Filtros : "BIOFÍSICA" "Estados Unidos" "IQSC" Removidos: "ELETROQUÍMICA" "IFQSC-SQI" "PEREZ, JOELMA" "RAMOS, LUIZ ANTONIO" "Universidade de São Paulo" "IME" Limpar

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  • Fonte: Structure. Unidades: IQSC, IF

    Assuntos: 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: 18 nov. 2024.
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      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 nov. 18 ] 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 nov. 18 ] Available from: https://doi.org/10.1016/j.str.2021.08.002
  • Fonte: Abstract Book. Nome do evento: Fungal Genetics Conference. Unidade: IQSC

    Assuntos: BIOQUÍMICA, BIOFÍSICA, PROTEÍNAS

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    • ABNT

      CAMPANELLA, J. E. M. et al. The Neurospora crassa RVB-1/2 protein complex, two proteins belonging to the AAA+ ATPase protein family, plays a functional role in heat stress response. 2019, Anais.. Pacific Grove: Genetics Society of America, 2019. Disponível em: http://conferences.genetics-gsa.org/fungal/2019/program-book. Acesso em: 18 nov. 2024.
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      Campanella, J. E. M., Ramos Junior, S. L., Barros, A. C., Freitas, F. Z., Borges, J. C., Fontes, M. R. M., & Bertolini, M. C. (2019). The Neurospora crassa RVB-1/2 protein complex, two proteins belonging to the AAA+ ATPase protein family, plays a functional role in heat stress response. In Abstract Book. Pacific Grove: Genetics Society of America. Recuperado de http://conferences.genetics-gsa.org/fungal/2019/program-book
    • NLM

      Campanella JEM, Ramos Junior SL, Barros AC, Freitas FZ, Borges JC, Fontes MRM, Bertolini MC. The Neurospora crassa RVB-1/2 protein complex, two proteins belonging to the AAA+ ATPase protein family, plays a functional role in heat stress response [Internet]. Abstract Book. 2019 ;[citado 2024 nov. 18 ] Available from: http://conferences.genetics-gsa.org/fungal/2019/program-book
    • Vancouver

      Campanella JEM, Ramos Junior SL, Barros AC, Freitas FZ, Borges JC, Fontes MRM, Bertolini MC. The Neurospora crassa RVB-1/2 protein complex, two proteins belonging to the AAA+ ATPase protein family, plays a functional role in heat stress response [Internet]. Abstract Book. 2019 ;[citado 2024 nov. 18 ] Available from: http://conferences.genetics-gsa.org/fungal/2019/program-book
  • Fonte: Biophysical Journal. Nome do evento: Annual Meeting of the Biophysical Society. Unidade: IQSC

    Assunto: BIOFÍSICA

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    • ABNT

      SANTIAGO, Patricia Soares et al. Characterization of amynthas gracilis hemoglobin (HbAg) and its subunits by AUC and MALDI-TOF-MS. Biophysical Journal. St Louis: Cell Press. . Acesso em: 18 nov. 2024. , 2015
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      Santiago, P. S., Carvalho, F. A., Oliveira, J. B. S., Linhares, A. P. D., Morgante, P. G., Carvalho, J. W. P., & Tabak, M. (2015). Characterization of amynthas gracilis hemoglobin (HbAg) and its subunits by AUC and MALDI-TOF-MS. Biophysical Journal. St Louis: Cell Press.
    • NLM

      Santiago PS, Carvalho FA, Oliveira JBS, Linhares APD, Morgante PG, Carvalho JWP, Tabak M. Characterization of amynthas gracilis hemoglobin (HbAg) and its subunits by AUC and MALDI-TOF-MS. Biophysical Journal. 2015 ; 108( 2): 375A.[citado 2024 nov. 18 ]
    • Vancouver

      Santiago PS, Carvalho FA, Oliveira JBS, Linhares APD, Morgante PG, Carvalho JWP, Tabak M. Characterization of amynthas gracilis hemoglobin (HbAg) and its subunits by AUC and MALDI-TOF-MS. Biophysical Journal. 2015 ; 108( 2): 375A.[citado 2024 nov. 18 ]
  • Fonte: Archives of Biochemistry and Biophysics. Unidades: IQSC, IF

    Assuntos: BIOFÍSICA, BIOLOGIA MOLECULAR

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    • ABNT

      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: 18 nov. 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
    • NLM

