Filtros : "PROTEÍNAS" "ITRI, ROSANGELA" Removidos: "SHS" "gh" Limpar

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  • Source: European Biophysics Journal. Conference titles: European Biophysics Congress - EBSA. Unidades: IFSC, IF

    Subjects: PROTEÍNAS, TERMODINÂMICA, CRISTALOGRAFIA

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      KUMAGAI, Patricia Suemy et al. Physiological septin-septin interactions prevents amyloid filaments formation. European Biophysics Journal. Heidelberg: Springer. Disponível em: https://doi.org/10.1007/s00249-019-01373-4. Acesso em: 03 jul. 2024. , 2019
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      Kumagai, P. S., Martins, C. S., Sales, E. M., Itri, R., & Araújo, A. P. U. de. (2019). Physiological septin-septin interactions prevents amyloid filaments formation. European Biophysics Journal. Heidelberg: Springer. doi:10.1007/s00249-019-01373-4
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      Kumagai PS, Martins CS, Sales EM, Itri R, Araújo APU de. Physiological septin-septin interactions prevents amyloid filaments formation [Internet]. European Biophysics Journal. 2019 ; 48 S149.[citado 2024 jul. 03 ] Available from: https://doi.org/10.1007/s00249-019-01373-4
    • Vancouver

      Kumagai PS, Martins CS, Sales EM, Itri R, Araújo APU de. Physiological septin-septin interactions prevents amyloid filaments formation [Internet]. European Biophysics Journal. 2019 ; 48 S149.[citado 2024 jul. 03 ] Available from: https://doi.org/10.1007/s00249-019-01373-4
  • Source: International Journal of Biological Macromolecules. Unidades: IF, IFSC, EESC

    Subjects: PROTEÍNAS, BIOFÍSICA, CRISTALOGRAFIA

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    • ABNT

      KUMAGAI, Patricia Suemy et al. Correct partner makes the difference: septin G-interface plays a critical role in amyloid formation. International Journal of Biological Macromolecules, v. 133, p. 428-435, 2019Tradução . . Disponível em: https://doi.org/10.1016/j.ijbiomac.2019.04.105. Acesso em: 03 jul. 2024.
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      Kumagai, P. S., Martins, C. S., Sales, E. M., Rosa, H. V. D., Mendonça, D. C., Damalio, J. C. P., et al. (2019). Correct partner makes the difference: septin G-interface plays a critical role in amyloid formation. International Journal of Biological Macromolecules, 133, 428-435. doi:10.1016/j.ijbiomac.2019.04.105
    • NLM

      Kumagai PS, Martins CS, Sales EM, Rosa HVD, Mendonça DC, Damalio JCP, Spinozzi F, Itri R, Araújo APU de. Correct partner makes the difference: septin G-interface plays a critical role in amyloid formation [Internet]. International Journal of Biological Macromolecules. 2019 ; 133 428-435.[citado 2024 jul. 03 ] Available from: https://doi.org/10.1016/j.ijbiomac.2019.04.105
    • Vancouver

      Kumagai PS, Martins CS, Sales EM, Rosa HVD, Mendonça DC, Damalio JCP, Spinozzi F, Itri R, Araújo APU de. Correct partner makes the difference: septin G-interface plays a critical role in amyloid formation [Internet]. International Journal of Biological Macromolecules. 2019 ; 133 428-435.[citado 2024 jul. 03 ] Available from: https://doi.org/10.1016/j.ijbiomac.2019.04.105
  • Source: Scientific Reports. Unidades: IF, FORP

    Subjects: DOENÇAS NEURODEGENERATIVAS, PROTEÍNAS, BIOFÍSICA

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      GONZÁLEZ-LIZÁRRAGA, Florencia et al. Repurposing doxycycline for synucleinopathies: remodelling of α-synuclein oligomers towards non-toxic parallel beta-sheet structured species. Scientific Reports, v. 7, n. 41755, p. 1-13, 2017Tradução . . Disponível em: https://doi.org/10.1038/srep41755. Acesso em: 03 jul. 2024.
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      González-Lizárraga, F., Socías, S. B., Ávila, C. L., Torres-Bugeau, C. M., Barbosa, L. R. S., Binolfi, A., et al. (2017). Repurposing doxycycline for synucleinopathies: remodelling of α-synuclein oligomers towards non-toxic parallel beta-sheet structured species. Scientific Reports, 7( 41755), 1-13. doi:10.1038/srep41755
    • NLM

