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  • Source: Structure. Unidades: IQSC, IF

    Subjects: BIOQUÍMICA, BIOFÍSICA, MACROMOLÉCULA, PROTEÍNAS

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    • ABNT

      SERAPHIM, Thiago V et al. Assembly principles of the human R2TP chaperone complex reveal the presence of R2T and R2P complexes. Structure, v. 30, p. 156–171, 2022Tradução . . Disponível em: https://doi.org/10.1016/j.str.2021.08.002. Acesso em: 10 out. 2024.
    • APA

      Seraphim, T. V., Nano, N., Cheung, Y. W. S., Aluksanasuwan, S., Colleti, C., Mao, Y. -Q., et al. (2022). Assembly principles of the human R2TP chaperone complex reveal the presence of R2T and R2P complexes. Structure, 30, 156–171. doi:10.1016/j.str.2021.08.002
    • NLM

      Seraphim TV, Nano N, Cheung YWS, Aluksanasuwan S, Colleti C, Mao Y-Q, Bhandari V, Young G, Holl L, Phanse S, Gordiyenko Y, Southworth DR, Robinson CV, Thongboonkerd V, Gava LM, Borges JC, Babu M, Barbosa LRS, Ramos CHI, Kukura P, Houry WA. Assembly principles of the human R2TP chaperone complex reveal the presence of R2T and R2P complexes [Internet]. Structure. 2022 ; 30 156–171.[citado 2024 out. 10 ] Available from: https://doi.org/10.1016/j.str.2021.08.002
    • Vancouver

      Seraphim TV, Nano N, Cheung YWS, Aluksanasuwan S, Colleti C, Mao Y-Q, Bhandari V, Young G, Holl L, Phanse S, Gordiyenko Y, Southworth DR, Robinson CV, Thongboonkerd V, Gava LM, Borges JC, Babu M, Barbosa LRS, Ramos CHI, Kukura P, Houry WA. Assembly principles of the human R2TP chaperone complex reveal the presence of R2T and R2P complexes [Internet]. Structure. 2022 ; 30 156–171.[citado 2024 out. 10 ] Available from: https://doi.org/10.1016/j.str.2021.08.002
  • 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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    • ABNT

      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: 10 out. 2024.
    • APA

      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
    • NLM

      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 out. 10 ] 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 out. 10 ] 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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    • ABNT

      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: 10 out. 2024.
    • APA

      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
    • NLM

      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 out. 10 ] 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 out. 10 ] Available from: https://doi.org/10.1016/j.bbapap.2021.140719
  • 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: 10 out. 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 out. 10 ] 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 out. 10 ] Available from: https://doi.org/10.1016/j.bbapap.2019.140282
  • Source: Archives of Biochemistry and Biophysics. Unidades: IQSC, IF

    Assunto: PROTEÍNAS

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    • ABNT

      SILVA, Noeli Soares Melo da et al. Solution structure of Plasmodium falciparum Hsp90 indicates a high flexible dimer. Archives of Biochemistry and Biophysics, v. 690, p. 108468, 2020Tradução . . Disponível em: https://doi.org/10.1016/j.abb.2020.108468. Acesso em: 10 out. 2024.
    • APA

      Silva, N. S. M. da, Torricillas, M. da S., Minari, K., Barbosa, L. R. S., Seraphim, T. V., & Borges, J. C. (2020). Solution structure of Plasmodium falciparum Hsp90 indicates a high flexible dimer. Archives of Biochemistry and Biophysics, 690, 108468. doi:10.1016/j.abb.2020.108468
    • NLM

      Silva NSM da, Torricillas M da S, Minari K, Barbosa LRS, Seraphim TV, Borges JC. Solution structure of Plasmodium falciparum Hsp90 indicates a high flexible dimer [Internet]. Archives of Biochemistry and Biophysics. 2020 ; 690 108468.[citado 2024 out. 10 ] Available from: https://doi.org/10.1016/j.abb.2020.108468
    • Vancouver

      Silva NSM da, Torricillas M da S, Minari K, Barbosa LRS, Seraphim TV, Borges JC. Solution structure of Plasmodium falciparum Hsp90 indicates a high flexible dimer [Internet]. Archives of Biochemistry and Biophysics. 2020 ; 690 108468.[citado 2024 out. 10 ] Available from: https://doi.org/10.1016/j.abb.2020.108468
  • Source: Abstract Book. Conference titles: RAU Annual Users Meeting LNLS/CNPEM. Unidades: IQSC, IF

    Subjects: ESPALHAMENTO DE RAIOS X A BAIXOS ÂNGULOS, PROTEÍNAS

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    • ABNT

      RODRIGUES, Luiz F. C. et al. Teaching an old dog new tricks: new strategies for saxs data analysis of proteins in solution. 2020, Anais.. Campinas: Instituto de Química de São Carlos, Universidade de São Paulo, 2020. Disponível em: http://pages.cnpem.br/rau/wp-content/uploads/sites/8/2020/12/30thRAU_Abstract-BookV2.pdf. Acesso em: 10 out. 2024.
    • APA

      Rodrigues, L. F. C., Silva, N. S. M. da, Dores-Silva, P. R., Quel, N. G., Pinheiro, G. M. S., Borges, J. C., et al. (2020). Teaching an old dog new tricks: new strategies for saxs data analysis of proteins in solution. In Abstract Book. Campinas: Instituto de Química de São Carlos, Universidade de São Paulo. Recuperado de http://pages.cnpem.br/rau/wp-content/uploads/sites/8/2020/12/30thRAU_Abstract-BookV2.pdf
    • NLM