      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 nov. 18 ] 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 nov. 18 ] Available from: https://doi.org/10.1016/j.abb.2014.10.015
  • Fonte: Archives of Biochemistry and Biophysics. Unidades: IF, IQSC

    Assuntos: BIOFÍSICA, BIOLOGIA MOLECULAR

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    • ABNT

      DORES-SILVA, Paulo Roberto das et al. Low resolution structural characterization of the Hsp70-interacting protein – Hip – from Leishmania braziliensis emphasizes its high asymmetry. Archives of Biochemistry and Biophysics, v. 520, n. 2, p. 88-98, 2012Tradução . . Disponível em: https://doi.org/10.1016/j.abb.2012.02.009. Acesso em: 18 nov. 2024.
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      Dores-Silva, P. R. das, Silva, E. R., Gomes, F. E. R., Silva, K. P., Barbosa, L. R. S., & Borges, J. C. (2012). Low resolution structural characterization of the Hsp70-interacting protein – Hip – from Leishmania braziliensis emphasizes its high asymmetry. Archives of Biochemistry and Biophysics, 520( 2), 88-98. doi:10.1016/j.abb.2012.02.009
    • NLM

      Dores-Silva PR das, Silva ER, Gomes FER, Silva KP, Barbosa LRS, Borges JC. Low resolution structural characterization of the Hsp70-interacting protein – Hip – from Leishmania braziliensis emphasizes its high asymmetry [Internet]. Archives of Biochemistry and Biophysics. 2012 ; 520( 2): 88-98.[citado 2024 nov. 18 ] Available from: https://doi.org/10.1016/j.abb.2012.02.009
    • Vancouver

      Dores-Silva PR das, Silva ER, Gomes FER, Silva KP, Barbosa LRS, Borges JC. Low resolution structural characterization of the Hsp70-interacting protein – Hip – from Leishmania braziliensis emphasizes its high asymmetry [Internet]. Archives of Biochemistry and Biophysics. 2012 ; 520( 2): 88-98.[citado 2024 nov. 18 ] Available from: https://doi.org/10.1016/j.abb.2012.02.009
  • Fonte: Archives of Biochemistry and Biophysics. Unidade: IQSC

    Assuntos: BIOFÍSICA, BIOLOGIA MOLECULAR

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    • ABNT

      CARVALHO, Francisco Adriano O e SANTIAGO, Patricia Soares e TABAK, Marcel. On the stability of the extracellular hemoglobin of glossoscolex paulistus, in two iron oxidation sates, in the presence of urea. Archives of Biochemistry and Biophysics, v. 519, n. 1, p. 46-58, 2012Tradução . . Disponível em: https://doi.org/10.1016/j.abb.2012.01.007. Acesso em: 18 nov. 2024.
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      Carvalho, F. A. O., Santiago, P. S., & Tabak, M. (2012). On the stability of the extracellular hemoglobin of glossoscolex paulistus, in two iron oxidation sates, in the presence of urea. Archives of Biochemistry and Biophysics, 519( 1), 46-58. doi:10.1016/j.abb.2012.01.007
    • NLM

      Carvalho FAO, Santiago PS, Tabak M. On the stability of the extracellular hemoglobin of glossoscolex paulistus, in two iron oxidation sates, in the presence of urea [Internet]. Archives of Biochemistry and Biophysics. 2012 ; 519( 1): 46-58.[citado 2024 nov. 18 ] Available from: https://doi.org/10.1016/j.abb.2012.01.007
    • Vancouver

      Carvalho FAO, Santiago PS, Tabak M. On the stability of the extracellular hemoglobin of glossoscolex paulistus, in two iron oxidation sates, in the presence of urea [Internet]. Archives of Biochemistry and Biophysics. 2012 ; 519( 1): 46-58.[citado 2024 nov. 18 ] Available from: https://doi.org/10.1016/j.abb.2012.01.007
  • Fonte: Archives of Biochemistry and Biophysics. Unidade: IQSC

    Assuntos: BIOFÍSICA, BIOLOGIA MOLECULAR

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    • ABNT

      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: 18 nov. 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 nov. 18 ] 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 nov. 18 ] Available from: https://doi.org/10.1016/j.abb.2011.06.015
  • Fonte: Abstracts. Nome do evento: Biophysical Society Annual Meeting. Unidade: IQSC