      González-Lizárraga F, Socías SB, Ávila CL, Torres-Bugeau CM, Barbosa LRS, Binolfi A, Sepúlveda-Díaz JE, Del-Bel E, Fernandez CO, Papy-Garcia D, Itri R, Raisman-Vozari Rita, Chehín RN. Repurposing doxycycline for synucleinopathies: remodelling of α-synuclein oligomers towards non-toxic parallel beta-sheet structured species [Internet]. Scientific Reports. 2017 ; 7( 41755): 1-13.[citado 2024 jul. 03 ] Available from: https://doi.org/10.1038/srep41755
    • Vancouver

      González-Lizárraga F, Socías SB, Ávila CL, Torres-Bugeau CM, Barbosa LRS, Binolfi A, Sepúlveda-Díaz JE, Del-Bel E, Fernandez CO, Papy-Garcia D, Itri R, Raisman-Vozari Rita, Chehín RN. Repurposing doxycycline for synucleinopathies: remodelling of α-synuclein oligomers towards non-toxic parallel beta-sheet structured species [Internet]. Scientific Reports. 2017 ; 7( 41755): 1-13.[citado 2024 jul. 03 ] Available from: https://doi.org/10.1038/srep41755
  • Source: European Biophysics Journal. Conference titles: European Biophysics Congress - EBSA. Unidades: IFSC, IF

    Subjects: PROTEÍNAS, TERMODINÂMICA, CRISTALOGRAFIA

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      ORTORE, M. G. et al. Septin 3 aggregation in solution: thermodynamic and structural characterization. European Biophysics Journal. Heidelberg: Springer. Disponível em: https://doi.org/10.1007/s00249-015-1045-6. Acesso em: 03 jul. 2024. , 2015
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      Ortore, M. G., Macedo, J. N. A., Araújo, A. P. U. de, Ferrero, C., Mariani, P., Spinozzi, F., & Itri, R. (2015). Septin 3 aggregation in solution: thermodynamic and structural characterization. European Biophysics Journal. Heidelberg: Springer. doi:10.1007/s00249-015-1045-6
    • NLM

      Ortore MG, Macedo JNA, Araújo APU de, Ferrero C, Mariani P, Spinozzi F, Itri R. Septin 3 aggregation in solution: thermodynamic and structural characterization [Internet]. European Biophysics Journal. 2015 ; 44 S208.[citado 2024 jul. 03 ] Available from: https://doi.org/10.1007/s00249-015-1045-6
    • Vancouver

      Ortore MG, Macedo JNA, Araújo APU de, Ferrero C, Mariani P, Spinozzi F, Itri R. Septin 3 aggregation in solution: thermodynamic and structural characterization [Internet]. European Biophysics Journal. 2015 ; 44 S208.[citado 2024 jul. 03 ] Available from: https://doi.org/10.1007/s00249-015-1045-6
  • Source: JOURNAL OF BIOLOGICAL CHEMISTRY. Unidade: IF

    Subjects: RADIOGRAFIA, PROTEÍNAS

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      AVILA, Cesar L. et al. Structural characterization of heparin-induced glyceraldehyde-3-phosphate dehydrogenase protofibrils preventing 'alfa'-synuclein oligomeric species toxicity. JOURNAL OF BIOLOGICAL CHEMISTRY, v. 289, n. 20, p. 13838-13850, 2014Tradução . . Disponível em: https://doi.org/10.1074/jbc.M113.544288. Acesso em: 03 jul. 2024.
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      Avila, C. L., Torres-Bugeau, C. M., Chehin, R. N., Ouidja, M. O., Socias, S. B., Raisman-Vozari, R., et al. (2014). Structural characterization of heparin-induced glyceraldehyde-3-phosphate dehydrogenase protofibrils preventing 'alfa'-synuclein oligomeric species toxicity. JOURNAL OF BIOLOGICAL CHEMISTRY, 289( 20), 13838-13850. doi:10.1074/jbc.M113.544288
    • NLM

