Filtros : "IQSC" "Ramos, Carlos Henrique Inacio" Limpar

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  • Source: Abstract book. Conference titles: Annual Meeting of the Brazilian Society for Biochemistry and Molecular Biology - SBBq. Unidade: IQSC

    Subjects: BIOQUÍMICA, RESSONÂNCIA MAGNÉTICA NUCLEAR

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      AGUIAR, Samile Bezerra de et al. Production of the Human Hsp70-Escort Protein (hHep1) for Structural Analysis by NMR. 2022, Anais.. São Paulo: Instituto de Química de São Carlos, Universidade de São Paulo, 2022. Disponível em: https://repositorio.usp.br/directbitstream/ecf647eb-750b-4592-a314-85120427b92d/P20419.pdf. Acesso em: 23 abr. 2024.
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      Aguiar, S. B. de, Matos, C. O., Silva, N. S. M. da, Ramos, C. H. I., & Borges, J. C. (2022). Production of the Human Hsp70-Escort Protein (hHep1) for Structural Analysis by NMR. In Abstract book. São Paulo: Instituto de Química de São Carlos, Universidade de São Paulo. Recuperado de https://repositorio.usp.br/directbitstream/ecf647eb-750b-4592-a314-85120427b92d/P20419.pdf
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      Aguiar SB de, Matos CO, Silva NSM da, Ramos CHI, Borges JC. Production of the Human Hsp70-Escort Protein (hHep1) for Structural Analysis by NMR [Internet]. Abstract book. 2022 ;[citado 2024 abr. 23 ] Available from: https://repositorio.usp.br/directbitstream/ecf647eb-750b-4592-a314-85120427b92d/P20419.pdf
    • Vancouver

      Aguiar SB de, Matos CO, Silva NSM da, Ramos CHI, Borges JC. Production of the Human Hsp70-Escort Protein (hHep1) for Structural Analysis by NMR [Internet]. Abstract book. 2022 ;[citado 2024 abr. 23 ] Available from: https://repositorio.usp.br/directbitstream/ecf647eb-750b-4592-a314-85120427b92d/P20419.pdf
  • Source: Abstract book. Conference titles: Annual Meeting of the Brazilian Society for Biochemistry and Molecular Biology - SBBq. Unidade: IQSC

    Subjects: BIOQUÍMICA, PROTEÍNAS, MITOCÔNDRIAS

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      SANTOS, Eduardo Feliciano de Lima et al. Studies on mitochondrial chaperone system proteins TRAP-1 and CyP-D, characterization e interaction. 2022, Anais.. São Paulo: Instituto de Química de São Carlos, Universidade de São Paulo, 2022. Disponível em: https://repositorio.usp.br/directbitstream/bbdb4919-9b18-41b8-8c90-a3011ad59ac7/P20421.pdf. Acesso em: 23 abr. 2024.
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      Santos, E. F. de L., Giudice, M. del, Libardi, S. H., Ramos, C. H. I., Borges, J. C., & Borges, L. M. G. (2022). Studies on mitochondrial chaperone system proteins TRAP-1 and CyP-D, characterization e interaction. In Abstract book. São Paulo: Instituto de Química de São Carlos, Universidade de São Paulo. Recuperado de https://repositorio.usp.br/directbitstream/bbdb4919-9b18-41b8-8c90-a3011ad59ac7/P20421.pdf
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      Santos EF de L, Giudice M del, Libardi SH, Ramos CHI, Borges JC, Borges LMG. Studies on mitochondrial chaperone system proteins TRAP-1 and CyP-D, characterization e interaction [Internet]. Abstract book. 2022 ;[citado 2024 abr. 23 ] Available from: https://repositorio.usp.br/directbitstream/bbdb4919-9b18-41b8-8c90-a3011ad59ac7/P20421.pdf
    • Vancouver

