Filtros : "Journal of Structural Biology" Removido: "Furtado, Adriano Alves" Limpar

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  • Source: Journal of Structural Biology. Unidade: ICB

    Subjects: MICROBIOLOGIA, CITOPLASMA, MYCOBACTERIUM TUBERCULOSIS, AMINOÁCIDOS, CATÁLISE, ATIVAÇÃO ENZIMÁTICA, RESISTÊNCIA MICROBIANA ÀS DROGAS, ANTIBIOTICOS

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      ROSSINI, Nicolas de Oliveira e SILVA, Catharina e DIAS, Marcio Vinicius Bertacine. The crystal structure of Mycobacterium thermoresistibile MurE ligase reveals the binding mode of the substrate m-diaminopimelate. Journal of Structural Biology, v. 215, n. 2, p. 1-10, 2023Tradução . . Disponível em: https://doi.org/10.1016/j.jsb.2023.107957. Acesso em: 07 out. 2025.
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      Rossini, N. de O., Silva, C., & Dias, M. V. B. (2023). The crystal structure of Mycobacterium thermoresistibile MurE ligase reveals the binding mode of the substrate m-diaminopimelate. Journal of Structural Biology, 215( 2), 1-10. doi:10.1016/j.jsb.2023.107957
    • NLM

      Rossini N de O, Silva C, Dias MVB. The crystal structure of Mycobacterium thermoresistibile MurE ligase reveals the binding mode of the substrate m-diaminopimelate [Internet]. Journal of Structural Biology. 2023 ; 215( 2): 1-10.[citado 2025 out. 07 ] Available from: https://doi.org/10.1016/j.jsb.2023.107957
    • Vancouver

      Rossini N de O, Silva C, Dias MVB. The crystal structure of Mycobacterium thermoresistibile MurE ligase reveals the binding mode of the substrate m-diaminopimelate [Internet]. Journal of Structural Biology. 2023 ; 215( 2): 1-10.[citado 2025 out. 07 ] Available from: https://doi.org/10.1016/j.jsb.2023.107957
  • Source: Journal of Structural Biology. Unidade: IFSC

    Subjects: CRISTALOGRAFIA, PROTEÍNAS, POLIMERIZAÇÃO

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      SILVA, Rafael Marques da et al. A key piece of the puzzle: the central tetramer of the Saccharomyces cerevisiae septin protofilament and its implications for self-assembly. Journal of Structural Biology, v. 215, n. 3, p. 107983-1-107983-13 + supplementary data: 1-3, 2023Tradução . . Disponível em: https://doi.org/10.1016/j.jsb.2023.107983. Acesso em: 07 out. 2025.
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      Silva, R. M. da, Saladino, G. C. dos R., Cabrejos, D. A. L., Pereira, H. d'M., Sculaccio, S. A., Araújo, A. P. U. de, & Garratt, R. C. (2023). A key piece of the puzzle: the central tetramer of the Saccharomyces cerevisiae septin protofilament and its implications for self-assembly. Journal of Structural Biology, 215( 3), 107983-1-107983-13 + supplementary data: 1-3. doi:10.1016/j.jsb.2023.107983
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      Silva RM da, Saladino GC dos R, Cabrejos DAL, Pereira H d'M, Sculaccio SA, Araújo APU de, Garratt RC. A key piece of the puzzle: the central tetramer of the Saccharomyces cerevisiae septin protofilament and its implications for self-assembly [Internet]. Journal of Structural Biology. 2023 ; 215( 3): 107983-1-107983-13 + supplementary data: 1-3.[citado 2025 out. 07 ] Available from: https://doi.org/10.1016/j.jsb.2023.107983
    • Vancouver

      Silva RM da, Saladino GC dos R, Cabrejos DAL, Pereira H d'M, Sculaccio SA, Araújo APU de, Garratt RC. A key piece of the puzzle: the central tetramer of the Saccharomyces cerevisiae septin protofilament and its implications for self-assembly [Internet]. Journal of Structural Biology. 2023 ; 215( 3): 107983-1-107983-13 + supplementary data: 1-3.[citado 2025 out. 07 ] Available from: https://doi.org/10.1016/j.jsb.2023.107983
  • Source: Journal of Structural Biology. Unidades: IFSC, EACH