      Avila CL, Torres-Bugeau CM, Chehin RN, Ouidja MO, Socias SB, Raisman-Vozari R, Papy-Garcia D, Soledad Celej M, Sales EM, Itri R, Barbosa LRS. Structural characterization of heparin-induced glyceraldehyde-3-phosphate dehydrogenase protofibrils preventing 'alfa'-synuclein oligomeric species toxicity [Internet]. JOURNAL OF BIOLOGICAL CHEMISTRY. 2014 ; 289( 20): 13838-13850.[citado 2024 jul. 03 ] Available from: https://doi.org/10.1074/jbc.M113.544288
    • Vancouver

      Avila CL, Torres-Bugeau CM, Chehin RN, Ouidja MO, Socias SB, Raisman-Vozari R, Papy-Garcia D, Soledad Celej M, Sales EM, Itri R, Barbosa LRS. Structural characterization of heparin-induced glyceraldehyde-3-phosphate dehydrogenase protofibrils preventing 'alfa'-synuclein oligomeric species toxicity [Internet]. JOURNAL OF BIOLOGICAL CHEMISTRY. 2014 ; 289( 20): 13838-13850.[citado 2024 jul. 03 ] Available from: https://doi.org/10.1074/jbc.M113.544288
  • Source: Proteins in Solution and at Interfaces: Methods and Applications in Biotechnology and Materials Science. Unidade: IF

    Subjects: BIOTECNOLOGIA, ALBUMINAS, PROTEÍNAS, ESPALHAMENTO DE RAIOS X A BAIXOS ÂNGULOS

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      BARBOSA, Leandro Ramos Souza et al. Small-Angle X-Ray Scattering Applied to Proteins in Solution. Proteins in Solution and at Interfaces: Methods and Applications in Biotechnology and Materials Science. Tradução . Hoboken, NJ: John Wiley & Sons, 2013. . Disponível em: http://onlinelibrary.wiley.com/doi/10.1002/9781118523063.ch3/summary. Acesso em: 03 jul. 2024.
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      Barbosa, L. R. S., Spinozzi, F., Mariani, P., & Itri, R. (2013). Small-Angle X-Ray Scattering Applied to Proteins in Solution. In Proteins in Solution and at Interfaces: Methods and Applications in Biotechnology and Materials Science. Hoboken, NJ: John Wiley & Sons. Recuperado de http://onlinelibrary.wiley.com/doi/10.1002/9781118523063.ch3/summary
    • NLM

      Barbosa LRS, Spinozzi F, Mariani P, Itri R. Small-Angle X-Ray Scattering Applied to Proteins in Solution [Internet]. In: Proteins in Solution and at Interfaces: Methods and Applications in Biotechnology and Materials Science. Hoboken, NJ: John Wiley & Sons; 2013. [citado 2024 jul. 03 ] Available from: http://onlinelibrary.wiley.com/doi/10.1002/9781118523063.ch3/summary
    • Vancouver

      Barbosa LRS, Spinozzi F, Mariani P, Itri R. Small-Angle X-Ray Scattering Applied to Proteins in Solution [Internet]. In: Proteins in Solution and at Interfaces: Methods and Applications in Biotechnology and Materials Science. Hoboken, NJ: John Wiley & Sons; 2013. [citado 2024 jul. 03 ] Available from: http://onlinelibrary.wiley.com/doi/10.1002/9781118523063.ch3/summary
  • Source: Biophysical Journal. Conference titles: Annual Meeting of the Biophysical Society. Unidades: IF, IFSC

    Subjects: PROTEÍNAS, BIOFÍSICA

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    • ABNT

      ITRI, Rosangela et al. Structural studies of Septin2G amyloid fibrils. Biophysical Journal. Saint Louis: Cell Press. Disponível em: https://doi.org/10.1016/j.bpj.2011.11.2087. Acesso em: 03 jul. 2024. , 2012
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      Itri, R., Sales, E. M., Damascio, J., Barbosa, L. R. S., Spinozzi, F., Mariani, P., & Araújo, A. P. U. de. (2012). Structural studies of Septin2G amyloid fibrils. Biophysical Journal. Saint Louis: Cell Press. doi:10.1016/j.bpj.2011.11.2087
    • NLM