      Santos EF de L, Giudice M del, Libardi SH, Ramos CHI, Borges JC, Borges LMG. Studies on mitochondrial chaperone system proteins TRAP-1 and CyP-D, characterization e interaction [Internet]. Abstract book. 2022 ;[citado 2024 abr. 23 ] Available from: https://repositorio.usp.br/directbitstream/bbdb4919-9b18-41b8-8c90-a3011ad59ac7/P20421.pdf
  • Source: Abstract book. Conference titles: Annual Meeting of the Brazilian Society for Biochemistry and Molecular Biology - SBBq. Unidades: IQSC, IF

    Assunto: PROTEÍNAS

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      RODRIGUES, Luiz Fernando de Camargo et al. Small Angle X-Ray Scattering (SAXS) As Tool For Obtaining Insights And Structural Models Of Molecular Chaperones: Recent Results And Perspectives. 2022, Anais.. São Paulo: Instituto de Química de São Carlos, Universidade de São Paulo, 2022. Disponível em: https://repositorio.usp.br/directbitstream/b0942c5e-3377-432c-b2e8-e1d3ccae61eb/P20429.pdf. Acesso em: 23 abr. 2024.
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      Rodrigues, L. F. de C., Borges, J. C., Ramos, C. H. I., & Barbosa, L. R. S. (2022). Small Angle X-Ray Scattering (SAXS) As Tool For Obtaining Insights And Structural Models Of Molecular Chaperones: Recent Results And Perspectives. In Abstract book. São Paulo: Instituto de Química de São Carlos, Universidade de São Paulo. Recuperado de https://repositorio.usp.br/directbitstream/b0942c5e-3377-432c-b2e8-e1d3ccae61eb/P20429.pdf
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      Rodrigues LF de C, Borges JC, Ramos CHI, Barbosa LRS. Small Angle X-Ray Scattering (SAXS) As Tool For Obtaining Insights And Structural Models Of Molecular Chaperones: Recent Results And Perspectives [Internet]. Abstract book. 2022 ;[citado 2024 abr. 23 ] Available from: https://repositorio.usp.br/directbitstream/b0942c5e-3377-432c-b2e8-e1d3ccae61eb/P20429.pdf
    • Vancouver

      Rodrigues LF de C, Borges JC, Ramos CHI, Barbosa LRS. Small Angle X-Ray Scattering (SAXS) As Tool For Obtaining Insights And Structural Models Of Molecular Chaperones: Recent Results And Perspectives [Internet]. Abstract book. 2022 ;[citado 2024 abr. 23 ] Available from: https://repositorio.usp.br/directbitstream/b0942c5e-3377-432c-b2e8-e1d3ccae61eb/P20429.pdf
  • Source: Biochimica et Biophysica Acta - Proteins and Proteomics. Unidades: IQSC, IF, FM

    Subjects: BIOQUÍMICA, PROTEÍNAS

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      SILVA, Noeli Soares Melo da et al. Structural, thermodynamic and functional studies of human 71 kDa heat shock cognate protein (HSPA8/hHsc70). Biochimica et Biophysica Acta - Proteins and Proteomics, v. 1869, 2021Tradução . . Disponível em: https://doi.org/10.1016/j.bbapap.2021.140719. Acesso em: 23 abr. 2024.
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      Silva, N. S. M. da, Rodrigues, L. F. de C., Silva, P. R. D., Montanari, C. A., Ramos, C. H. I., Barbosa, L. R. S., & Borges, J. C. (2021). Structural, thermodynamic and functional studies of human 71 kDa heat shock cognate protein (HSPA8/hHsc70). Biochimica et Biophysica Acta - Proteins and Proteomics, 1869. doi:10.1016/j.bbapap.2021.140719
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      Silva NSM da, Rodrigues LF de C, Silva PRD, Montanari CA, Ramos CHI, Barbosa LRS, Borges JC. Structural, thermodynamic and functional studies of human 71 kDa heat shock cognate protein (HSPA8/hHsc70) [Internet]. Biochimica et Biophysica Acta - Proteins and Proteomics. 2021 ; 1869[citado 2024 abr. 23 ] Available from: https://doi.org/10.1016/j.bbapap.2021.140719
    • Vancouver