    Subjects: CRISTALOGRAFIA, SUPERÓXIDO DISMUTASE, TRICHODERMA

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      RENGIFO, Emérita Mendoza et al. Unexpected plasticity of the quaternary structure of iron-manganese superoxide dismutases. Journal of Structural Biology, v. 214, n. 2, p. 107855-1-107855-11, 2022Tradução . . Disponível em: https://doi.org/10.1016/j.jsb.2022.107855. Acesso em: 07 out. 2025.
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      Rengifo, E. M., Fontolan, L. S. B., Ferreira Junior, J. R. dos S., Bleicher, L., Penner-Hahn, J. E., & Garratt, R. C. (2022). Unexpected plasticity of the quaternary structure of iron-manganese superoxide dismutases. Journal of Structural Biology, 214( 2), 107855-1-107855-11. doi:10.1016/j.jsb.2022.107855
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      Rengifo EM, Fontolan LSB, Ferreira Junior JR dos S, Bleicher L, Penner-Hahn JE, Garratt RC. Unexpected plasticity of the quaternary structure of iron-manganese superoxide dismutases [Internet]. Journal of Structural Biology. 2022 ; 214( 2): 107855-1-107855-11.[citado 2025 out. 07 ] Available from: https://doi.org/10.1016/j.jsb.2022.107855
    • Vancouver

      Rengifo EM, Fontolan LSB, Ferreira Junior JR dos S, Bleicher L, Penner-Hahn JE, Garratt RC. Unexpected plasticity of the quaternary structure of iron-manganese superoxide dismutases [Internet]. Journal of Structural Biology. 2022 ; 214( 2): 107855-1-107855-11.[citado 2025 out. 07 ] Available from: https://doi.org/10.1016/j.jsb.2022.107855
  • Source: Journal of Structural Biology. Unidades: FCF, IQ

    Subjects: PROTEÍNAS, AMINOÁCIDOS, RESSONÂNCIA MAGNÉTICA NUCLEAR, CENTRALIDADE

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      ALMEIDA, Vitor Medeiros et al. Role of a high centrality residue in protein dynamics and thermal stability. Journal of Structural Biology, v. 213, n. 3, p. 1-11 art. 107773, 2021Tradução . . Disponível em: https://doi.org/10.1016/j.jsb.2021.107773. Acesso em: 07 out. 2025.
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      Almeida, V. M., Chaudhuri, A., Cardoso, M. V. C., Matsuyama, B. Y., Ferreira, G. M., Trossini, G. H. G., et al. (2021). Role of a high centrality residue in protein dynamics and thermal stability. Journal of Structural Biology, 213( 3), 1-11 art. 107773. doi:10.1016/j.jsb.2021.107773
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      Almeida VM, Chaudhuri A, Cardoso MVC, Matsuyama BY, Ferreira GM, Trossini GHG, Salinas RK, Loria JP, Marana SR. Role of a high centrality residue in protein dynamics and thermal stability [Internet]. Journal of Structural Biology. 2021 ; 213( 3): 1-11 art. 107773.[citado 2025 out. 07 ] Available from: https://doi.org/10.1016/j.jsb.2021.107773
    • Vancouver

      Almeida VM, Chaudhuri A, Cardoso MVC, Matsuyama BY, Ferreira GM, Trossini GHG, Salinas RK, Loria JP, Marana SR. Role of a high centrality residue in protein dynamics and thermal stability [Internet]. Journal of Structural Biology. 2021 ; 213( 3): 1-11 art. 107773.[citado 2025 out. 07 ] Available from: https://doi.org/10.1016/j.jsb.2021.107773
  • Source: Journal of Structural Biology. Unidade: FFCLRP