      Rodrigues LFC, Silva NSM da, Dores-Silva PR, Quel NG, Pinheiro GMS, Borges JC, Ramos CHI, Barbosa LRS. Teaching an old dog new tricks: new strategies for saxs data analysis of proteins in solution [Internet]. Abstract Book. 2020 ;[citado 2024 out. 10 ] Available from: http://pages.cnpem.br/rau/wp-content/uploads/sites/8/2020/12/30thRAU_Abstract-BookV2.pdf
    • Vancouver

      Rodrigues LFC, Silva NSM da, Dores-Silva PR, Quel NG, Pinheiro GMS, Borges JC, Ramos CHI, Barbosa LRS. Teaching an old dog new tricks: new strategies for saxs data analysis of proteins in solution [Internet]. Abstract Book. 2020 ;[citado 2024 out. 10 ] Available from: http://pages.cnpem.br/rau/wp-content/uploads/sites/8/2020/12/30thRAU_Abstract-BookV2.pdf
  • Source: International Journal of Biological Macromolecules. Unidades: IQSC, IF

    Assunto: PROTEÍNAS

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    • ABNT

      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: 10 out. 2024.
    • APA

      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 out. 10 ] 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 out. 10 ] Available from: https://doi.org/10.1016/j.ijbiomac.2018.11.130
  • Source: Biophysical Reviews. Unidades: IQSC, IF

    Subjects: PROTEÍNAS, BIOQUÍMICA CELULAR

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    • ABNT

      BORGES, Julio Cesar et al. A review of multi-domain and flexible molecular chaperones studies by small-angle X-ray scattering. Biophysical Reviews, 2016Tradução . . Disponível em: https://doi.org/10.1007/s12551-016-0194-x. Acesso em: 10 out. 2024.
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      Borges, J. C., Seraphim, T. V., Dores-Silva, P. R. das, & Barbosa, L. R. S. (2016). A review of multi-domain and flexible molecular chaperones studies by small-angle X-ray scattering. Biophysical Reviews. doi:10.1007/s12551-016-0194-x
    • NLM

      Borges JC, Seraphim TV, Dores-Silva PR das, Barbosa LRS. A review of multi-domain and flexible molecular chaperones studies by small-angle X-ray scattering [Internet]. Biophysical Reviews. 2016 ;[citado 2024 out. 10 ] Available from: https://doi.org/10.1007/s12551-016-0194-x
    • Vancouver

      Borges JC, Seraphim TV, Dores-Silva PR das, Barbosa LRS. A review of multi-domain and flexible molecular chaperones studies by small-angle X-ray scattering [Internet]. Biophysical Reviews. 2016 ;[citado 2024 out. 10 ] Available from: https://doi.org/10.1007/s12551-016-0194-x
  • Source: PLoS ONE. Unidades: IF, IQSC

    Assunto: PROTEÍNAS

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    • ABNT

      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: 10 out. 2024.
    • APA

      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
    • NLM

      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 out. 10 ] 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 out. 10 ] Available from: https://doi.org/10.1371/journal.pone.0117170
  • Source: PLoS ONE. Unidades: IF, IQSC

    Subjects: PROTEÍNAS, LEISHMANIA BRASILIENSIS

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    • ABNT

      SERAPHIM, Thiago Vargas et al. Low resolution structural studies indicate that the activator of Hsp90 ATPase 1 (Aha1) of leishmania braziliensis Has an elongated shape which allows its interaction with both N- and M-domains of Hsp90. PLoS ONE, v. 8, n. 6, p. e 66822, 2013Tradução . . Disponível em: https://doi.org/10.1371/journal.pone.0066822. Acesso em: 10 out. 2024.
    • APA

      Seraphim, T. V., Alves, M. M., Silva, I. M. da, Gomes, F. E. R., Silva, K. P., Murta, S. M. F., et al. (2013). Low resolution structural studies indicate that the activator of Hsp90 ATPase 1 (Aha1) of leishmania braziliensis Has an elongated shape which allows its interaction with both N- and M-domains of Hsp90. PLoS ONE, 8( 6), e 66822. doi:10.1371/journal.pone.0066822
    • NLM

      Seraphim TV, Alves MM, Silva IM da, Gomes FER, Silva KP, Murta SMF, Barbosa LRS, Borges JC. Low resolution structural studies indicate that the activator of Hsp90 ATPase 1 (Aha1) of leishmania braziliensis Has an elongated shape which allows its interaction with both N- and M-domains of Hsp90 [Internet]. PLoS ONE. 2013 ; 8( 6): e 66822.[citado 2024 out. 10 ] Available from: https://doi.org/10.1371/journal.pone.0066822
    • Vancouver

      Seraphim TV, Alves MM, Silva IM da, Gomes FER, Silva KP, Murta SMF, Barbosa LRS, Borges JC. Low resolution structural studies indicate that the activator of Hsp90 ATPase 1 (Aha1) of leishmania braziliensis Has an elongated shape which allows its interaction with both N- and M-domains of Hsp90 [Internet]. PLoS ONE. 2013 ; 8( 6): e 66822.[citado 2024 out. 10 ] Available from: https://doi.org/10.1371/journal.pone.0066822

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