      Silva NSM da, Rodrigues LF de C, Silva PRD, Montanari CA, Ramos CHI, Barbosa LRS, Borges JC. Structural, thermodynamic and functional studies of human 71 kDa heat shock cognate protein (HSPA8/hHsc70) [Internet]. Biochimica et Biophysica Acta - Proteins and Proteomics. 2021 ; 1869[citado 2024 abr. 23 ] Available from: https://doi.org/10.1016/j.bbapap.2021.140719
  • Source: International Journal of Biological Macromolecules. Unidades: IQSC, IFSC

    Assunto: PROTEÍNAS

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      MINARI, Karine et al. Thermodynamic analysis of interactions of the Hsp90 with adenosine nucleotides: a comparative perspective. International Journal of Biological Macromolecules, v. 130, p. 125-138, 2019Tradução . . Disponível em: https://doi.org/10.1016/j.ijbiomac.2019.02.116. Acesso em: 23 abr. 2024.
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      Minari, K., Azevedo, É. C. de, Kiraly, V. T. R., Batista, F. A. H., Moraes, F. R., Melo, F. A. de, et al. (2019). Thermodynamic analysis of interactions of the Hsp90 with adenosine nucleotides: a comparative perspective. International Journal of Biological Macromolecules, 130, 125-138. doi:10.1016/j.ijbiomac.2019.02.116
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      Minari K, Azevedo ÉC de, Kiraly VTR, Batista FAH, Moraes FR, Melo FA de, Nascimento AS, Gava LM, Ramos CHI, Borges JC. Thermodynamic analysis of interactions of the Hsp90 with adenosine nucleotides: a comparative perspective [Internet]. International Journal of Biological Macromolecules. 2019 ;130 125-138.[citado 2024 abr. 23 ] Available from: https://doi.org/10.1016/j.ijbiomac.2019.02.116
    • Vancouver

      Minari K, Azevedo ÉC de, Kiraly VTR, Batista FAH, Moraes FR, Melo FA de, Nascimento AS, Gava LM, Ramos CHI, Borges JC. Thermodynamic analysis of interactions of the Hsp90 with adenosine nucleotides: a comparative perspective [Internet]. International Journal of Biological Macromolecules. 2019 ;130 125-138.[citado 2024 abr. 23 ] Available from: https://doi.org/10.1016/j.ijbiomac.2019.02.116
  • Source: Frontiers in structural biology: Role of molecular chaperones in structural, biological functions, and drug interactions of client proteins. Unidade: IQSC

    Assunto: PROTEÍNAS

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      BORGES, Julio Cesar e RAMOS, Carlos Henrique Inacio. Quaternary structure of chaperones from the Hsp70 system determined by samll angel x-ray scattering (SAXS) and analytical ultracentrifugation. Frontiers in structural biology: Role of molecular chaperones in structural, biological functions, and drug interactions of client proteins. Tradução . Sharjah: Instituto de Química de São Carlos, Universidade de São Paulo, 2018. v. 1. . Disponível em: https://doi.org/10.2174/97816810861561180101. Acesso em: 23 abr. 2024.
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      Borges, J. C., & Ramos, C. H. I. (2018). Quaternary structure of chaperones from the Hsp70 system determined by samll angel x-ray scattering (SAXS) and analytical ultracentrifugation. In Frontiers in structural biology: Role of molecular chaperones in structural, biological functions, and drug interactions of client proteins (Vol. 1). Sharjah: Instituto de Química de São Carlos, Universidade de São Paulo. doi:10.2174/97816810861561180101
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      Borges JC, Ramos CHI. Quaternary structure of chaperones from the Hsp70 system determined by samll angel x-ray scattering (SAXS) and analytical ultracentrifugation [Internet]. In: Frontiers in structural biology: Role of molecular chaperones in structural, biological functions, and drug interactions of client proteins. Sharjah: Instituto de Química de São Carlos, Universidade de São Paulo; 2018. [citado 2024 abr. 23 ] Available from: https://doi.org/10.2174/97816810861561180101
    • Vancouver