      Itri R, Sales EM, Damascio J, Barbosa LRS, Spinozzi F, Mariani P, Araújo APU de. Structural studies of Septin2G amyloid fibrils [Internet]. Biophysical Journal. 2012 ; 102( Ja 2012): 381a-382a.[citado 2024 jul. 03 ] Available from: https://doi.org/10.1016/j.bpj.2011.11.2087
    • Vancouver

      Itri R, Sales EM, Damascio J, Barbosa LRS, Spinozzi F, Mariani P, Araújo APU de. Structural studies of Septin2G amyloid fibrils [Internet]. Biophysical Journal. 2012 ; 102( Ja 2012): 381a-382a.[citado 2024 jul. 03 ] Available from: https://doi.org/10.1016/j.bpj.2011.11.2087
  • Source: FEBS Journal. Conference titles: FEBS Congress. Unidades: IF, IFSC

    Subjects: PROTEÍNAS, NANOTECNOLOGIA, BIOTECNOLOGIA, ORGANELAS CELULARES, BIOFÍSICA, FUNGOS

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      CAMARGO, A. I. et al. AFM and SAXS structural analises of two centrins from fungi Blastocladiella emersoni. FEBS Journal. Malden: Wiley-Blackwell. Disponível em: https://doi.org/10.1111/j.1742-4658.2009.07049.x. Acesso em: 03 jul. 2024. , 2009
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      Camargo, A. I., Camargo, P. C., Barbosa, L., Itri, R., & Beltramini, L. M. (2009). AFM and SAXS structural analises of two centrins from fungi Blastocladiella emersoni. FEBS Journal. Malden: Wiley-Blackwell. doi:10.1111/j.1742-4658.2009.07049.x
    • NLM

      Camargo AI, Camargo PC, Barbosa L, Itri R, Beltramini LM. AFM and SAXS structural analises of two centrins from fungi Blastocladiella emersoni [Internet]. FEBS Journal. 2009 ; 276 133.[citado 2024 jul. 03 ] Available from: https://doi.org/10.1111/j.1742-4658.2009.07049.x
    • Vancouver

      Camargo AI, Camargo PC, Barbosa L, Itri R, Beltramini LM. AFM and SAXS structural analises of two centrins from fungi Blastocladiella emersoni [Internet]. FEBS Journal. 2009 ; 276 133.[citado 2024 jul. 03 ] Available from: https://doi.org/10.1111/j.1742-4658.2009.07049.x
  • Source: Journal of Nanoscience and Nanotechnology. Unidade: IF

    Subjects: DIFRAÇÃO POR RAIOS X, FÍSICO-QUÍMICA, PROTEÍNAS, ALBUMINAS

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      CAETANO, Wilker e AMARAL, Carmen Lucia C e ITRI, Rosangela. The influence of urea on the structure of proteins in reversed micelles. Journal of Nanoscience and Nanotechnology, v. 6, n. 8, p. 2416-2424, 2006Tradução . . Disponível em: http://docserver.ingentaconnect.com/deliver/connect/asp/15334880/v6n8/s21.pdf?expires=1160007108&id=32148875&titleid=4286&accname=Universidade+de+S%C3%A3o+Paulo+-+Instituto+Oceanogr%C3%A1fico+-+IO&checksum=FA19E0AFA42143B6C2F4E351465CEDFC. Acesso em: 03 jul. 2024.
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      Caetano, W., Amaral, C. L. C., & Itri, R. (2006). The influence of urea on the structure of proteins in reversed micelles. Journal of Nanoscience and Nanotechnology, 6( 8), 2416-2424. Recuperado de http://docserver.ingentaconnect.com/deliver/connect/asp/15334880/v6n8/s21.pdf?expires=1160007108&id=32148875&titleid=4286&accname=Universidade+de+S%C3%A3o+Paulo+-+Instituto+Oceanogr%C3%A1fico+-+IO&checksum=FA19E0AFA42143B6C2F4E351465CEDFC
    • NLM