    Subjects: FOSFATOS, CÁLCIO, BIOMINERALIZAÇÃO, ESPECTROSCOPIA, INFRAVERMELHO

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      CRUZ, Marcos Antônio Eufrasio et al. Phosphatidylserine controls calcium phosphate nucleation and growth on lipid monolayers: a physicochemical understanding of matrix vesicle-driven biomineralization. Journal of Structural Biology, v. 212, n. 2, 2020Tradução . . Disponível em: https://doi.org/10.1016/j.jsb.2020.107607. Acesso em: 07 out. 2025.
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      Cruz, M. A. E., Ferreira, C. dos R., Tovani, C. B., Oliveira, F. A. de, Bolean, M., Caseli, L., et al. (2020). Phosphatidylserine controls calcium phosphate nucleation and growth on lipid monolayers: a physicochemical understanding of matrix vesicle-driven biomineralization. Journal of Structural Biology, 212( 2). doi:10.1016/j.jsb.2020.107607
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      Cruz MAE, Ferreira C dos R, Tovani CB, Oliveira FA de, Bolean M, Caseli L, Mebarek S, Millán JL, Buchet R, Bottini M, Ciancaglini P, Ramos AP. Phosphatidylserine controls calcium phosphate nucleation and growth on lipid monolayers: a physicochemical understanding of matrix vesicle-driven biomineralization [Internet]. Journal of Structural Biology. 2020 ; 212( 2):[citado 2025 out. 07 ] Available from: https://doi.org/10.1016/j.jsb.2020.107607
    • Vancouver

      Cruz MAE, Ferreira C dos R, Tovani CB, Oliveira FA de, Bolean M, Caseli L, Mebarek S, Millán JL, Buchet R, Bottini M, Ciancaglini P, Ramos AP. Phosphatidylserine controls calcium phosphate nucleation and growth on lipid monolayers: a physicochemical understanding of matrix vesicle-driven biomineralization [Internet]. Journal of Structural Biology. 2020 ; 212( 2):[citado 2025 out. 07 ] Available from: https://doi.org/10.1016/j.jsb.2020.107607
  • Source: Journal of Structural Biology. Unidade: IFSC

    Subjects: CRISTALOGRAFIA, BIOFÍSICA, PROTEÍNAS

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      BROGNARA, Gabriel et al. Revisiting SEPT7 and the slippage of β-strands in the septin family. Journal of Structural Biology, v. 207, n. 1, p. 67-73, 2019Tradução . . Disponível em: https://doi.org/10.1016/j.jsb.2019.04.015. Acesso em: 07 out. 2025.
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      Brognara, G., Pereira, H. d'M., Brandão-Neto, J., Araújo, A. P. U. de, & Garratt, R. C. (2019). Revisiting SEPT7 and the slippage of β-strands in the septin family. Journal of Structural Biology, 207( 1), 67-73. doi:10.1016/j.jsb.2019.04.015
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      Brognara G, Pereira H d'M, Brandão-Neto J, Araújo APU de, Garratt RC. Revisiting SEPT7 and the slippage of β-strands in the septin family [Internet]. Journal of Structural Biology. 2019 ; 207( 1): 67-73.[citado 2025 out. 07 ] Available from: https://doi.org/10.1016/j.jsb.2019.04.015
    • Vancouver

      Brognara G, Pereira H d'M, Brandão-Neto J, Araújo APU de, Garratt RC. Revisiting SEPT7 and the slippage of β-strands in the septin family [Internet]. Journal of Structural Biology. 2019 ; 207( 1): 67-73.[citado 2025 out. 07 ] Available from: https://doi.org/10.1016/j.jsb.2019.04.015
  • Source: Journal of Structural Biology. Unidade: IFSC