    Assunto: BIOFÍSICA

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    • ABNT

      SANTIAGO, Patricia Soares et al. On the thermal stability of extracellular hemoglobin of glossoscolex paulistus: optical spectroscopic studies. 2010, Anais.. San Francisco: Instituto de Química de São Carlos, Universidade de São Paulo, 2010. . Acesso em: 18 nov. 2024.
    • APA

      Santiago, P. S., Carvalho, J. W. P., Poli, A. L., Domingues, M. M., Santos, N. C., & Tabak, M. (2010). On the thermal stability of extracellular hemoglobin of glossoscolex paulistus: optical spectroscopic studies. In Abstracts. San Francisco: Instituto de Química de São Carlos, Universidade de São Paulo.
    • NLM

      Santiago PS, Carvalho JWP, Poli AL, Domingues MM, Santos NC, Tabak M. On the thermal stability of extracellular hemoglobin of glossoscolex paulistus: optical spectroscopic studies. Abstracts. 2010 ;[citado 2024 nov. 18 ]
    • Vancouver

      Santiago PS, Carvalho JWP, Poli AL, Domingues MM, Santos NC, Tabak M. On the thermal stability of extracellular hemoglobin of glossoscolex paulistus: optical spectroscopic studies. Abstracts. 2010 ;[citado 2024 nov. 18 ]
  • Fonte: Langmuir. Unidade: IQSC

    Assunto: BIOFÍSICA

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    • ABNT

      SANTIAGO, Patricia Soares et al. Isoelectric point determination for glossoscolex paulistus extracellular hemoglobin: oligomeric stability in acidic pH and relevance to protein - surfactant interactions. Langmuir, v. 26, n. 12, p. 9794-9801, 2010Tradução . . Disponível em: http://pubs.acs.org/doi/abs/10.1021/la100060p. Acesso em: 18 nov. 2024.
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      Santiago, P. S., Carvalho, F. A. O., Domingues, M. M., Carvalho, J. W. P., Santos, N. C., & Tabak, M. (2010). Isoelectric point determination for glossoscolex paulistus extracellular hemoglobin: oligomeric stability in acidic pH and relevance to protein - surfactant interactions. Langmuir, 26( 12), 9794-9801. Recuperado de http://pubs.acs.org/doi/abs/10.1021/la100060p
    • NLM

      Santiago PS, Carvalho FAO, Domingues MM, Carvalho JWP, Santos NC, Tabak M. Isoelectric point determination for glossoscolex paulistus extracellular hemoglobin: oligomeric stability in acidic pH and relevance to protein - surfactant interactions [Internet]. Langmuir. 2010 ; 26( 12): 9794-9801.[citado 2024 nov. 18 ] Available from: http://pubs.acs.org/doi/abs/10.1021/la100060p
    • Vancouver

      Santiago PS, Carvalho FAO, Domingues MM, Carvalho JWP, Santos NC, Tabak M. Isoelectric point determination for glossoscolex paulistus extracellular hemoglobin: oligomeric stability in acidic pH and relevance to protein - surfactant interactions [Internet]. Langmuir. 2010 ; 26( 12): 9794-9801.[citado 2024 nov. 18 ] Available from: http://pubs.acs.org/doi/abs/10.1021/la100060p
  • Fonte: Abstracts. Nome do evento: Biophysical Society Annual Meeting. Unidade: IQSC

    Assunto: BIOFÍSICA

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    • ABNT

      CARVALHO, José Wilson Pires e SANTIAGO, Patricia Soares e TABAK, Marcel. Thermal stability of the extracellular hemoglobin off glossoscolex paulistus: differential scanning calorimetry (DSC) and circular dichroism (CD) studies. 2010, Anais.. San Francisco: Instituto de Química de São Carlos, Universidade de São Paulo, 2010. . Acesso em: 18 nov. 2024.
    • APA

      Carvalho, J. W. P., Santiago, P. S., & Tabak, M. (2010). Thermal stability of the extracellular hemoglobin off glossoscolex paulistus: differential scanning calorimetry (DSC) and circular dichroism (CD) studies. In Abstracts. San Francisco: Instituto de Química de São Carlos, Universidade de São Paulo.
    • NLM

      Carvalho JWP, Santiago PS, Tabak M. Thermal stability of the extracellular hemoglobin off glossoscolex paulistus: differential scanning calorimetry (DSC) and circular dichroism (CD) studies. Abstracts. 2010 ;[citado 2024 nov. 18 ]
    • Vancouver