      Borges JC, Ramos CHI. Quaternary structure of chaperones from the Hsp70 system determined by samll angel x-ray scattering (SAXS) and analytical ultracentrifugation [Internet]. In: Frontiers in structural biology: Role of molecular chaperones in structural, biological functions, and drug interactions of client proteins. Sharjah: Instituto de Química de São Carlos, Universidade de São Paulo; 2018. [citado 2024 abr. 23 ] Available from: https://doi.org/10.2174/97816810861561180101
  • Source: Archives Biochemistry and Biophysics. Unidades: IF, IQSC

    Assunto: LEISHMANIA BRASILIENSIS

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      BATISTA, Fernanda Aparecida Heleno et al. Low sequence identity but high structural and functional conservation: The case of Hsp70/Hsp90 organizing protein (Hop/Sti1) of Leishmania braziliensis. Archives Biochemistry and Biophysics, v. 600, p. 12-22, 2016Tradução . . Disponível em: https://doi.org/10.1016/j.abb.2016.04.008. Acesso em: 23 abr. 2024.
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      Batista, F. A. H., Seraphim, T. V., Santos, C. A. dos, Gonzaga, M. R., Barbosa, L. R. S., Ramos, C. H. I., & Borges, J. C. (2016). Low sequence identity but high structural and functional conservation: The case of Hsp70/Hsp90 organizing protein (Hop/Sti1) of Leishmania braziliensis. Archives Biochemistry and Biophysics, 600, 12-22. doi:10.1016/j.abb.2016.04.008
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      Batista FAH, Seraphim TV, Santos CA dos, Gonzaga MR, Barbosa LRS, Ramos CHI, Borges JC. Low sequence identity but high structural and functional conservation: The case of Hsp70/Hsp90 organizing protein (Hop/Sti1) of Leishmania braziliensis [Internet]. Archives Biochemistry and Biophysics. 2016 ; 600 12-22.[citado 2024 abr. 23 ] Available from: https://doi.org/10.1016/j.abb.2016.04.008
    • Vancouver

      Batista FAH, Seraphim TV, Santos CA dos, Gonzaga MR, Barbosa LRS, Ramos CHI, Borges JC. Low sequence identity but high structural and functional conservation: The case of Hsp70/Hsp90 organizing protein (Hop/Sti1) of Leishmania braziliensis [Internet]. Archives Biochemistry and Biophysics. 2016 ; 600 12-22.[citado 2024 abr. 23 ] Available from: https://doi.org/10.1016/j.abb.2016.04.008
  • Source: Livro de resumos. Conference titles: Congress of the International Union for Biochemistry and Molecular Biology - UBMB. Unidade: IQSC

    Subjects: PROTEÍNAS, BIOQUÍMICA

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      DORES-SILVA, Paulo Roberto das e RAMOS, Carlos Henrique Inacio e BORGES, Julio Cesar. Human mortalin (mtHsp70) agrregates at lower temperatures than cytoplasmic counterpart Hsp70-1A. 2015, Anais.. São Paulo: Instituto de Química de São Carlos, Universidade de São Paulo, 2015. Disponível em: https://repositorio.usp.br/directbitstream/5c7d5345-3515-4c1d-af3e-db6651bb90be/P15912.pdf. Acesso em: 23 abr. 2024.
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      Dores-Silva, P. R. das, Ramos, C. H. I., & Borges, J. C. (2015). Human mortalin (mtHsp70) agrregates at lower temperatures than cytoplasmic counterpart Hsp70-1A. In Livro de resumos. São Paulo: Instituto de Química de São Carlos, Universidade de São Paulo. Recuperado de https://repositorio.usp.br/directbitstream/5c7d5345-3515-4c1d-af3e-db6651bb90be/P15912.pdf
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      Dores-Silva PR das, Ramos CHI, Borges JC. Human mortalin (mtHsp70) agrregates at lower temperatures than cytoplasmic counterpart Hsp70-1A [Internet]. Livro de resumos. 2015 ;[citado 2024 abr. 23 ] Available from: https://repositorio.usp.br/directbitstream/5c7d5345-3515-4c1d-af3e-db6651bb90be/P15912.pdf
    • Vancouver