      Caetano W, Amaral CLC, Itri R. The influence of urea on the structure of proteins in reversed micelles [Internet]. Journal of Nanoscience and Nanotechnology. 2006 ; 6( 8): 2416-2424.[citado 2024 jul. 03 ] Available from: http://docserver.ingentaconnect.com/deliver/connect/asp/15334880/v6n8/s21.pdf?expires=1160007108&id=32148875&titleid=4286&accname=Universidade+de+S%C3%A3o+Paulo+-+Instituto+Oceanogr%C3%A1fico+-+IO&checksum=FA19E0AFA42143B6C2F4E351465CEDFC
    • Vancouver

      Caetano W, Amaral CLC, Itri R. The influence of urea on the structure of proteins in reversed micelles [Internet]. Journal of Nanoscience and Nanotechnology. 2006 ; 6( 8): 2416-2424.[citado 2024 jul. 03 ] Available from: http://docserver.ingentaconnect.com/deliver/connect/asp/15334880/v6n8/s21.pdf?expires=1160007108&id=32148875&titleid=4286&accname=Universidade+de+S%C3%A3o+Paulo+-+Instituto+Oceanogr%C3%A1fico+-+IO&checksum=FA19E0AFA42143B6C2F4E351465CEDFC
  • Source: Brazilian Journal of Physics. Unidades: IF, IQ

    Subjects: FÍSICO-QUÍMICA, DIFRAÇÃO POR RAIOS X, SURFACTANTES, PROTEÍNAS

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      ITRI, Rosangela et al. Effect of urea on bovine serum albumin in aqueous and reverse micelle environmentes investigated by small angle X-ray scattering, fluorescence and circular dichroism. Brazilian Journal of Physics, 2004Tradução . . Disponível em: https://doi.org/10.1590/s0103-97332004000100009. Acesso em: 03 jul. 2024.
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      Itri, R., Caetano, W., Barbosa, L. R. S., & Baptista, M. da S. (2004). Effect of urea on bovine serum albumin in aqueous and reverse micelle environmentes investigated by small angle X-ray scattering, fluorescence and circular dichroism. Brazilian Journal of Physics. doi:10.1590/s0103-97332004000100009
    • NLM

      Itri R, Caetano W, Barbosa LRS, Baptista M da S. Effect of urea on bovine serum albumin in aqueous and reverse micelle environmentes investigated by small angle X-ray scattering, fluorescence and circular dichroism [Internet]. Brazilian Journal of Physics. 2004 ;[citado 2024 jul. 03 ] Available from: https://doi.org/10.1590/s0103-97332004000100009
    • Vancouver

      Itri R, Caetano W, Barbosa LRS, Baptista M da S. Effect of urea on bovine serum albumin in aqueous and reverse micelle environmentes investigated by small angle X-ray scattering, fluorescence and circular dichroism [Internet]. Brazilian Journal of Physics. 2004 ;[citado 2024 jul. 03 ] Available from: https://doi.org/10.1590/s0103-97332004000100009
  • Source: Livro de resumos. Conference titles: Reunião Anual da Sociedade Brasileira de Química. Unidades: IF, IQ

    Subjects: FÍSICO-QUÍMICA, PROTEÍNAS

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      SILVA, Marcelo Alves da e ITRI, Rosangela e ARÊAS, Elizabeth Pinheiro Gomes. Investigação de redes tridimensionais transientes em sistemas lisozima/água/tetrametiluréia. 2001, Anais.. São Paulo: SBQ, 2001. . Acesso em: 03 jul. 2024.
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      Silva, M. A. da, Itri, R., & Arêas, E. P. G. (2001). Investigação de redes tridimensionais transientes em sistemas lisozima/água/tetrametiluréia. In Livro de resumos. São Paulo: SBQ.
    • NLM

      Silva MA da, Itri R, Arêas EPG. Investigação de redes tridimensionais transientes em sistemas lisozima/água/tetrametiluréia. Livro de resumos. 2001 ;[citado 2024 jul. 03 ]
    • Vancouver

      Silva MA da, Itri R, Arêas EPG. Investigação de redes tridimensionais transientes em sistemas lisozima/água/tetrametiluréia. Livro de resumos. 2001 ;[citado 2024 jul. 03 ]

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