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Filtros : "PROTEÍNAS" "IF-FAP" Removidos: "FOB-BAM" "ENGENHARIAS IV" "Indexado na Curr-Cont" "Biologia Celular e do Desenvolvimento" "FÍSICA DOS MATERIAIS E MECÂNICA" "FCFRP-604" "FERRAZ, JOSE BENTO STERMAN" "Pró-Reitoria de Pesquisa/USP" "HRAC" Limpar

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  • Artigo de periodico

    Effect of setting data collection parameters on the reliability of a circular dichroism spectrum (2021)

    Sousa Victor Klein de ; Pedro, Jéssica Aparecida Ferreira ; Kumagai, Patricia Suemy ; Lopes, José Luiz de Souza

    Source: European Biophysics Journal. Unidades: IF, IFSC

    Subjects: BIOFÍSICA, ESPECTROSCOPIA DA LUZ, MOLÉCULA, PROTEÍNAS, GLOBULINAS, BIOINFORMÁTICA, AMOSTRAGEM EXPERIMENTAL

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      SOUSA VICTOR KLEIN DE, et al. Effect of setting data collection parameters on the reliability of a circular dichroism spectrum. European Biophysics Journal, v. 50, n. 5, p. 687-697, 2021Tradução . . Disponível em: https://doi.org/10.1007/s00249-021-01499-4. Acesso em: 13 jul. 2024.

    • APA

      Sousa Victor Klein de,, Pedro, J. A. F., Kumagai, P. S., & Lopes, J. L. de S. (2021). Effect of setting data collection parameters on the reliability of a circular dichroism spectrum. European Biophysics Journal, 50( 5), 687-697. doi:10.1007/s00249-021-01499-4

    • NLM

      Sousa Victor Klein de, Pedro JAF, Kumagai PS, Lopes JL de S. Effect of setting data collection parameters on the reliability of a circular dichroism spectrum [Internet]. European Biophysics Journal. 2021 ; 50( 5): 687-697.[citado 2024 jul. 13 ] Available from: https://doi.org/10.1007/s00249-021-01499-4

    • Vancouver

      Sousa Victor Klein de, Pedro JAF, Kumagai PS, Lopes JL de S. Effect of setting data collection parameters on the reliability of a circular dichroism spectrum [Internet]. European Biophysics Journal. 2021 ; 50( 5): 687-697.[citado 2024 jul. 13 ] Available from: https://doi.org/10.1007/s00249-021-01499-4

  • Trabalho de evento-resumo periodico

    Physiological septin-septin interactions prevents amyloid filaments formation (2019)

    Kumagai, Patricia Suemy; Martins, Carla Silva; Sales, Elisa Morandé; Itri, Rosângela; Araújo, Ana Paula Ulian de

    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: 13 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

    • NLM

      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. 13 ] 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. 13 ] Available from: https://doi.org/10.1007/s00249-019-01373-4

  • Artigo de periodico

    Correct partner makes the difference: septin G-interface plays a critical role in amyloid formation (2019)

    Kumagai, Patricia Suemy; Martins, Carla Silva; Sales, Elisa Morandé; Rosa, Higor Vinicius Dias; Mendonça, Deborah Cezar; Damalio, Júlio Cesar P.; Spinozzi, Francesco; Itri, Rosângela; Araújo, Ana Paula Ulian de

    Source: International Journal of Biological Macromolecules. Unidades: IF, IFSC, EESC

    Subjects: PROTEÍNAS, BIOFÍSICA, CRISTALOGRAFIA

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      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: 13 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. 13 ] 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. 13 ] Available from: https://doi.org/10.1016/j.ijbiomac.2019.04.105

  • Trabalho de evento-resumo

    Anaerobaculum hydrogeniformans esterase (ahest): a new thermostable esterase for biotechnological applications (2017)

