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  • Source: Biochimica et Biophysica Acta - Proteins and Proteomics. Unidades: IF, IQSC, BIOINFORMÁTICA

    Assunto: PROTEÍNAS

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    • ABNT

      SILVA, Noeli Soares Melo da et al. Structural studies of the Hsp70/Hsp90 organizing protein of Plasmodium falciparum and its modulation of Hsp70 and Hsp90 ATPase activities. Biochimica et Biophysica Acta - Proteins and Proteomics, v. 1868, n. 1, p. 140282, 2020Tradução . . Disponível em: https://doi.org/10.1016/j.bbapap.2019.140282. Acesso em: 19 nov. 2024.
    • APA

      Silva, N. S. M. da, Reis, D. E. B., Silva, P. R. D., Annetta, F. B., Seraphim, T. V., Barbosa, L. R. S., & Borges, J. C. (2020). Structural studies of the Hsp70/Hsp90 organizing protein of Plasmodium falciparum and its modulation of Hsp70 and Hsp90 ATPase activities. Biochimica et Biophysica Acta - Proteins and Proteomics, 1868( 1), 140282. doi:10.1016/j.bbapap.2019.140282
    • NLM

      Silva NSM da, Reis DEB, Silva PRD, Annetta FB, Seraphim TV, Barbosa LRS, Borges JC. Structural studies of the Hsp70/Hsp90 organizing protein of Plasmodium falciparum and its modulation of Hsp70 and Hsp90 ATPase activities [Internet]. Biochimica et Biophysica Acta - Proteins and Proteomics. 2020 ; 1868( 1): 140282.[citado 2024 nov. 19 ] Available from: https://doi.org/10.1016/j.bbapap.2019.140282
    • Vancouver

      Silva NSM da, Reis DEB, Silva PRD, Annetta FB, Seraphim TV, Barbosa LRS, Borges JC. Structural studies of the Hsp70/Hsp90 organizing protein of Plasmodium falciparum and its modulation of Hsp70 and Hsp90 ATPase activities [Internet]. Biochimica et Biophysica Acta - Proteins and Proteomics. 2020 ; 1868( 1): 140282.[citado 2024 nov. 19 ] Available from: https://doi.org/10.1016/j.bbapap.2019.140282
  • Source: Journal of Enzyme Inhibition and Medicinal Chemistry. Unidade: IQSC

    Assunto: LEISHMANIA BRASILIENSIS

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      BATISTA, Fernanda A. H et al. Discovery of small molecule inhibitors of Leishmania braziliensis Hsp90 chaperone. Journal of Enzyme Inhibition and Medicinal Chemistry, v. 35, n. 1, p. 639-649, 2020Tradução . . Disponível em: https://doi.org/10.1080/14756366.2020.1726342. Acesso em: 19 nov. 2024.
    • APA

      Batista, F. A. H., Ramos Junior, S. L., Tassone, G., Leitão, A., Montanari, C. A., Botta, M., et al. (2020). Discovery of small molecule inhibitors of Leishmania braziliensis Hsp90 chaperone. Journal of Enzyme Inhibition and Medicinal Chemistry, 35( 1), 639-649. doi:10.1080/14756366.2020.1726342
    • NLM

      Batista FAH, Ramos Junior SL, Tassone G, Leitão A, Montanari CA, Botta M, Mori M, Borges JC. Discovery of small molecule inhibitors of Leishmania braziliensis Hsp90 chaperone [Internet]. Journal of Enzyme Inhibition and Medicinal Chemistry. 2020 ; 35( 1): 639-649.[citado 2024 nov. 19 ] Available from: https://doi.org/10.1080/14756366.2020.1726342
    • Vancouver

      Batista FAH, Ramos Junior SL, Tassone G, Leitão A, Montanari CA, Botta M, Mori M, Borges JC. Discovery of small molecule inhibitors of Leishmania braziliensis Hsp90 chaperone [Internet]. Journal of Enzyme Inhibition and Medicinal Chemistry. 2020 ; 35( 1): 639-649.[citado 2024 nov. 19 ] Available from: https://doi.org/10.1080/14756366.2020.1726342
  • Source: Cell Stress and Chaperones. Unidade: IQSC