      Dores-Silva PR das, Ramos CHI, Borges JC. Human mortalin (mtHsp70) agrregates at lower temperatures than cytoplasmic counterpart Hsp70-1A [Internet]. Livro de resumos. 2015 ;[citado 2024 abr. 23 ] Available from: https://repositorio.usp.br/directbitstream/5c7d5345-3515-4c1d-af3e-db6651bb90be/P15912.pdf
  • Source: PLOS ONE. Unidades: IF, IQSC

    Assunto: PROTEÍNAS

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      DORES-SILVA, Paulo Roberto das et al. Human mitochondrial Hsp70 (Mortalin): shedding light on ATPase activity, interaction with adenosine nucleotides, solution structure and domain organization. PLOS ONE, v. 10, n. 1, 2015Tradução . . Disponível em: https://doi.org/10.1371/journal.pone.0117170. Acesso em: 23 abr. 2024.
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      Dores-Silva, P. R. das, Barbosa, L. R. S., Ramos, C. H. I., & Borges, J. C. (2015). Human mitochondrial Hsp70 (Mortalin): shedding light on ATPase activity, interaction with adenosine nucleotides, solution structure and domain organization. PLOS ONE, 10( 1). doi:10.1371/journal.pone.0117170
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      Dores-Silva PR das, Barbosa LRS, Ramos CHI, Borges JC. Human mitochondrial Hsp70 (Mortalin): shedding light on ATPase activity, interaction with adenosine nucleotides, solution structure and domain organization [Internet]. PLOS ONE. 2015 ; 10( 1):[citado 2024 abr. 23 ] Available from: https://doi.org/10.1371/journal.pone.0117170
    • Vancouver

      Dores-Silva PR das, Barbosa LRS, Ramos CHI, Borges JC. Human mitochondrial Hsp70 (Mortalin): shedding light on ATPase activity, interaction with adenosine nucleotides, solution structure and domain organization [Internet]. PLOS ONE. 2015 ; 10( 1):[citado 2024 abr. 23 ] Available from: https://doi.org/10.1371/journal.pone.0117170
  • 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: 23 abr. 2024.
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      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
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      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 abr. 23 ] Available from: https://doi.org/10.2174/1389203716666150505225744
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      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 abr. 23 ] Available from: https://doi.org/10.2174/1389203716666150505225744
  • Conference titles: Congress of the International Union for Biochemistry and Molecular Biology - UBMB. Unidade: IQSC

    Assunto: BIOQUÍMICA

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      COLLETI, Carolina et al. Effects of curcumin on HSP90 protein stability. 2015, Anais.. São Paulo: Instituto de Química de São Carlos, Universidade de São Paulo, 2015. Disponível em: https://repositorio.usp.br/directbitstream/b497090a-bcc9-461a-8640-21614195b67b/P15911.pdf. Acesso em: 23 abr. 2024.
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      Colleti, C., Borges, J. C., Ramos, C. H. I., & Gava, L. M. (2015). Effects of curcumin on HSP90 protein stability. In . São Paulo: Instituto de Química de São Carlos, Universidade de São Paulo. Recuperado de https://repositorio.usp.br/directbitstream/b497090a-bcc9-461a-8640-21614195b67b/P15911.pdf
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      Colleti C, Borges JC, Ramos CHI, Gava LM. Effects of curcumin on HSP90 protein stability [Internet]. 2015 ;[citado 2024 abr. 23 ] Available from: https://repositorio.usp.br/directbitstream/b497090a-bcc9-461a-8640-21614195b67b/P15911.pdf
    • Vancouver

      Colleti C, Borges JC, Ramos CHI, Gava LM. Effects of curcumin on HSP90 protein stability [Internet]. 2015 ;[citado 2024 abr. 23 ] Available from: https://repositorio.usp.br/directbitstream/b497090a-bcc9-461a-8640-21614195b67b/P15911.pdf
  • Source: Archives of Biochemistry and Biophysics. Unidades: IQSC, IF