    Gutierrez, R.; Martins, J. M.; Kumagai, P. S.; Castro, A. M.; Lopes, José Luiz de Souza; Araújo, Ana Paula Ulian de

    Source: Scientific Programme. Conference titles: Congress of European Microbiologists. Unidades: IF, IFSC

    Subjects: PROTEÍNAS, MEMBRANAS CELULARES, CRISTALOGRAFIA

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    • ABNT

      GUTIERREZ, R. et al. Anaerobaculum hydrogeniformans esterase (ahest): a new thermostable esterase for biotechnological applications. 2017, Anais.. Wrexham: Federation of European Microbiological Societies - FEMS, 2017. Disponível em: http://www.fems-microbiology2017.kenes.com/scientific-information/interactive-programme#.WdeiqFtSzcd. Acesso em: 13 jul. 2024.

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      Gutierrez, R., Martins, J. M., Kumagai, P. S., Castro, A. M., Lopes, J. L. de S., & Araújo, A. P. U. de. (2017). Anaerobaculum hydrogeniformans esterase (ahest): a new thermostable esterase for biotechnological applications. In Scientific Programme. Wrexham: Federation of European Microbiological Societies - FEMS. Recuperado de http://www.fems-microbiology2017.kenes.com/scientific-information/interactive-programme#.WdeiqFtSzcd

    • NLM

      Gutierrez R, Martins JM, Kumagai PS, Castro AM, Lopes JL de S, Araújo APU de. Anaerobaculum hydrogeniformans esterase (ahest): a new thermostable esterase for biotechnological applications [Internet]. Scientific Programme. 2017 ;[citado 2024 jul. 13 ] Available from: http://www.fems-microbiology2017.kenes.com/scientific-information/interactive-programme#.WdeiqFtSzcd

    • Vancouver

      Gutierrez R, Martins JM, Kumagai PS, Castro AM, Lopes JL de S, Araújo APU de. Anaerobaculum hydrogeniformans esterase (ahest): a new thermostable esterase for biotechnological applications [Internet]. Scientific Programme. 2017 ;[citado 2024 jul. 13 ] Available from: http://www.fems-microbiology2017.kenes.com/scientific-information/interactive-programme#.WdeiqFtSzcd

  • Artigo de periodico

    Advantages of synchrotron radiation circular dichroism spectroscopy to study intrinsically disordered proteins (2017)

    Kumagai, Patricia S.; De Marco, Ricardo; Lopes, José luiz de Souza

    Source: European Biophysics Journal. Unidades: IFSC, IF

    Subjects: PROTEÍNAS, CRISTALOGRAFIA, MEMBRANAS CELULARES

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      KUMAGAI, Patricia S. e DE MARCO, Ricardo e LOPES, José luiz de Souza. Advantages of synchrotron radiation circular dichroism spectroscopy to study intrinsically disordered proteins. European Biophysics Journal, v. 46, n. 7, p. 599-606, 2017Tradução . . Disponível em: https://doi.org/10.1007/s00249-017-1202-1. Acesso em: 13 jul. 2024.

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      Kumagai, P. S., De Marco, R., & Lopes, J. luiz de S. (2017). Advantages of synchrotron radiation circular dichroism spectroscopy to study intrinsically disordered proteins. European Biophysics Journal, 46( 7), 599-606. doi:10.1007/s00249-017-1202-1

    • NLM

      Kumagai PS, De Marco R, Lopes J luiz de S. Advantages of synchrotron radiation circular dichroism spectroscopy to study intrinsically disordered proteins [Internet]. European Biophysics Journal. 2017 ; 46( 7): 599-606.[citado 2024 jul. 13 ] Available from: https://doi.org/10.1007/s00249-017-1202-1

    • Vancouver

      Kumagai PS, De Marco R, Lopes J luiz de S. Advantages of synchrotron radiation circular dichroism spectroscopy to study intrinsically disordered proteins [Internet]. European Biophysics Journal. 2017 ; 46( 7): 599-606.[citado 2024 jul. 13 ] Available from: https://doi.org/10.1007/s00249-017-1202-1

  • Trabalho de evento-resumo

    Challenges in studying intrinsically disordered proteins (2017)

    Lopes, José Luiz de Souza; Kumagai, P. S.; De Marco, Ricardo; Araújo, Ana Paula Ulian de; Wallace, B. A.