      Carvalho JWP, Santiago PS, Tabak M. Thermal stability of the extracellular hemoglobin off glossoscolex paulistus: differential scanning calorimetry (DSC) and circular dichroism (CD) studies. Abstracts. 2010 ;[citado 2024 nov. 18 ]
  • Fonte: Biophysical Journal. Unidade: IQSC

    Assunto: BIOFÍSICA

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    • ABNT

      SANTIAGO, Patricia Soares et al. Dynamic light scaterring and optical absorption spectroscopy study of pH and temperature stabilities of the extracellular hemoglobin of glossoscolex paulistus. Biophysical Journal, v. 94, p. 2228-2240, 2008Tradução . . Disponível em: http://www.biophysj.org/cgi/reprint/94/6/2228. Acesso em: 18 nov. 2024.
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      Santiago, P. S., Moura, F., Moreira, L. M., Domingues, M. M., Santos, N. C., & Tabak, M. (2008). Dynamic light scaterring and optical absorption spectroscopy study of pH and temperature stabilities of the extracellular hemoglobin of glossoscolex paulistus. Biophysical Journal, 94, 2228-2240. Recuperado de http://www.biophysj.org/cgi/reprint/94/6/2228
    • NLM

      Santiago PS, Moura F, Moreira LM, Domingues MM, Santos NC, Tabak M. Dynamic light scaterring and optical absorption spectroscopy study of pH and temperature stabilities of the extracellular hemoglobin of glossoscolex paulistus [Internet]. Biophysical Journal. 2008 ; 94 2228-2240.[citado 2024 nov. 18 ] Available from: http://www.biophysj.org/cgi/reprint/94/6/2228
    • Vancouver

      Santiago PS, Moura F, Moreira LM, Domingues MM, Santos NC, Tabak M. Dynamic light scaterring and optical absorption spectroscopy study of pH and temperature stabilities of the extracellular hemoglobin of glossoscolex paulistus [Internet]. Biophysical Journal. 2008 ; 94 2228-2240.[citado 2024 nov. 18 ] Available from: http://www.biophysj.org/cgi/reprint/94/6/2228
  • Fonte: Journal of Physical Chemistry B. Unidades: IF, IQSC

    Assuntos: ESPECTROSCOPIA DE RAIO X, BIOFÍSICA

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    • ABNT

      BARBOSA, Leandro R. S. et al. Self-assembling of phenothiazine compounds investigated by small-angle x-ray scattering and electron paramagnetic resonance spectroscopy. Journal of Physical Chemistry B, v. 112, n. 14, p. 4261-4269, 2008Tradução . . Disponível em: http://pubs.acs.org/cgi-bin/article.cgi/jpcbfk/2008/112/i14/pdf/jp710332t.pdf. Acesso em: 18 nov. 2024.
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      Barbosa, L. R. S., Itri, R., Caetano, W., Sousa Neto, D. de, & Tabak, M. (2008). Self-assembling of phenothiazine compounds investigated by small-angle x-ray scattering and electron paramagnetic resonance spectroscopy. Journal of Physical Chemistry B, 112( 14), 4261-4269. Recuperado de http://pubs.acs.org/cgi-bin/article.cgi/jpcbfk/2008/112/i14/pdf/jp710332t.pdf
    • NLM

      Barbosa LRS, Itri R, Caetano W, Sousa Neto D de, Tabak M. Self-assembling of phenothiazine compounds investigated by small-angle x-ray scattering and electron paramagnetic resonance spectroscopy [Internet]. Journal of Physical Chemistry B. 2008 ; 112( 14): 4261-4269.[citado 2024 nov. 18 ] Available from: http://pubs.acs.org/cgi-bin/article.cgi/jpcbfk/2008/112/i14/pdf/jp710332t.pdf
    • Vancouver

      Barbosa LRS, Itri R, Caetano W, Sousa Neto D de, Tabak M. Self-assembling of phenothiazine compounds investigated by small-angle x-ray scattering and electron paramagnetic resonance spectroscopy [Internet]. Journal of Physical Chemistry B. 2008 ; 112( 14): 4261-4269.[citado 2024 nov. 18 ] Available from: http://pubs.acs.org/cgi-bin/article.cgi/jpcbfk/2008/112/i14/pdf/jp710332t.pdf
  • Fonte: Plant Molecular Biology Reporter. Unidades: IFSC, IQSC