    Assunto: PROTEÍNAS

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      SILVA, Paulo Roberto Dores et al. Interaction of HSPA5 (Grp78, BIP) with negatively charged phospholipid membranes via oligomerization involving the N-terminal end domain. Cell Stress and Chaperones, v. 25, p. 979–991, 2020Tradução . . Disponível em: https://doi.org/10.1007/s12192-020-01134-9. Acesso em: 19 nov. 2024.
    • APA

      Silva, P. R. D., Cauvi, D. M., Coto, A. L. de S., Kiraly, V. T. R., Borges, J. C., & Maio, A. D. (2020). Interaction of HSPA5 (Grp78, BIP) with negatively charged phospholipid membranes via oligomerization involving the N-terminal end domain. Cell Stress and Chaperones, 25, 979–991. doi:10.1007/s12192-020-01134-9
    • NLM

      Silva PRD, Cauvi DM, Coto AL de S, Kiraly VTR, Borges JC, Maio AD. Interaction of HSPA5 (Grp78, BIP) with negatively charged phospholipid membranes via oligomerization involving the N-terminal end domain [Internet]. Cell Stress and Chaperones. 2020 ; 25 979–991.[citado 2024 nov. 19 ] Available from: https://doi.org/10.1007/s12192-020-01134-9
    • Vancouver

      Silva PRD, Cauvi DM, Coto AL de S, Kiraly VTR, Borges JC, Maio AD. Interaction of HSPA5 (Grp78, BIP) with negatively charged phospholipid membranes via oligomerization involving the N-terminal end domain [Internet]. Cell Stress and Chaperones. 2020 ; 25 979–991.[citado 2024 nov. 19 ] Available from: https://doi.org/10.1007/s12192-020-01134-9
  • Source: International Journal of Biological Macromolecules. Unidade: IQSC

    Subjects: BIOQUÍMICA, BIOLOGIA MOLECULAR, PROTEÍNAS

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      KIRALY, Vanessa T. R et al. Thermal aggregates of human mortalin and Hsp70-1A behave as supramolecular assemblies. International Journal of Biological Macromolecules, v. 146, p. 320-331, 2020Tradução . . Disponível em: https://doi.org/10.1016/j.ijbiomac.2019.12.236. Acesso em: 19 nov. 2024.
    • APA

      Kiraly, V. T. R., Dores-Silva, P. R., Serrão, V. H. B., Cauvi, D. M., De Maio, A., & Borges, J. C. (2020). Thermal aggregates of human mortalin and Hsp70-1A behave as supramolecular assemblies. International Journal of Biological Macromolecules, 146, 320-331. doi:10.1016/j.ijbiomac.2019.12.236
    • NLM

      Kiraly VTR, Dores-Silva PR, Serrão VHB, Cauvi DM, De Maio A, Borges JC. Thermal aggregates of human mortalin and Hsp70-1A behave as supramolecular assemblies [Internet]. International Journal of Biological Macromolecules. 2020 ;146 320-331.[citado 2024 nov. 19 ] Available from: https://doi.org/10.1016/j.ijbiomac.2019.12.236
    • Vancouver

      Kiraly VTR, Dores-Silva PR, Serrão VHB, Cauvi DM, De Maio A, Borges JC. Thermal aggregates of human mortalin and Hsp70-1A behave as supramolecular assemblies [Internet]. International Journal of Biological Macromolecules. 2020 ;146 320-331.[citado 2024 nov. 19 ] Available from: https://doi.org/10.1016/j.ijbiomac.2019.12.236
  • Source: Current Proteomics. Unidade: IQSC

    Assunto: PROTEÍNAS

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      BATISTA, Fernanda A. H e DORES-SILVA, Paulo R e BORGES, Julio Cesar. Molecular Chaperones Involved in Protein Recovery from Aggregates are Present in Protozoa Causative of Malaria and Leishmaniasis. Current Proteomics, v. 16, p. 12-21, 2019Tradução . . Disponível em: https://doi.org/10.2174/1570164615666180626123823. Acesso em: 19 nov. 2024.
    • APA

      Batista, F. A. H., Dores-Silva, P. R., & Borges, J. C. (2019). Molecular Chaperones Involved in Protein Recovery from Aggregates are Present in Protozoa Causative of Malaria and Leishmaniasis. Current Proteomics, 16, 12-21. doi:10.2174/1570164615666180626123823
    • NLM