    Source: Scientific Program. Conference titles: Congresso da Sociedade Brasileira de Biofísica - SBBf. Unidades: IF, IFSC

    Subjects: PROTEÍNAS, ESPECTROSCOPIA, ESTRUTURA MOLECULAR (QUÍMICA TEÓRICA)

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      LOPES, José Luiz de Souza et al. Challenges in studying intrinsically disordered proteins. 2017, Anais.. Rio de Janeiro: Sociedade Brasileira de Biofísica - SBBf, 2017. Disponível em: http://www.sbbf.org.br/xliisbbf2017/wp-content/uploads/2017/05/Scientific-Program-SBBf2017.pdf. Acesso em: 13 jul. 2024.

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      Lopes, J. L. de S., Kumagai, P. S., De Marco, R., Araújo, A. P. U. de, & Wallace, B. A. (2017). Challenges in studying intrinsically disordered proteins. In Scientific Program. Rio de Janeiro: Sociedade Brasileira de Biofísica - SBBf. Recuperado de http://www.sbbf.org.br/xliisbbf2017/wp-content/uploads/2017/05/Scientific-Program-SBBf2017.pdf

    • NLM

      Lopes JL de S, Kumagai PS, De Marco R, Araújo APU de, Wallace BA. Challenges in studying intrinsically disordered proteins [Internet]. Scientific Program. 2017 ;[citado 2024 jul. 13 ] Available from: http://www.sbbf.org.br/xliisbbf2017/wp-content/uploads/2017/05/Scientific-Program-SBBf2017.pdf

    • Vancouver

      Lopes JL de S, Kumagai PS, De Marco R, Araújo APU de, Wallace BA. Challenges in studying intrinsically disordered proteins [Internet]. Scientific Program. 2017 ;[citado 2024 jul. 13 ] Available from: http://www.sbbf.org.br/xliisbbf2017/wp-content/uploads/2017/05/Scientific-Program-SBBf2017.pdf

  • Artigo de periodico

    Repurposing doxycycline for synucleinopathies: remodelling of α-synuclein oligomers towards non-toxic parallel beta-sheet structured species (2017)

    González-Lizárraga, Florencia; Socías, Sergio B; Ávila, César L; Torres-Bugeau, Clarisa M; Barbosa, Leandro Ramos Souza; Binolfi, Andres; Sepúlveda-Díaz, Julia E; Del-Bel, Elaine; Fernandez, Claudio O; Papy-Garcia, Dulce; Itri, Rosangela; Raisman-Vozari Rita; Chehín, Rosana N

    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: 13 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. 13 ] 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. 13 ] Available from: https://doi.org/10.1038/srep41755

  • Artigo de periodico

    Interaction of an esophageal MEG protein from schistosomes with a human S100 protein involved in inflammatory response (2017)

    Orcia, Débora; Zeraik, Ana Eliza; Lopes, José Luiz de Souza; Macêdo, Joci Neuby Alves; Santos, Clarissa Romano dos; Oliveira, Kátia Cristina de; Anderson, Letícia; Wallace, B. A; Verjovski-Almeida, Sergio ; Araújo, Ana Paula Ulian de; De Marco, Ricardo

    Source: Biochimica et Biophysica Acta: General Subjects. Unidades: IF, IQ, IFSC

    Subjects: RADIAÇÃO SINCROTRON, PROTEÍNAS

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      ORCIA, Débora et al. Interaction of an esophageal MEG protein from schistosomes with a human S100 protein involved in inflammatory response. Biochimica et Biophysica Acta: General Subjects, v. 1861, n. Ja 2017, p. 3490-3497, 2017Tradução . . Disponível em: https://doi.org/10.1016/j.bbagen.2016.09.015. Acesso em: 13 jul. 2024.