    Subjects: STAPHYLOCOCCUS, ENZIMAS, PROTEÍNAS (ESTUDO), BACTÉRIAS

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      AZEVEDO, Érika Chang de e NASCIMENTO, Alessandro Silva. Energy landscape of the domain movement in Staphylococcus aureus UDP-Nacetylglucosamine 2-epimerase. Journal of Structural Biology, v. 207, n. 2, p. 158-168, 2019Tradução . . Disponível em: https://doi.org/10.1016/j.jsb.2019.05.004. Acesso em: 07 out. 2025.
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      Azevedo, É. C. de, & Nascimento, A. S. (2019). Energy landscape of the domain movement in Staphylococcus aureus UDP-Nacetylglucosamine 2-epimerase. Journal of Structural Biology, 207( 2), 158-168. doi:10.1016/j.jsb.2019.05.004
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      Azevedo ÉC de, Nascimento AS. Energy landscape of the domain movement in Staphylococcus aureus UDP-Nacetylglucosamine 2-epimerase [Internet]. Journal of Structural Biology. 2019 ; 207( 2): 158-168.[citado 2025 out. 07 ] Available from: https://doi.org/10.1016/j.jsb.2019.05.004
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      Azevedo ÉC de, Nascimento AS. Energy landscape of the domain movement in Staphylococcus aureus UDP-Nacetylglucosamine 2-epimerase [Internet]. Journal of Structural Biology. 2019 ; 207( 2): 158-168.[citado 2025 out. 07 ] Available from: https://doi.org/10.1016/j.jsb.2019.05.004
  • Source: Journal of Structural Biology. Unidade: FFCLRP

    Subjects: LEISHMANIA, NUCLEOSÍDEOS, PROTEÍNAS QUINASES

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      VIEIRA, Plínio Salmazo et al. The role of the C-terminus and Kpn loop in the quaternary structure stability of nucleoside diphosphate kinase from Leishmania parasites. Journal of Structural Biology, v. 192, n. 3, p. 336-341, 2015Tradução . . Disponível em: https://doi.org/10.1016/j.jsb.2015.09.009. Acesso em: 07 out. 2025.
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      Vieira, P. S., Giuseppe, P. O. de, Oliveira, A. H. C. de, & Murakami, M. T. (2015). The role of the C-terminus and Kpn loop in the quaternary structure stability of nucleoside diphosphate kinase from Leishmania parasites. Journal of Structural Biology, 192( 3), 336-341. doi:10.1016/j.jsb.2015.09.009
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      Vieira PS, Giuseppe PO de, Oliveira AHC de, Murakami MT. The role of the C-terminus and Kpn loop in the quaternary structure stability of nucleoside diphosphate kinase from Leishmania parasites [Internet]. Journal of Structural Biology. 2015 ; 192( 3): 336-341.[citado 2025 out. 07 ] Available from: https://doi.org/10.1016/j.jsb.2015.09.009
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      Vieira PS, Giuseppe PO de, Oliveira AHC de, Murakami MT. The role of the C-terminus and Kpn loop in the quaternary structure stability of nucleoside diphosphate kinase from Leishmania parasites [Internet]. Journal of Structural Biology. 2015 ; 192( 3): 336-341.[citado 2025 out. 07 ] Available from: https://doi.org/10.1016/j.jsb.2015.09.009
  • Source: Journal of Structural Biology. Unidade: IFSC

    Subjects: RECEPTORES, INSULINA, CRISTALOGRAFIA FÍSICA (ESTRUTURA)

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      SANTOS, Jademilson Celestino dos et al. Different binding and recognition modes of GL479, a dual agonist of peroxisome proliferator-activated receptor α/γ. Journal of Structural Biology, v. 191, n. 3, p. 332-340, 2015Tradução . . Disponível em: https://doi.org/10.1016/j.jsb.2015.07.006. Acesso em: 07 out. 2025.
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      Santos, J. C. dos, Bernardes, A., Giampietro, L., Ammazzalorso, A., De Filippis, B., Amoroso, R., & Polikarpov, I. (2015). Different binding and recognition modes of GL479, a dual agonist of peroxisome proliferator-activated receptor α/γ. Journal of Structural Biology, 191( 3), 332-340. doi:10.1016/j.jsb.2015.07.006
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      Santos JC dos, Bernardes A, Giampietro L, Ammazzalorso A, De Filippis B, Amoroso R, Polikarpov I. Different binding and recognition modes of GL479, a dual agonist of peroxisome proliferator-activated receptor α/γ [Internet]. Journal of Structural Biology. 2015 ; 191( 3): 332-340.[citado 2025 out. 07 ] Available from: https://doi.org/10.1016/j.jsb.2015.07.006
    • Vancouver