      Batista FAH, Dores-Silva PR, Borges JC. Molecular Chaperones Involved in Protein Recovery from Aggregates are Present in Protozoa Causative of Malaria and Leishmaniasis [Internet]. Current Proteomics. 2019 ;16 12-21.[citado 2024 nov. 19 ] Available from: https://doi.org/10.2174/1570164615666180626123823
    • Vancouver

      Batista FAH, Dores-Silva PR, Borges JC. Molecular Chaperones Involved in Protein Recovery from Aggregates are Present in Protozoa Causative of Malaria and Leishmaniasis [Internet]. Current Proteomics. 2019 ;16 12-21.[citado 2024 nov. 19 ] Available from: https://doi.org/10.2174/1570164615666180626123823
  • Source: International Journal of Biological Macromolecules. Unidades: IQSC, IF

    Assunto: PROTEÍNAS

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      TIROLI-CEPEDA, Ana Olivia et al. Studies on the effect of the J-domain on the substrate binding domain (SBD) of Hsp70 using a chimeric human J-SBD polypeptide. International Journal of Biological Macromolecules, v. 124, p. 111-120, 2019Tradução . . Disponível em: https://doi.org/10.1016/j.ijbiomac.2018.11.130. Acesso em: 19 nov. 2024.
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      Tiroli-Cepeda, A. O., Seraphim, T. V., Pinheiro, G. M. S., Souto, D. E. P., Kubota, L. T., Borges, J. C., et al. (2019). Studies on the effect of the J-domain on the substrate binding domain (SBD) of Hsp70 using a chimeric human J-SBD polypeptide. International Journal of Biological Macromolecules, 124, 111-120. doi:10.1016/j.ijbiomac.2018.11.130
    • NLM

      Tiroli-Cepeda AO, Seraphim TV, Pinheiro GMS, Souto DEP, Kubota LT, Borges JC, Barbosa LRS, Ramos CHI. Studies on the effect of the J-domain on the substrate binding domain (SBD) of Hsp70 using a chimeric human J-SBD polypeptide [Internet]. International Journal of Biological Macromolecules. 2019 ;124 111-120.[citado 2024 nov. 19 ] Available from: https://doi.org/10.1016/j.ijbiomac.2018.11.130
    • Vancouver

      Tiroli-Cepeda AO, Seraphim TV, Pinheiro GMS, Souto DEP, Kubota LT, Borges JC, Barbosa LRS, Ramos CHI. Studies on the effect of the J-domain on the substrate binding domain (SBD) of Hsp70 using a chimeric human J-SBD polypeptide [Internet]. International Journal of Biological Macromolecules. 2019 ;124 111-120.[citado 2024 nov. 19 ] Available from: https://doi.org/10.1016/j.ijbiomac.2018.11.130
  • Source: Current Proteomics. Unidade: IQSC

    Assunto: PROTEÍNAS

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      BORGES, Julio Cesar. Chaperones & Co:: roles in Protein/Nucleic Acid Homeostasis. [Editorial]. Current Proteomics. Sharjah, United Arab Emirates: Instituto de Química de São Carlos, Universidade de São Paulo. Disponível em: http://www.eurekaselect.com/166739/article. Acesso em: 19 nov. 2024. , 2019
    • APA

      Borges, J. C. (2019). Chaperones & Co:: roles in Protein/Nucleic Acid Homeostasis. [Editorial]. Current Proteomics. Sharjah, United Arab Emirates: Instituto de Química de São Carlos, Universidade de São Paulo. doi:10.2174/157016461601181029143029
    • NLM

      Borges JC. Chaperones & Co:: roles in Protein/Nucleic Acid Homeostasis. [Editorial] [Internet]. Current Proteomics. 2019 ;16( 1):3-4.[citado 2024 nov. 19 ] Available from: http://www.eurekaselect.com/166739/article
    • Vancouver

      Borges JC. Chaperones & Co:: roles in Protein/Nucleic Acid Homeostasis. [Editorial] [Internet]. Current Proteomics. 2019 ;16( 1):3-4.[citado 2024 nov. 19 ] Available from: http://www.eurekaselect.com/166739/article
  • Source: International Journal of Biological Macromolecules. Unidade: IQSC

    Subjects: LEISHMANIA BRASILIENSIS, PROTOZOA

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      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: 19 nov. 2024.
    • APA

      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 nov. 19 ] 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 nov. 19 ] Available from: https://doi.org/10.1016/j.ijbiomac.2018.06.123

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