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      Orcia, D., Zeraik, A. E., Lopes, J. L. de S., Macêdo, J. N. A., Santos, C. R. dos, Oliveira, K. C. de, et al. (2017). Interaction of an esophageal MEG protein from schistosomes with a human S100 protein involved in inflammatory response. Biochimica et Biophysica Acta: General Subjects, 1861( Ja 2017), 3490-3497. doi:10.1016/j.bbagen.2016.09.015

    • NLM

      Orcia D, Zeraik AE, Lopes JL de S, Macêdo JNA, Santos CR dos, Oliveira KC de, Anderson L, Wallace BA, Verjovski-Almeida S, Araújo APU de, De Marco R. Interaction of an esophageal MEG protein from schistosomes with a human S100 protein involved in inflammatory response [Internet]. Biochimica et Biophysica Acta: General Subjects. 2017 ; 1861( Ja 2017): 3490-3497.[citado 2024 jul. 13 ] Available from: https://doi.org/10.1016/j.bbagen.2016.09.015

    • Vancouver

      Orcia D, Zeraik AE, Lopes JL de S, Macêdo JNA, Santos CR dos, Oliveira KC de, Anderson L, Wallace BA, Verjovski-Almeida S, Araújo APU de, De Marco R. Interaction of an esophageal MEG protein from schistosomes with a human S100 protein involved in inflammatory response [Internet]. Biochimica et Biophysica Acta: General Subjects. 2017 ; 1861( Ja 2017): 3490-3497.[citado 2024 jul. 13 ] Available from: https://doi.org/10.1016/j.bbagen.2016.09.015

  • Artigo de periodico

    Going deep into protein secondary structure with synchrotron radiation circular dichroism spectroscopy (2017)

    Kumagai, Patricia S.; Araújo, Ana Paula Ulian de; Lopes, José Luiz de Souza

    Source: Biophysical Reviews. Unidades: IFSC, IF

    Subjects: ESPECTROSCOPIA, PROTEÍNAS

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      KUMAGAI, Patricia S. e ARAÚJO, Ana Paula Ulian de e LOPES, José Luiz de Souza. Going deep into protein secondary structure with synchrotron radiation circular dichroism spectroscopy. Biophysical Reviews, v. 9, n. 5, p. 517-527, 2017Tradução . . Disponível em: https://doi.org/10.1007/s12551-017-0314-2. Acesso em: 13 jul. 2024.

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      Kumagai, P. S., Araújo, A. P. U. de, & Lopes, J. L. de S. (2017). Going deep into protein secondary structure with synchrotron radiation circular dichroism spectroscopy. Biophysical Reviews, 9( 5), 517-527. doi:10.1007/s12551-017-0314-2

    • NLM

      Kumagai PS, Araújo APU de, Lopes JL de S. Going deep into protein secondary structure with synchrotron radiation circular dichroism spectroscopy [Internet]. Biophysical Reviews. 2017 ; 9( 5): 517-527.[citado 2024 jul. 13 ] Available from: https://doi.org/10.1007/s12551-017-0314-2

    • Vancouver

      Kumagai PS, Araújo APU de, Lopes JL de S. Going deep into protein secondary structure with synchrotron radiation circular dichroism spectroscopy [Internet]. Biophysical Reviews. 2017 ; 9( 5): 517-527.[citado 2024 jul. 13 ] Available from: https://doi.org/10.1007/s12551-017-0314-2

  • Artigo de periodico

    Frog foam nest protein diversity and synthesis (2016)