      Santos JC dos, Bernardes A, Giampietro L, Ammazzalorso A, De Filippis B, Amoroso R, Polikarpov I. Different binding and recognition modes of GL479, a dual agonist of peroxisome proliferator-activated receptor α/γ [Internet]. Journal of Structural Biology. 2015 ; 191( 3): 332-340.[citado 2025 out. 07 ] Available from: https://doi.org/10.1016/j.jsb.2015.07.006
  • Source: Journal of Structural Biology. Unidade: IFSC

    Subjects: FLAVONÓIDES, PRODUTOS NATURAIS

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      TRIVELLA, Daniela B. B. et al. Flavonoid interactions with human transthyretin: combined structural and thermodynamic analysis. Journal of Structural Biology, v. 180, n. 1, p. 143-153, 2012Tradução . . Disponível em: https://doi.org/10.1016/j.jsb.2012.07.008. Acesso em: 07 out. 2025.
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      Trivella, D. B. B., Reis, C. V., Lima, L. M. T. R., Foguel, D., & Polikarpov, I. (2012). Flavonoid interactions with human transthyretin: combined structural and thermodynamic analysis. Journal of Structural Biology, 180( 1), 143-153. doi:10.1016/j.jsb.2012.07.008
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      Trivella DBB, Reis CV, Lima LMTR, Foguel D, Polikarpov I. Flavonoid interactions with human transthyretin: combined structural and thermodynamic analysis [Internet]. Journal of Structural Biology. 2012 ; 180( 1): 143-153.[citado 2025 out. 07 ] Available from: https://doi.org/10.1016/j.jsb.2012.07.008
    • Vancouver

      Trivella DBB, Reis CV, Lima LMTR, Foguel D, Polikarpov I. Flavonoid interactions with human transthyretin: combined structural and thermodynamic analysis [Internet]. Journal of Structural Biology. 2012 ; 180( 1): 143-153.[citado 2025 out. 07 ] Available from: https://doi.org/10.1016/j.jsb.2012.07.008
  • Source: Journal of Structural Biology. Unidade: IFSC

    Subjects: CRISTALOGRAFIA, HORMÔNIOS TIREOIDIANOS, RECEPTORES

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      TRIVELLA, Daniela B. B. et al. The binding of synthetic triiodo L-thyronine analogs to human transthyretin: Molecular basis of cooperative and non-cooperative ligand recognition. Journal of Structural Biology, v. 173, n. 2, p. 323-332, 2011Tradução . . Disponível em: https://doi.org/10.1016/j.jsb.2010.10.003. Acesso em: 07 out. 2025.
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      Trivella, D. B. B., Sairre, M. I., Foguel, D., Lima, L. M. T. R., & Polikarpov, I. (2011). The binding of synthetic triiodo L-thyronine analogs to human transthyretin: Molecular basis of cooperative and non-cooperative ligand recognition. Journal of Structural Biology, 173( 2), 323-332. doi:10.1016/j.jsb.2010.10.003
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      Trivella DBB, Sairre MI, Foguel D, Lima LMTR, Polikarpov I. The binding of synthetic triiodo L-thyronine analogs to human transthyretin: Molecular basis of cooperative and non-cooperative ligand recognition [Internet]. Journal of Structural Biology. 2011 ; 173( 2): 323-332.[citado 2025 out. 07 ] Available from: https://doi.org/10.1016/j.jsb.2010.10.003
    • Vancouver

      Trivella DBB, Sairre MI, Foguel D, Lima LMTR, Polikarpov I. The binding of synthetic triiodo L-thyronine analogs to human transthyretin: Molecular basis of cooperative and non-cooperative ligand recognition [Internet]. Journal of Structural Biology. 2011 ; 173( 2): 323-332.[citado 2025 out. 07 ] Available from: https://doi.org/10.1016/j.jsb.2010.10.003
  • Source: Journal of Structural Biology. Unidade: FCFRP