    Assuntos: ENZIMAS, CANA-DE-AÇÚCAR, BIOFÍSICA

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      SCULACCIO, Susana Andrea et al. Sugarcane phosphoribosyl pyrophosphate synthetase: molecular characterization of a phosphate-independent PRS. Plant Molecular Biology Reporter, v. 26, n. 4, p. 301-315, 2008Tradução . . Disponível em: https://doi.org/10.1007/s11105-008-0043-6. Acesso em: 18 nov. 2024.
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      Sculaccio, S. A., Napolitano, H. B., Beltramini, L. M., Oliva, G., Carrilho, E., & Thiemann, O. H. (2008). Sugarcane phosphoribosyl pyrophosphate synthetase: molecular characterization of a phosphate-independent PRS. Plant Molecular Biology Reporter, 26( 4), 301-315. doi:10.1007/s11105-008-0043-6
    • NLM

      Sculaccio SA, Napolitano HB, Beltramini LM, Oliva G, Carrilho E, Thiemann OH. Sugarcane phosphoribosyl pyrophosphate synthetase: molecular characterization of a phosphate-independent PRS [Internet]. Plant Molecular Biology Reporter. 2008 ; 26( 4): 301-315.[citado 2024 nov. 18 ] Available from: https://doi.org/10.1007/s11105-008-0043-6
    • Vancouver

      Sculaccio SA, Napolitano HB, Beltramini LM, Oliva G, Carrilho E, Thiemann OH. Sugarcane phosphoribosyl pyrophosphate synthetase: molecular characterization of a phosphate-independent PRS [Internet]. Plant Molecular Biology Reporter. 2008 ; 26( 4): 301-315.[citado 2024 nov. 18 ] Available from: https://doi.org/10.1007/s11105-008-0043-6
  • Fonte: Abstracts. Nome do evento: Biophysical Society Annual Meeting. Unidade: IQSC

    Assunto: BIOFÍSICA

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    • ABNT

      SANTIAGO, Patricia Soares et al. On the molecular mass of the extracellular hemoglobin of glossoscolex paulistus: analytical ultracentrifugation re-examination. 2008, Anais.. Long Beach: Instituto de Química de São Carlos, Universidade de São Paulo, 2008. . Acesso em: 18 nov. 2024.
    • APA

      Santiago, P. S., Oliveira, M. S., Borges, J. C., & Tabak, M. (2008). On the molecular mass of the extracellular hemoglobin of glossoscolex paulistus: analytical ultracentrifugation re-examination. In Abstracts. Long Beach: Instituto de Química de São Carlos, Universidade de São Paulo.
    • NLM

      Santiago PS, Oliveira MS, Borges JC, Tabak M. On the molecular mass of the extracellular hemoglobin of glossoscolex paulistus: analytical ultracentrifugation re-examination. Abstracts. 2008 ;[citado 2024 nov. 18 ]
    • Vancouver

      Santiago PS, Oliveira MS, Borges JC, Tabak M. On the molecular mass of the extracellular hemoglobin of glossoscolex paulistus: analytical ultracentrifugation re-examination. Abstracts. 2008 ;[citado 2024 nov. 18 ]
  • Fonte: Journal of Inorganic Biochemistry. Unidade: IQSC

    Assuntos: BIOFÍSICA, BIOQUÍMICA

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      SANTIAGO, Patricia Soares e MOREIRA, Leonardo Marmo e TABAK, Marcel. Phosphate group effects upon the equilibrium of iron(III) meso-tetrakis (4-N-methylpyridiniumyl) porphyrin in aqueous solution. Journal of Inorganic Biochemistry, v. 100, n. 11, p. 1715-1721, 2006Tradução . . Disponível em: https://doi.org/10.1016/j.jinorgbio.2006.03.018. Acesso em: 18 nov. 2024.
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      Santiago, P. S., Moreira, L. M., & Tabak, M. (2006). Phosphate group effects upon the equilibrium of iron(III) meso-tetrakis (4-N-methylpyridiniumyl) porphyrin in aqueous solution. Journal of Inorganic Biochemistry, 100( 11), 1715-1721. doi:10.1016/j.jinorgbio.2006.03.018
    • NLM