    Hissa, Denise Cavalcante; Bezerra, Walderly Melgaço; Freitas, Cléverson Diniz Teixeira de; Ramos, Márcio Viana; Lopes, José Luiz de Souza; Beltramini, Leila Maria; Roberto, Igor Joventino; Cascon, Paulo; Melo, Vânia Maria Maciel

    Source: Journal of Experimental Zoology A. Unidades: IF, IFSC

    Subjects: ANFÍBIOS, PROTEÍNAS, NINHOS

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      HISSA, Denise Cavalcante et al. Frog foam nest protein diversity and synthesis. Journal of Experimental Zoology A, v. 325, n. 7, p. 425-433, 2016Tradução . . Disponível em: https://doi.org/10.1002/jez.2027. Acesso em: 13 jul. 2024.

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      Hissa, D. C., Bezerra, W. M., Freitas, C. D. T. de, Ramos, M. V., Lopes, J. L. de S., Beltramini, L. M., et al. (2016). Frog foam nest protein diversity and synthesis. Journal of Experimental Zoology A, 325( 7), 425-433. doi:10.1002/jez.2027

    • NLM

      Hissa DC, Bezerra WM, Freitas CDT de, Ramos MV, Lopes JL de S, Beltramini LM, Roberto IJ, Cascon P, Melo VMM. Frog foam nest protein diversity and synthesis [Internet]. Journal of Experimental Zoology A. 2016 ; 325( 7): 425-433.[citado 2024 jul. 13 ] Available from: https://doi.org/10.1002/jez.2027

    • Vancouver

      Hissa DC, Bezerra WM, Freitas CDT de, Ramos MV, Lopes JL de S, Beltramini LM, Roberto IJ, Cascon P, Melo VMM. Frog foam nest protein diversity and synthesis [Internet]. Journal of Experimental Zoology A. 2016 ; 325( 7): 425-433.[citado 2024 jul. 13 ] Available from: https://doi.org/10.1002/jez.2027

  • Trabalho de evento-resumo periodico

    Septin 3 aggregation in solution: thermodynamic and structural characterization (2015)

    Ortore, M. G.; Macedo, J. N. A.; Araújo, Ana Paula Ulian de; Ferrero, C.; Mariani, P.; Spinozzi, F.; Itri, Rosângela

    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: 13 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. 13 ] 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. 13 ] Available from: https://doi.org/10.1007/s00249-015-1045-6

  • Artigo de periodico

    Structural characterization of heparin-induced glyceraldehyde-3-phosphate dehydrogenase protofibrils preventing 'alfa'-synuclein oligomeric species toxicity (2014)

    Avila, Cesar L.; Torres-Bugeau, Clarisa M.; Chehin, Rosana N.; Ouidja, Mohand O.; Socias, Sergio B.; Raisman-Vozari, Rita; Papy-Garcia, Dulce; Soledad Celej, M.; Sales, Elisa Morandé; Itri, Rosangela ; Barbosa, Leandro Ramos Souza

    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: 13 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. 13 ] 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. 13 ] Available from: https://doi.org/10.1074/jbc.M113.544288

  • Parte de monografia/livro

    Small-Angle X-Ray Scattering Applied to Proteins in Solution (2013)

    Barbosa, Leandro Ramos Souza; Spinozzi, Francesco; Mariani, Paolo; Itri, Rosangela

    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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    • ABNT

      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: 13 jul. 2024.

    • APA

      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. 13 ] 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. 13 ] Available from: http://onlinelibrary.wiley.com/doi/10.1002/9781118523063.ch3/summary

  • Trabalho de evento-resumo periodico

    Structural studies of Septin2G amyloid fibrils (2012)

    Itri, Rosangela; Sales, Elisa Morandé; Damascio, Júlio; Barbosa, Leandro Ramos Souza; Spinozzi, Francesco; Mariani, Paolo; Araújo, Ana Paula Ulian de

    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: 13 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. 13 ] 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. 13 ] Available from: https://doi.org/10.1016/j.bpj.2011.11.2087