    Subjects: BIOFÍSICA, BIOLOGIA MOLECULAR

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      SERAPHIM, Thiago Vargas et al. The C-terminal region of the human p23 chaperone modulates its structure and function. Archives of Biochemistry and Biophysics, v. 565, p. 57-67, 2015Tradução . . Disponível em: https://doi.org/10.1016/j.abb.2014.10.015. Acesso em: 23 abr. 2024.
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      Seraphim, T. V., Gava, L. M., Mokry, D. Z., Cagliari, T. D., Barbosa, L. R. S., Ramos, C. H. I., & Borges, J. C. (2015). The C-terminal region of the human p23 chaperone modulates its structure and function. Archives of Biochemistry and Biophysics, 565, 57-67. doi:10.1016/j.abb.2014.10.015
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      Seraphim TV, Gava LM, Mokry DZ, Cagliari TD, Barbosa LRS, Ramos CHI, Borges JC. The C-terminal region of the human p23 chaperone modulates its structure and function [Internet]. Archives of Biochemistry and Biophysics. 2015 ; 565 57-67.[citado 2024 abr. 23 ] Available from: https://doi.org/10.1016/j.abb.2014.10.015
    • Vancouver

      Seraphim TV, Gava LM, Mokry DZ, Cagliari TD, Barbosa LRS, Ramos CHI, Borges JC. The C-terminal region of the human p23 chaperone modulates its structure and function [Internet]. Archives of Biochemistry and Biophysics. 2015 ; 565 57-67.[citado 2024 abr. 23 ] Available from: https://doi.org/10.1016/j.abb.2014.10.015
  • 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: 23 abr. 2024.
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      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
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      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 abr. 23 ] 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 abr. 23 ] Available from: http://link.springer.com/chapter/10.1007/978-1-4939-1130-1_17
  • Source: Biochemistry. Unidade: IQSC

    Assunto: BIOLOGIA MOLECULAR

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      ARAUJO, Thaís L. S. et al. Conformational changes in human Hsp70 induced by high hydrostatic pressure produce oligomers with ATPase activity but without chaperone activity. Biochemistry, v. 53, n. 18, p. 2884-2889, 2014Tradução . . Disponível em: https://doi.org/10.1021/bi500004q. Acesso em: 23 abr. 2024.
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      Araujo, T. L. S., Borges, J. C., Ramos, C. H. I., Meyer-Fernandes, J. R., Oliveira Júnior, R. S., Pascutti, P. G., et al. (2014). Conformational changes in human Hsp70 induced by high hydrostatic pressure produce oligomers with ATPase activity but without chaperone activity. Biochemistry, 53( 18), 2884-2889. doi:10.1021/bi500004q
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      Araujo TLS, Borges JC, Ramos CHI, Meyer-Fernandes JR, Oliveira Júnior RS, Pascutti PG, Foguel D, Palhano FL. Conformational changes in human Hsp70 induced by high hydrostatic pressure produce oligomers with ATPase activity but without chaperone activity [Internet]. Biochemistry. 2014 ; 53( 18): 2884-2889.[citado 2024 abr. 23 ] Available from: https://doi.org/10.1021/bi500004q
    • Vancouver

      Araujo TLS, Borges JC, Ramos CHI, Meyer-Fernandes JR, Oliveira Júnior RS, Pascutti PG, Foguel D, Palhano FL. Conformational changes in human Hsp70 induced by high hydrostatic pressure produce oligomers with ATPase activity but without chaperone activity [Internet]. Biochemistry. 2014 ; 53( 18): 2884-2889.[citado 2024 abr. 23 ] Available from: https://doi.org/10.1021/bi500004q
  • Source: International Journal of Biological Macromolecules. Unidades: IF, IQSC

    Assunto: BIOLOGIA MOLECULAR

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      DORES-SILVA, Paulo Roberto et al. Structural and stability studies of the human mtHsp70-escort protein 1: an essential mortalin co-chaperone. International Journal of Biological Macromolecules, v. 56, p. 140-148, 2013Tradução . . Disponível em: https://doi.org/10.1016/j.ijbiomac.2013.02.009. Acesso em: 23 abr. 2024.
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      Dores-Silva, P. R., Minari, K., Ramos, C. H. I., Barbosa, L. R. S., & Borges, J. C. (2013). Structural and stability studies of the human mtHsp70-escort protein 1: an essential mortalin co-chaperone. International Journal of Biological Macromolecules, 56, 140-148. doi:10.1016/j.ijbiomac.2013.02.009
    • NLM

