Filtros : "Indexado no Science Citation Index" "Polikarpov, Igor" "2003" Removidos: "Bissa, W M" "Elsevier" Limpar

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  • Source: Acta Crystallographica D. Unidade: IFSC

    Subjects: CRISTALOGRAFIA, SEQUÊNCIA DE AMINOÁCIDOS, ENZIMAS, PROTEÍNAS, VENENOS DE ORIGEM ANIMAL

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    • ABNT

      RIGDEN, Daniel J. et al. The structure of the D49 phospholipase 'A IND.2' piratoxin III from Bothrops pirajai reveals unprecedented structural displacement of the calcuim-binding loop: possible relationship to cooperative substrate binding. Acta Crystallographica D, v. 59, p. 255-262, 2003Tradução . . Disponível em: https://doi.org/10.1107/s0907444902021467. Acesso em: 16 out. 2024.
    • APA

      Rigden, D. J., Lee, W. -H., Marangoni, S., Toyama, M. H., & Polikarpov, I. (2003). The structure of the D49 phospholipase 'A IND.2' piratoxin III from Bothrops pirajai reveals unprecedented structural displacement of the calcuim-binding loop: possible relationship to cooperative substrate binding. Acta Crystallographica D, 59, 255-262. doi:10.1107/s0907444902021467
    • NLM

      Rigden DJ, Lee W-H, Marangoni S, Toyama MH, Polikarpov I. The structure of the D49 phospholipase 'A IND.2' piratoxin III from Bothrops pirajai reveals unprecedented structural displacement of the calcuim-binding loop: possible relationship to cooperative substrate binding [Internet]. Acta Crystallographica D. 2003 ; 59 255-262.[citado 2024 out. 16 ] Available from: https://doi.org/10.1107/s0907444902021467
    • Vancouver

      Rigden DJ, Lee W-H, Marangoni S, Toyama MH, Polikarpov I. The structure of the D49 phospholipase 'A IND.2' piratoxin III from Bothrops pirajai reveals unprecedented structural displacement of the calcuim-binding loop: possible relationship to cooperative substrate binding [Internet]. Acta Crystallographica D. 2003 ; 59 255-262.[citado 2024 out. 16 ] Available from: https://doi.org/10.1107/s0907444902021467
  • Source: Acta Crystallographica D. Unidades: FCF, IFSC

    Subjects: CRISTALOGRAFIA, ENZIMAS

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      SANCHES, Mario et al. Structural comparison of Escherichia coli l-asparaginase in two monoclinic space groups. Acta Crystallographica D, v. 59, p. 416-422, 2003Tradução . . Disponível em: https://doi.org/10.1107/s0907444902021200. Acesso em: 16 out. 2024.
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      Sanches, M., Barbosa, J. A. R. G., Oliveira, R. T., Abrahão Neto, J., & Polikarpov, I. (2003). Structural comparison of Escherichia coli l-asparaginase in two monoclinic space groups. Acta Crystallographica D, 59, 416-422. doi:10.1107/s0907444902021200
    • NLM

      Sanches M, Barbosa JARG, Oliveira RT, Abrahão Neto J, Polikarpov I. Structural comparison of Escherichia coli l-asparaginase in two monoclinic space groups [Internet]. Acta Crystallographica D. 2003 ; 59 416-422.[citado 2024 out. 16 ] Available from: https://doi.org/10.1107/s0907444902021200
    • Vancouver

      Sanches M, Barbosa JARG, Oliveira RT, Abrahão Neto J, Polikarpov I. Structural comparison of Escherichia coli l-asparaginase in two monoclinic space groups [Internet]. Acta Crystallographica D. 2003 ; 59 416-422.[citado 2024 out. 16 ] Available from: https://doi.org/10.1107/s0907444902021200
  • Source: Biochemical and Biophysical Research Communications. Unidade: IFSC

    Subjects: CRISTALOGRAFIA, CRISTALIZAÇÃO, RAIOS X

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      KRAUCHENKO, Sandra et al. Crystal structure of the Kunitz (STI)-type inhibitor from Delonix regia seeds. Biochemical and Biophysical Research Communications, v. 312, n. 4, p. 1303-1308, 2003Tradução . . Disponível em: https://doi.org/10.1016/j.bbrc.2003.11.062. Acesso em: 16 out. 2024.
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      Krauchenko, S., Pando, S. C., Marangoni, S., & Polikarpov, I. (2003). Crystal structure of the Kunitz (STI)-type inhibitor from Delonix regia seeds. Biochemical and Biophysical Research Communications, 312( 4), 1303-1308. doi:10.1016/j.bbrc.2003.11.062
    • NLM

      Krauchenko S, Pando SC, Marangoni S, Polikarpov I. Crystal structure of the Kunitz (STI)-type inhibitor from Delonix regia seeds [Internet]. Biochemical and Biophysical Research Communications. 2003 ; 312( 4): 1303-1308.[citado 2024 out. 16 ] Available from: https://doi.org/10.1016/j.bbrc.2003.11.062
    • Vancouver

      Krauchenko S, Pando SC, Marangoni S, Polikarpov I. Crystal structure of the Kunitz (STI)-type inhibitor from Delonix regia seeds [Internet]. Biochemical and Biophysical Research Communications. 2003 ; 312( 4): 1303-1308.[citado 2024 out. 16 ] Available from: https://doi.org/10.1016/j.bbrc.2003.11.062
  • Source: Acta Crystallographica D. Unidade: IFSC