      Santiago PS, Moreira LM, Tabak M. Phosphate group effects upon the equilibrium of iron(III) meso-tetrakis (4-N-methylpyridiniumyl) porphyrin in aqueous solution [Internet]. Journal of Inorganic Biochemistry. 2006 ; 100( 11): 1715-1721.[citado 2024 nov. 18 ] Available from: https://doi.org/10.1016/j.jinorgbio.2006.03.018
    • Vancouver

      Santiago PS, Moreira LM, Tabak M. Phosphate group effects upon the equilibrium of iron(III) meso-tetrakis (4-N-methylpyridiniumyl) porphyrin in aqueous solution [Internet]. Journal of Inorganic Biochemistry. 2006 ; 100( 11): 1715-1721.[citado 2024 nov. 18 ] Available from: https://doi.org/10.1016/j.jinorgbio.2006.03.018
  • Fonte: The Journal of Physical Chemistry Part B. Unidades: IF, IQSC

    Assuntos: DIFRAÇÃO POR RAIOS X, BIOFÍSICA

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    • ABNT

      GANDINI, Shirley C M et al. Porphyrin effects on zwitterionic HPS micelles as investigated by small-angle X-ray scattering (SAXS) and electron paramagnetic resonance (EPR). The Journal of Physical Chemistry Part B, v. 109, n. 47, p. 22264-22272, 2005Tradução . . Disponível em: http://pubs3.acs.org/acs/journals/toc.page?incoden=jpcbfk&indecade=0&involume=109&inissue=47. Acesso em: 18 nov. 2024.
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      Gandini, S. C. M., Itri, R., Sousa Neto, D. de, & Tabak, M. (2005). Porphyrin effects on zwitterionic HPS micelles as investigated by small-angle X-ray scattering (SAXS) and electron paramagnetic resonance (EPR). The Journal of Physical Chemistry Part B, 109( 47), 22264-22272. Recuperado de http://pubs3.acs.org/acs/journals/toc.page?incoden=jpcbfk&indecade=0&involume=109&inissue=47
    • NLM

      Gandini SCM, Itri R, Sousa Neto D de, Tabak M. Porphyrin effects on zwitterionic HPS micelles as investigated by small-angle X-ray scattering (SAXS) and electron paramagnetic resonance (EPR) [Internet]. The Journal of Physical Chemistry Part B. 2005 ; 109( 47): 22264-22272.[citado 2024 nov. 18 ] Available from: http://pubs3.acs.org/acs/journals/toc.page?incoden=jpcbfk&indecade=0&involume=109&inissue=47
    • Vancouver

      Gandini SCM, Itri R, Sousa Neto D de, Tabak M. Porphyrin effects on zwitterionic HPS micelles as investigated by small-angle X-ray scattering (SAXS) and electron paramagnetic resonance (EPR) [Internet]. The Journal of Physical Chemistry Part B. 2005 ; 109( 47): 22264-22272.[citado 2024 nov. 18 ] Available from: http://pubs3.acs.org/acs/journals/toc.page?incoden=jpcbfk&indecade=0&involume=109&inissue=47
  • Fonte: Biophysical Journal. Unidades: IQSC, IF

    Assunto: BIOFÍSICA

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    • ABNT

      GANDINI, Shirley de Cássia Monte et al. Small angle x-ray scattering study of meso-tetrakis (4-sulfonatophenyl) porphyrin in aqueous solution. Biophysical Journal, v. 85, p. 1259-1268, 2003Tradução . . Acesso em: 18 nov. 2024.
    • APA

      Gandini, S. de C. M., Gelamo, E. L., Itri, R., & Tabak, M. (2003). Small angle x-ray scattering study of meso-tetrakis (4-sulfonatophenyl) porphyrin in aqueous solution. Biophysical Journal, 85, 1259-1268.
    • NLM

      Gandini S de CM, Gelamo EL, Itri R, Tabak M. Small angle x-ray scattering study of meso-tetrakis (4-sulfonatophenyl) porphyrin in aqueous solution. Biophysical Journal. 2003 ; 85 1259-1268.[citado 2024 nov. 18 ]
    • Vancouver

      Gandini S de CM, Gelamo EL, Itri R, Tabak M. Small angle x-ray scattering study of meso-tetrakis (4-sulfonatophenyl) porphyrin in aqueous solution. Biophysical Journal. 2003 ; 85 1259-1268.[citado 2024 nov. 18 ]
  • Fonte: Journal of Mass Spectrometry. Unidade: IQSC