      Dores-Silva PR, Minari K, Ramos CHI, Barbosa LRS, Borges JC. Structural and stability studies of the human mtHsp70-escort protein 1: an essential mortalin co-chaperone [Internet]. International Journal of Biological Macromolecules. 2013 ; 56 140-148.[citado 2024 abr. 23 ] Available from: https://doi.org/10.1016/j.ijbiomac.2013.02.009
    • Vancouver

      Dores-Silva PR, Minari K, Ramos CHI, Barbosa LRS, Borges JC. Structural and stability studies of the human mtHsp70-escort protein 1: an essential mortalin co-chaperone [Internet]. International Journal of Biological Macromolecules. 2013 ; 56 140-148.[citado 2024 abr. 23 ] Available from: https://doi.org/10.1016/j.ijbiomac.2013.02.009
  • Source: PLOS ONE. Unidade: IQSC

    Assunto: PROTEÍNAS

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    • ABNT

      BORGES, Julio Cesar et al. Identification of regions involved in substrate binding and dimer stabilization within the central domains of yeast Hsp40 Sis1. PLOS ONE, v. 7, n. 12, p. e50927, 2012Tradução . . Disponível em: https://doi.org/10.1371/journal.pone.0050927. Acesso em: 23 abr. 2024.
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      Borges, J. C., Seraphim, T. V., Mokry, D. Z., Almeida, F. C. L. de, Cyr, D. M., & Ramos, C. H. I. (2012). Identification of regions involved in substrate binding and dimer stabilization within the central domains of yeast Hsp40 Sis1. PLOS ONE, 7( 12), e50927. doi:10.1371/journal.pone.0050927
    • NLM

      Borges JC, Seraphim TV, Mokry DZ, Almeida FCL de, Cyr DM, Ramos CHI. Identification of regions involved in substrate binding and dimer stabilization within the central domains of yeast Hsp40 Sis1 [Internet]. PLOS ONE. 2012 ; 7( 12): e50927.[citado 2024 abr. 23 ] Available from: https://doi.org/10.1371/journal.pone.0050927
    • Vancouver

      Borges JC, Seraphim TV, Mokry DZ, Almeida FCL de, Cyr DM, Ramos CHI. Identification of regions involved in substrate binding and dimer stabilization within the central domains of yeast Hsp40 Sis1 [Internet]. PLOS ONE. 2012 ; 7( 12): e50927.[citado 2024 abr. 23 ] Available from: https://doi.org/10.1371/journal.pone.0050927
  • Source: BMC Structure Biology. Unidade: IQSC

    Assunto: BIOLOGIA MOLECULAR

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    • ABNT

      SILVA, Julio C et al. Central domain deletions affect the SAXS solution structure and function of yeast Hsp40 proteins Sis1 and Ydj1. BMC Structure Biology, v. 11, 2011Tradução . . Disponível em: https://doi.org/10.1186/1472-6807-11-40. Acesso em: 23 abr. 2024.
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      Silva, J. C., Borges, J. C., Cyr, D. M., Ramos, C. H. I., & Torriani, I. L. (2011). Central domain deletions affect the SAXS solution structure and function of yeast Hsp40 proteins Sis1 and Ydj1. BMC Structure Biology, 11. doi:10.1186/1472-6807-11-40
    • NLM

      Silva JC, Borges JC, Cyr DM, Ramos CHI, Torriani IL. Central domain deletions affect the SAXS solution structure and function of yeast Hsp40 proteins Sis1 and Ydj1 [Internet]. BMC Structure Biology. 2011 ; 11[citado 2024 abr. 23 ] Available from: https://doi.org/10.1186/1472-6807-11-40
    • Vancouver

