Filtros : "ENZIMAS" "Acta Crystallographica D" Removidos: "PARTE DE MONOGRAFIA/LIVRO" "Universidade do Vale do Itajaí (Univali)" Limpar

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  • Source: Acta Crystallographica D. Unidade: IFSC

    Subjects: SCHISTOSOMA MANSONI, ENZIMAS, NUCLEOSÍDEOS

    Acesso à fonteDOIHow to cite
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    • ABNT

      PEREIRA, Humberto d'Muniz et al. Adenosine binding to low-molecular-weight purine nucleoside phosphorylase: the structural basis for recognition based on its complex with the enzyme from Schistosoma mansoni. Acta Crystallographica D, v. 66, n. Ja 2010, p. 73-79, 2010Tradução . . Disponível em: https://doi.org/10.1107/S0907444909045715. Acesso em: 07 set. 2024.
    • APA

      Pereira, H. d'M., Rezende, M. M., Castilho, M. S., Oliva, G., & Garratt, R. C. (2010). Adenosine binding to low-molecular-weight purine nucleoside phosphorylase: the structural basis for recognition based on its complex with the enzyme from Schistosoma mansoni. Acta Crystallographica D, 66( Ja 2010), 73-79. doi:10.1107/S0907444909045715
    • NLM

      Pereira H d'M, Rezende MM, Castilho MS, Oliva G, Garratt RC. Adenosine binding to low-molecular-weight purine nucleoside phosphorylase: the structural basis for recognition based on its complex with the enzyme from Schistosoma mansoni [Internet]. Acta Crystallographica D. 2010 ; 66( Ja 2010): 73-79.[citado 2024 set. 07 ] Available from: https://doi.org/10.1107/S0907444909045715
    • Vancouver

      Pereira H d'M, Rezende MM, Castilho MS, Oliva G, Garratt RC. Adenosine binding to low-molecular-weight purine nucleoside phosphorylase: the structural basis for recognition based on its complex with the enzyme from Schistosoma mansoni [Internet]. Acta Crystallographica D. 2010 ; 66( Ja 2010): 73-79.[citado 2024 set. 07 ] Available from: https://doi.org/10.1107/S0907444909045715
  • Source: Acta Crystallographica D. Unidade: IFSC

    Subjects: CRISTALOGRAFIA, ENZIMAS, LEISHMANIA MEXICANA, PROTEÍNAS

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    • ABNT

      CORDEIRO, Artur T. et al. Leishmania mexicana mexicana glucose-6-phosphate isomerase: crystallization, molecular-replacement solution and inhibition. Acta Crystallographica D, v. 60, p. 915-919, 2004Tradução . . Disponível em: https://doi.org/10.1107/s0907444904003762. Acesso em: 07 set. 2024.
    • APA

      Cordeiro, A. T., Hardré, R., Michels, P. A. M., Salmon, L., Delboni, L. F., & Thiemann, O. H. (2004). Leishmania mexicana mexicana glucose-6-phosphate isomerase: crystallization, molecular-replacement solution and inhibition. Acta Crystallographica D, 60, 915-919. doi:10.1107/s0907444904003762
    • NLM

      Cordeiro AT, Hardré R, Michels PAM, Salmon L, Delboni LF, Thiemann OH. Leishmania mexicana mexicana glucose-6-phosphate isomerase: crystallization, molecular-replacement solution and inhibition [Internet]. Acta Crystallographica D. 2004 ; 60 915-919.[citado 2024 set. 07 ] Available from: https://doi.org/10.1107/s0907444904003762
    • Vancouver

      Cordeiro AT, Hardré R, Michels PAM, Salmon L, Delboni LF, Thiemann OH. Leishmania mexicana mexicana glucose-6-phosphate isomerase: crystallization, molecular-replacement solution and inhibition [Internet]. Acta Crystallographica D. 2004 ; 60 915-919.[citado 2024 set. 07 ] Available from: https://doi.org/10.1107/s0907444904003762
  • Source: Acta Crystallographica D. Unidade: IFSC