  • Trabalho de evento-resumo periodico

    AFM and SAXS structural analises of two centrins from fungi Blastocladiella emersoni (2009)

    Camargo, A. I.; Camargo, P. C.; Barbosa, L.; Itri, Rosangela; Beltramini, Leila Maria

    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: 13 jul. 2024. , 2009

    • APA

      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. 13 ] 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. 13 ] Available from: https://doi.org/10.1111/j.1742-4658.2009.07049.x

  • Artigo de periodico

    Ordered mesoporous silica SBA-15: a new effective adjuvant to induce antibody response (2006)

    Mercuri, Lucildes P; Carvalho, Luciana V; Lima, Flavia A; Quayle, Carolina; Fantini, Márcia Carvalho de Abreu ; Tanaka, Gabriela S; Cabrera, Wafa H; Furtado, Maria F D; Tambourgi, Denise V; Matos, Jivaldo do Rosário ; Jaroniec, Mietek; Sant’Anna, Osvaldo A (Microbiology Laboratory, Center for Applied Toxinology, Butantan Institute, São Paulo, Brazil)

    Source: Small. Unidades: IF, IQ

    Subjects: PROTEÍNAS, ANTICORPOS

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      MERCURI, Lucildes P et al. Ordered mesoporous silica SBA-15: a new effective adjuvant to induce antibody response. Small, v. 2, n. 2, p. 254-256, 2006Tradução . . Disponível em: http://www3.interscience.wiley.com/cgi-bin/fulltext/112213664/PDFSTART. Acesso em: 13 jul. 2024.

    • APA

      Mercuri, L. P., Carvalho, L. V., Lima, F. A., Quayle, C., Fantini, M. C. de A., Tanaka, G. S., et al. (2006). Ordered mesoporous silica SBA-15: a new effective adjuvant to induce antibody response. Small, 2( 2), 254-256. Recuperado de http://www3.interscience.wiley.com/cgi-bin/fulltext/112213664/PDFSTART

    • NLM

      Mercuri LP, Carvalho LV, Lima FA, Quayle C, Fantini MC de A, Tanaka GS, Cabrera WH, Furtado MFD, Tambourgi DV, Matos J do R, Jaroniec M. Ordered mesoporous silica SBA-15: a new effective adjuvant to induce antibody response [Internet]. Small. 2006 ; 2( 2): 254-256.[citado 2024 jul. 13 ] Available from: http://www3.interscience.wiley.com/cgi-bin/fulltext/112213664/PDFSTART

    • Vancouver

      Mercuri LP, Carvalho LV, Lima FA, Quayle C, Fantini MC de A, Tanaka GS, Cabrera WH, Furtado MFD, Tambourgi DV, Matos J do R, Jaroniec M. Ordered mesoporous silica SBA-15: a new effective adjuvant to induce antibody response [Internet]. Small. 2006 ; 2( 2): 254-256.[citado 2024 jul. 13 ] Available from: http://www3.interscience.wiley.com/cgi-bin/fulltext/112213664/PDFSTART

  • Artigo de periodico

    The influence of urea on the structure of proteins in reversed micelles (2006)

    Caetano, Wilker; Amaral, Carmen Lucia C; Itri, Rosangela

    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: 13 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. 13 ] 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. 13 ] 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

  • Artigo de periodico

    Structural insights into the 'beta'-xylosidase from Trichoderma reesei obtained by synchrotron small-angle X-ray scaterring and circular dichroism spectroscopy (2005)

    Rojas, Adriana L.; Fischer, Hannes; Eneiskaya, Elena V.; Kulminskaya, Anna A.; Shabalin, Konstantin A.; Neustroev, Kirill N.; Craievich, Aldo Felix; Golubev, Alexander M.; Polikarpov, Igor

    Source: Biochemistry. Unidades: IF, IFSC

    Subjects: PROTEÍNAS, ENZIMAS, ESPECTROS, ESTRUTURA CELULAR

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    • ABNT

      ROJAS, Adriana L. et al. Structural insights into the 'beta'-xylosidase from Trichoderma reesei obtained by synchrotron small-angle X-ray scaterring and circular dichroism spectroscopy. Biochemistry, v. No 2005, n. 47, p. 15578-15584, 2005Tradução . . Acesso em: 13 jul. 2024.