      Silva JC, Borges JC, Cyr DM, Ramos CHI, Torriani IL. Central domain deletions affect the SAXS solution structure and function of yeast Hsp40 proteins Sis1 and Ydj1 [Internet]. BMC Structure Biology. 2011 ; 11[citado 2024 abr. 23 ] Available from: https://doi.org/10.1186/1472-6807-11-40
  • Source: Archives of Biochemistry and Biophysics. Unidade: IQSC

    Subjects: BIOFÍSICA, BIOLOGIA MOLECULAR

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      GAVA, Lisandra M et al. Stoichiometry and thermodynamics of the interaction between the C-terminus of human 90KDa heat schock protein Hsp90 and the mitochondrial translocase of outer membrane Tom70. Archives of Biochemistry and Biophysics, v. 513, n. 2, p. 119-125, 2011Tradução . . Disponível em: https://doi.org/10.1016/j.abb.2011.06.015. Acesso em: 23 abr. 2024.
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      Gava, L. M., Gonçalves, D. C., Borges, J. C., & Ramos, C. H. I. (2011). Stoichiometry and thermodynamics of the interaction between the C-terminus of human 90KDa heat schock protein Hsp90 and the mitochondrial translocase of outer membrane Tom70. Archives of Biochemistry and Biophysics, 513( 2), 119-125. doi:10.1016/j.abb.2011.06.015
    • NLM

      Gava LM, Gonçalves DC, Borges JC, Ramos CHI. Stoichiometry and thermodynamics of the interaction between the C-terminus of human 90KDa heat schock protein Hsp90 and the mitochondrial translocase of outer membrane Tom70 [Internet]. Archives of Biochemistry and Biophysics. 2011 ; 513( 2): 119-125.[citado 2024 abr. 23 ] Available from: https://doi.org/10.1016/j.abb.2011.06.015
    • Vancouver

      Gava LM, Gonçalves DC, Borges JC, Ramos CHI. Stoichiometry and thermodynamics of the interaction between the C-terminus of human 90KDa heat schock protein Hsp90 and the mitochondrial translocase of outer membrane Tom70 [Internet]. Archives of Biochemistry and Biophysics. 2011 ; 513( 2): 119-125.[citado 2024 abr. 23 ] Available from: https://doi.org/10.1016/j.abb.2011.06.015
  • Source: Activity Report 2008. Unidades: IQSC, FMRP

    Subjects: BIOLOGIA MOLECULAR, RAIOS X

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      BRESSAN, Gustavo Costa et al. X-ray structural low-resolution features and functional insights to human Ki-1/57: an intrinsically unstructured protein that localizes to nuclear bodies related with RNA metabolism. Activity Report 2008, p. 23-25, 2009Tradução . . Acesso em: 23 abr. 2024.
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      Bressan, G. C., Silva, J. C., Borges, J. C., Passos, D. O. dos, Ramos, C. H. I., Quaresma, A. J. C., et al. (2009). X-ray structural low-resolution features and functional insights to human Ki-1/57: an intrinsically unstructured protein that localizes to nuclear bodies related with RNA metabolism. Activity Report 2008, 23-25.
    • NLM

      Bressan GC, Silva JC, Borges JC, Passos DO dos, Ramos CHI, Quaresma AJC, Moraes EC, Manfioli AO, Gomes MD, Torriani ICL de, Kobarg J. X-ray structural low-resolution features and functional insights to human Ki-1/57: an intrinsically unstructured protein that localizes to nuclear bodies related with RNA metabolism. Activity Report 2008. 2009 ; 23-25.[citado 2024 abr. 23 ]
    • Vancouver

      Bressan GC, Silva JC, Borges JC, Passos DO dos, Ramos CHI, Quaresma AJC, Moraes EC, Manfioli AO, Gomes MD, Torriani ICL de, Kobarg J. X-ray structural low-resolution features and functional insights to human Ki-1/57: an intrinsically unstructured protein that localizes to nuclear bodies related with RNA metabolism. Activity Report 2008. 2009 ; 23-25.[citado 2024 abr. 23 ]

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