    Subjects: ENZIMAS, BIOFÍSICA, CRISTALOGRAFIA, GENES, SCHISTOSOMA MANSONI, MUTAÇÃO

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    • ABNT

      CARDOSO, Rosa M. F. et al. Structure of the cytosolic Cu,Zn superoxide dismutase from Schistosoma mansoni. Acta Crystallographica D, v. 60, p. Se 2004, 2004Tradução . . Disponível em: https://doi.org/10.1107/s0907444904016798. Acesso em: 07 set. 2024.
    • APA

      Cardoso, R. M. F., Silva, C. H. T. P., Araújo, A. P. U. de, Tanaka, T., Tanaka, M., & Garratt, R. C. (2004). Structure of the cytosolic Cu,Zn superoxide dismutase from Schistosoma mansoni. Acta Crystallographica D, 60, Se 2004. doi:10.1107/s0907444904016798
    • NLM

      Cardoso RMF, Silva CHTP, Araújo APU de, Tanaka T, Tanaka M, Garratt RC. Structure of the cytosolic Cu,Zn superoxide dismutase from Schistosoma mansoni [Internet]. Acta Crystallographica D. 2004 ; 60 Se 2004.[citado 2024 set. 07 ] Available from: https://doi.org/10.1107/s0907444904016798
    • Vancouver

      Cardoso RMF, Silva CHTP, Araújo APU de, Tanaka T, Tanaka M, Garratt RC. Structure of the cytosolic Cu,Zn superoxide dismutase from Schistosoma mansoni [Internet]. Acta Crystallographica D. 2004 ; 60 Se 2004.[citado 2024 set. 07 ] Available from: https://doi.org/10.1107/s0907444904016798
  • 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: 07 set. 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 set. 07 ] 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 set. 07 ] Available from: https://doi.org/10.1107/s0907444902021467
  • Source: Acta Crystallographica D. Unidades: FCF, IFSC

    Subjects: CRISTALOGRAFIA, ENZIMAS

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    • ABNT

      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: 07 set. 2024.
    • APA

      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 set. 07 ] 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 set. 07 ] Available from: https://doi.org/10.1107/s0907444902021200
  • Source: Acta Crystallographica D. Unidade: IFSC

    Subjects: CRISTALOGRAFIA, ENZIMAS

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    • ABNT

      LEE, Wen-Hwa et al. Comparison of different crystal forms of 3-dehydroquinase from Salmonella typhi and its implication for the enzyme activity. Acta Crystallographica D, v. 58, p. 798-804, 2002Tradução . . Disponível em: https://doi.org/10.1107/s0907444902003918. Acesso em: 07 set. 2024.
    • APA

      Lee, W. -H., Perles, L. A., Nagem, R. A. P., Shrive, A. K., Hawkins, A., Sawyer, L., & Polikarpov, I. (2002). Comparison of different crystal forms of 3-dehydroquinase from Salmonella typhi and its implication for the enzyme activity. Acta Crystallographica D, 58, 798-804. doi:10.1107/s0907444902003918
    • NLM

      Lee W-H, Perles LA, Nagem RAP, Shrive AK, Hawkins A, Sawyer L, Polikarpov I. Comparison of different crystal forms of 3-dehydroquinase from Salmonella typhi and its implication for the enzyme activity [Internet]. Acta Crystallographica D. 2002 ; 58 798-804.[citado 2024 set. 07 ] Available from: https://doi.org/10.1107/s0907444902003918
    • Vancouver

      Lee W-H, Perles LA, Nagem RAP, Shrive AK, Hawkins A, Sawyer L, Polikarpov I. Comparison of different crystal forms of 3-dehydroquinase from Salmonella typhi and its implication for the enzyme activity [Internet]. Acta Crystallographica D. 2002 ; 58 798-804.[citado 2024 set. 07 ] Available from: https://doi.org/10.1107/s0907444902003918

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