    Assunto: BIOFÍSICA

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      RODRIGUES FILHO, Edson e TABAK, Marcel e ALMEIDA, Adaila Marta Paixão. Fragmentation of dipyridamole and related dipyrimidines by electrospray ionization collisional activated decomposition mass spectrometry. Journal of Mass Spectrometry, v. 38, p. 54-547, 2003Tradução . . Disponível em: https://doi.org/10.1002/jms.468. Acesso em: 18 nov. 2024.
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      Rodrigues Filho, E., Tabak, M., & Almeida, A. M. P. (2003). Fragmentation of dipyridamole and related dipyrimidines by electrospray ionization collisional activated decomposition mass spectrometry. Journal of Mass Spectrometry, 38, 54-547. doi:10.1002/jms.468
    • NLM

      Rodrigues Filho E, Tabak M, Almeida AMP. Fragmentation of dipyridamole and related dipyrimidines by electrospray ionization collisional activated decomposition mass spectrometry [Internet]. Journal of Mass Spectrometry. 2003 ; 38 54-547.[citado 2024 nov. 18 ] Available from: https://doi.org/10.1002/jms.468
    • Vancouver

      Rodrigues Filho E, Tabak M, Almeida AMP. Fragmentation of dipyridamole and related dipyrimidines by electrospray ionization collisional activated decomposition mass spectrometry [Internet]. Journal of Mass Spectrometry. 2003 ; 38 54-547.[citado 2024 nov. 18 ] Available from: https://doi.org/10.1002/jms.468
  • Fonte: Biophysical Journal. Nome do evento: Annual Meeting of the Biophysical Society. Unidade: IQSC

    Assunto: BIOFÍSICA

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    • ABNT

      GELAMO, Emerson Luiz e BIANCONI, Maria Lucia e TABAK, Marcel. Ionic surfactants interaction with human (HSA) and bovine (BSA) serum albumins: an ITC study. Biophysical Journal. Bethesda: Instituto de Química de São Carlos, Universidade de São Paulo. . Acesso em: 18 nov. 2024. , 2002
    • APA

      Gelamo, E. L., Bianconi, M. L., & Tabak, M. (2002). Ionic surfactants interaction with human (HSA) and bovine (BSA) serum albumins: an ITC study. Biophysical Journal. Bethesda: Instituto de Química de São Carlos, Universidade de São Paulo.
    • NLM

      Gelamo EL, Bianconi ML, Tabak M. Ionic surfactants interaction with human (HSA) and bovine (BSA) serum albumins: an ITC study. Biophysical Journal. 2002 ; 82( 1): 335a.[citado 2024 nov. 18 ]
    • Vancouver

      Gelamo EL, Bianconi ML, Tabak M. Ionic surfactants interaction with human (HSA) and bovine (BSA) serum albumins: an ITC study. Biophysical Journal. 2002 ; 82( 1): 335a.[citado 2024 nov. 18 ]
  • Fonte: Biophysical Journal. Nome do evento: Annual Meeting of the Biophysical Society. Unidade: IQSC

    Assunto: BIOFÍSICA

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    • ABNT

      TABAK, Marcel e SANTIAGO, Patricia Soares e GANDINI, Shirley de Cássia Monte. Interaction of Fe(III)-TMPyP with ionic micelles: an optical absorption, light scattering and NMR study. Biophysical Journal. Bethesda: Instituto de Química de São Carlos, Universidade de São Paulo. . Acesso em: 18 nov. 2024. , 2002
    • APA

      Tabak, M., Santiago, P. S., & Gandini, S. de C. M. (2002). Interaction of Fe(III)-TMPyP with ionic micelles: an optical absorption, light scattering and NMR study. Biophysical Journal. Bethesda: Instituto de Química de São Carlos, Universidade de São Paulo.
    • NLM

      Tabak M, Santiago PS, Gandini S de CM. Interaction of Fe(III)-TMPyP with ionic micelles: an optical absorption, light scattering and NMR study. Biophysical Journal. 2002 ; 82( 1): 545a.[citado 2024 nov. 18 ]
    • Vancouver

      Tabak M, Santiago PS, Gandini S de CM. Interaction of Fe(III)-TMPyP with ionic micelles: an optical absorption, light scattering and NMR study. Biophysical Journal. 2002 ; 82( 1): 545a.[citado 2024 nov. 18 ]

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