    • APA

      Rojas, A. L., Fischer, H., Eneiskaya, E. V., Kulminskaya, A. A., Shabalin, K. A., Neustroev, K. N., et al. (2005). Structural insights into the 'beta'-xylosidase from Trichoderma reesei obtained by synchrotron small-angle X-ray scaterring and circular dichroism spectroscopy. Biochemistry, No 2005( 47), 15578-15584.

    • NLM

      Rojas AL, Fischer H, Eneiskaya EV, Kulminskaya AA, Shabalin KA, Neustroev KN, Craievich AF, Golubev AM, Polikarpov I. Structural insights into the 'beta'-xylosidase from Trichoderma reesei obtained by synchrotron small-angle X-ray scaterring and circular dichroism spectroscopy. Biochemistry. 2005 ; No 2005( 47): 15578-15584.[citado 2024 jul. 13 ]

    • Vancouver

      Rojas AL, Fischer H, Eneiskaya EV, Kulminskaya AA, Shabalin KA, Neustroev KN, Craievich AF, Golubev AM, Polikarpov I. Structural insights into the 'beta'-xylosidase from Trichoderma reesei obtained by synchrotron small-angle X-ray scaterring and circular dichroism spectroscopy. Biochemistry. 2005 ; No 2005( 47): 15578-15584.[citado 2024 jul. 13 ]

  • Artigo de periodico

    Effect of urea on bovine serum albumin in aqueous and reverse micelle environmentes investigated by small angle X-ray scattering, fluorescence and circular dichroism (2004)

    Itri, Rosangela; Caetano, Wilker; Barbosa, Leandro R S; Baptista, Maurício da Silva

    Source: Brazilian Journal of Physics. Unidades: IF, IQ

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

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    • ABNT

      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: 13 jul. 2024.

    • APA

      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. 13 ] 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. 13 ] Available from: https://doi.org/10.1590/s0103-97332004000100009

  • Trabalho de evento-resumo

    Is it possible to determine the solvent content of protein crystals from diffraction intensity analisys? (2003)

    Napolitano, H. B.; Trapani, S.; Oliva, Glaucius; Fischer, H.; Craievich, Aldo Felix

    Source: Resumos. Conference titles: Reunião da Sociedade Brasileira de Cristalografia - SBCr. Unidades: IFSC, IF

    Assunto: PROTEÍNAS

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    • ABNT

      NAPOLITANO, H. B. et al. Is it possible to determine the solvent content of protein crystals from diffraction intensity analisys? 2003, Anais.. São Carlos: Universidade de São Paulo, Instituto de Física de São Carlos, 2003. . Acesso em: 13 jul. 2024.

    • APA

      Napolitano, H. B., Trapani, S., Oliva, G., Fischer, H., & Craievich, A. F. (2003). Is it possible to determine the solvent content of protein crystals from diffraction intensity analisys? In Resumos. São Carlos: Universidade de São Paulo, Instituto de Física de São Carlos.

    • NLM

      Napolitano HB, Trapani S, Oliva G, Fischer H, Craievich AF. Is it possible to determine the solvent content of protein crystals from diffraction intensity analisys? Resumos. 2003 ;[citado 2024 jul. 13 ]

    • Vancouver

      Napolitano HB, Trapani S, Oliva G, Fischer H, Craievich AF. Is it possible to determine the solvent content of protein crystals from diffraction intensity analisys? Resumos. 2003 ;[citado 2024 jul. 13 ]

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