2024.
    • APA

      Batista, F. A. H., Gava, L. M., Pinheiro, G. M. S., Ramos, C. H. I., & Borges, J. C. (2015). From Conformation to Interaction: Techniques to Explore the Hsp70/ Hsp90 Network. Current Protein and Peptide Science, 16, 735-753. doi:10.2174/1389203716666150505225744
    • NLM

      Batista FAH, Gava LM, Pinheiro GMS, Ramos CHI, Borges JC. From Conformation to Interaction: Techniques to Explore the Hsp70/ Hsp90 Network [Internet]. Current Protein and Peptide Science. 2015 ; 16 735-753.[citado 2024 maio 09 ] Available from: https://doi.org/10.2174/1389203716666150505225744
    • Vancouver

      Batista FAH, Gava LM, Pinheiro GMS, Ramos CHI, Borges JC. From Conformation to Interaction: Techniques to Explore the Hsp70/ Hsp90 Network [Internet]. Current Protein and Peptide Science. 2015 ; 16 735-753.[citado 2024 maio 09 ] Available from: https://doi.org/10.2174/1389203716666150505225744
  • Source: The molecular chaperones interaction networks in protein folding and degradation. Unidade: IQSC

    Subjects: BIOLOGIA MOLECULAR, MALÁRIA

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      SERAPHIM, Thiago Vargas e RAMOS, Carlos Henrique Inacio e BORGES, Julio Cesar. The interaction networks of Hsp70 and Hsp90 in the plasmodium and leishmania parasites. The molecular chaperones interaction networks in protein folding and degradation. Tradução . New York: Springer, 2014. . Disponível em: http://link.springer.com/chapter/10.1007/978-1-4939-1130-1_17. Acesso em: 09 maio 2024.
    • APA

      Seraphim, T. V., Ramos, C. H. I., & Borges, J. C. (2014). The interaction networks of Hsp70 and Hsp90 in the plasmodium and leishmania parasites. In The molecular chaperones interaction networks in protein folding and degradation. New York: Springer. doi:10.1007/978-1-4939-1130-1_17
    • NLM

      Seraphim TV, Ramos CHI, Borges JC. The interaction networks of Hsp70 and Hsp90 in the plasmodium and leishmania parasites [Internet]. In: The molecular chaperones interaction networks in protein folding and degradation. New York: Springer; 2014. [citado 2024 maio 09 ] Available from: http://link.springer.com/chapter/10.1007/978-1-4939-1130-1_17
    • Vancouver

      Seraphim TV, Ramos CHI, Borges JC. The interaction networks of Hsp70 and Hsp90 in the plasmodium and leishmania parasites [Internet]. In: The molecular chaperones interaction networks in protein folding and degradation. New York: Springer; 2014. [citado 2024 maio 09 ] Available from: http://link.springer.com/chapter/10.1007/978-1-4939-1130-1_17
  • Source: Biochimica et Biophysica Acta. Unidade: IQSC

    Subjects: BIOFÍSICA, BIOLOGIA MOLECULAR

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      SILVA, Kelly Prata e SERAPHIM, T e BORGES, Julio Cesar. Structural and functional studies of leishmania braziliensis Hsp90. Biochimica et Biophysica Acta, v. 1834, n. 1, p. 351-361, 2013Tradução . . Disponível em: https://doi.org/10.1016/j.bbapap.2012.08.004. Acesso em: 09 maio 2024.
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      Silva, K. P., Seraphim, T., & Borges, J. C. (2013). Structural and functional studies of leishmania braziliensis Hsp90. Biochimica et Biophysica Acta, 1834( 1), 351-361. doi:10.1016/j.bbapap.2012.08.004
    • NLM

      Silva KP, Seraphim T, Borges JC. Structural and functional studies of leishmania braziliensis Hsp90 [Internet]. Biochimica et Biophysica Acta. 2013 ; 1834( 1): 351-361.[citado 2024 maio 09 ] Available from: https://doi.org/10.1016/j.bbapap.2012.08.004
    • Vancouver

      Silva KP, Seraphim T, Borges JC. Structural and functional studies of leishmania braziliensis Hsp90 [Internet]. Biochimica et Biophysica Acta. 2013 ; 1834( 1): 351-361.[citado 2024 maio 09 ] Available from: https://doi.org/10.1016/j.bbapap.2012.08.004
  • 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: 09 maio 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 maio 09 ] 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 maio 09 ] Available from: https://doi.org/10.1016/j.bpc.2013.08.004
  • Source: Protein and Peptide Letters. Unidade: IQSC

    Subjects: BIOLOGIA MOLECULAR, BIOQUÍMICA

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      SILVA, Kelly P da e BORGES, Julio Cesar. The molecular chaperone Hsp70 family members function by a bidirectional heterotrophic allosteric mechanism. Protein and Peptide Letters, v. 18, n. 2, p. 132-142, 2011Tradução . . Acesso em: 09 maio 2024.
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      Silva, K. P. da, & Borges, J. C. (2011). The molecular chaperone Hsp70 family members function by a bidirectional heterotrophic allosteric mechanism. Protein and Peptide Letters, 18( 2), 132-142.
    • NLM

      Silva KP da, Borges JC. The molecular chaperone Hsp70 family members function by a bidirectional heterotrophic allosteric mechanism. Protein and Peptide Letters. 2011 ; 18( 2): 132-142.[citado 2024 maio 09 ]
    • Vancouver

      Silva KP da, Borges JC. The molecular chaperone Hsp70 family members function by a bidirectional heterotrophic allosteric mechanism. Protein and Peptide Letters. 2011 ; 18( 2): 132-142.[citado 2024 maio 09 ]

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