    Subjects: CRISTALOGRAFIA, TOXINAS

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      PINHEIRO, Carlos Basílio et al. Structural analysis of Tityus serrulatus Ts1 neurotoxin at atomic resolution: insights into interactions with 'Na POT.+' channels. Acta Crystallographica D, v. 59, p. 405-415, 2003Tradução . . Disponível em: https://doi.org/10.1107/s090744490202111x. Acesso em: 16 out. 2024.
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      Pinheiro, C. B., Marangoni, S., Toyama, M. H., & Polikarpov, I. (2003). Structural analysis of Tityus serrulatus Ts1 neurotoxin at atomic resolution: insights into interactions with 'Na POT.+' channels. Acta Crystallographica D, 59, 405-415. doi:10.1107/s090744490202111x
    • NLM

      Pinheiro CB, Marangoni S, Toyama MH, Polikarpov I. Structural analysis of Tityus serrulatus Ts1 neurotoxin at atomic resolution: insights into interactions with 'Na POT.+' channels [Internet]. Acta Crystallographica D. 2003 ; 59 405-415.[citado 2024 out. 16 ] Available from: https://doi.org/10.1107/s090744490202111x
    • Vancouver

      Pinheiro CB, Marangoni S, Toyama MH, Polikarpov I. Structural analysis of Tityus serrulatus Ts1 neurotoxin at atomic resolution: insights into interactions with 'Na POT.+' channels [Internet]. Acta Crystallographica D. 2003 ; 59 405-415.[citado 2024 out. 16 ] Available from: https://doi.org/10.1107/s090744490202111x
  • Source: Methods in Enzymology. Unidade: IFSC

    Assunto: CRISTALOGRAFIA

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      NAGEM, R. A. P. e POLIKARPOV, Igor e DAUTER, Z. Phasing on rapidly soaked ions. Methods in Enzymology, v. 374, p. 120-137, 2003Tradução . . Acesso em: 16 out. 2024.
    • APA

      Nagem, R. A. P., Polikarpov, I., & Dauter, Z. (2003). Phasing on rapidly soaked ions. Methods in Enzymology, 374, 120-137.
    • NLM

      Nagem RAP, Polikarpov I, Dauter Z. Phasing on rapidly soaked ions. Methods in Enzymology. 2003 ; 374 120-137.[citado 2024 out. 16 ]
    • Vancouver

      Nagem RAP, Polikarpov I, Dauter Z. Phasing on rapidly soaked ions. Methods in Enzymology. 2003 ; 374 120-137.[citado 2024 out. 16 ]
  • Source: Journal of Molecular Biology. Unidade: IFSC

    Subjects: CRISTALOGRAFIA, PROTEÍNAS

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      APARICIO, Ricardo e FERREIRA, Sérgio T. e POLIKARPOV, Igor. Closed conformation of the active site loop of rabbit muscle triosephosphate isomerase in the absence of substrate: evidence of conformational heterogeneity. Journal of Molecular Biology, v. 334, n. 5, p. 1023-1041, 2003Tradução . . Acesso em: 16 out. 2024.
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      Aparicio, R., Ferreira, S. T., & Polikarpov, I. (2003). Closed conformation of the active site loop of rabbit muscle triosephosphate isomerase in the absence of substrate: evidence of conformational heterogeneity. Journal of Molecular Biology, 334( 5), 1023-1041.
    • NLM

      Aparicio R, Ferreira ST, Polikarpov I. Closed conformation of the active site loop of rabbit muscle triosephosphate isomerase in the absence of substrate: evidence of conformational heterogeneity. Journal of Molecular Biology. 2003 ; 334( 5): 1023-1041.[citado 2024 out. 16 ]
    • Vancouver

      Aparicio R, Ferreira ST, Polikarpov I. Closed conformation of the active site loop of rabbit muscle triosephosphate isomerase in the absence of substrate: evidence of conformational heterogeneity. Journal of Molecular Biology. 2003 ; 334( 5): 1023-1041.[citado 2024 out. 16 ]
  • Source: Journal of Biological Chemistry. Unidades: IF, IFSC

    Subjects: BIOLOGIA MOLECULAR, CRISTALOGRAFIA FÍSICA, DNA, BIOQUÍMICA, PROTEÍNAS

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      FISCHER, Hannes et al. Low resolution structures of the retinoid X receptor DNA-binding and ligand-binding domains revealed by synchrotron X-ray solution scattering. Journal of Biological Chemistry, v. 278, n. 18, p. 16030-16038, 2003Tradução . . Acesso em: 16 out. 2024.
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      Fischer, H., Dias, S. M. G., Santos, M. A. M., Alves, A. C., Zanchin, N., Craievich, A. F., et al. (2003). Low resolution structures of the retinoid X receptor DNA-binding and ligand-binding domains revealed by synchrotron X-ray solution scattering. Journal of Biological Chemistry, 278( 18), 16030-16038.
    • NLM

      Fischer H, Dias SMG, Santos MAM, Alves AC, Zanchin N, Craievich AF, Apriletti JW, Baxter J, Webb P, Neves FAR, Ribeiro RCJ, Polikarpov I. Low resolution structures of the retinoid X receptor DNA-binding and ligand-binding domains revealed by synchrotron X-ray solution scattering. Journal of Biological Chemistry. 2003 ; 278( 18): 16030-16038.[citado 2024 out. 16 ]
    • Vancouver

      Fischer H, Dias SMG, Santos MAM, Alves AC, Zanchin N, Craievich AF, Apriletti JW, Baxter J, Webb P, Neves FAR, Ribeiro RCJ, Polikarpov I. Low resolution structures of the retinoid X receptor DNA-binding and ligand-binding domains revealed by synchrotron X-ray solution scattering. Journal of Biological Chemistry. 2003 ; 278( 18): 16030-16038.[citado 2024 out. 16 ]

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