    Subjects: FOSFOLIPASES A, CRISTALOGRAFIA DE RAIOS X, VENENOS DE ORIGEM ANIMAL

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      FERNANDES, Carlos A. H. et al. Comparison between apo and complexed structures of bothropstoxin-I reveals the role Lys122 and 'Ca POT.2+'- binding loop region for the catalytically inactive Lys49-PL'A IND.2'S. Journal of Structural Biology, v. 171, n. 1, p. 31-43, 2010Tradução . . Acesso em: 07 out. 2025.
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      Fernandes, C. A. H., Marchi-Salvador, D. P., Marchi-Salvador, D. P., Salvador, G. M., Silva, M. C. O., Costa, T. R., et al. (2010). Comparison between apo and complexed structures of bothropstoxin-I reveals the role Lys122 and 'Ca POT.2+'- binding loop region for the catalytically inactive Lys49-PL'A IND.2'S. Journal of Structural Biology, 171( 1), 31-43.
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      Fernandes CAH, Marchi-Salvador DP, Marchi-Salvador DP, Salvador GM, Silva MCO, Costa TR, Soares AM, Fontes MRM. Comparison between apo and complexed structures of bothropstoxin-I reveals the role Lys122 and 'Ca POT.2+'- binding loop region for the catalytically inactive Lys49-PL'A IND.2'S. Journal of Structural Biology. 2010 ; 171( 1): 31-43.[citado 2025 out. 07 ]
    • Vancouver

      Fernandes CAH, Marchi-Salvador DP, Marchi-Salvador DP, Salvador GM, Silva MCO, Costa TR, Soares AM, Fontes MRM. Comparison between apo and complexed structures of bothropstoxin-I reveals the role Lys122 and 'Ca POT.2+'- binding loop region for the catalytically inactive Lys49-PL'A IND.2'S. Journal of Structural Biology. 2010 ; 171( 1): 31-43.[citado 2025 out. 07 ]
  • Source: Journal of Structural Biology. Unidades: IQSC, IFSC

    Subjects: CRISTALOGRAFIA (ESTRUTURA), SOJA (ENZIMOLOGIA), PROTEÍNAS (ESTUDO), AMILOIDOSE (ESTUDO;TRATAMENTO)

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      TRIVELLA, Daniela B. B. et al. Conformational differences between the wild type and V30M mutant transthyretin modulate its binding to genistein: implications to tetramer stability and ligand-binding. Journal of Structural Biology, v. 170, n. 3, p. 522-531, 2010Tradução . . Disponível em: https://doi.org/10.1016/j.jsb.2010.03.002. Acesso em: 07 out. 2025.
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      Trivella, D. B. B., Bleicher, L., Palmieri, L. de C., Wiggers, H. J., Montanari, C. A., Kelly, J. W., et al. (2010). Conformational differences between the wild type and V30M mutant transthyretin modulate its binding to genistein: implications to tetramer stability and ligand-binding. Journal of Structural Biology, 170( 3), 522-531. doi:10.1016/j.jsb.2010.03.002
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      Trivella DBB, Bleicher L, Palmieri L de C, Wiggers HJ, Montanari CA, Kelly JW, Lima LMTR, Foguel D, Polikarpov I. Conformational differences between the wild type and V30M mutant transthyretin modulate its binding to genistein: implications to tetramer stability and ligand-binding [Internet]. Journal of Structural Biology. 2010 ; 170( 3): 522-531.[citado 2025 out. 07 ] Available from: https://doi.org/10.1016/j.jsb.2010.03.002
    • Vancouver

      Trivella DBB, Bleicher L, Palmieri L de C, Wiggers HJ, Montanari CA, Kelly JW, Lima LMTR, Foguel D, Polikarpov I. Conformational differences between the wild type and V30M mutant transthyretin modulate its binding to genistein: implications to tetramer stability and ligand-binding [Internet]. Journal of Structural Biology. 2010 ; 170( 3): 522-531.[citado 2025 out. 07 ] Available from: https://doi.org/10.1016/j.jsb.2010.03.002
  • Source: Journal of Structural Biology. Unidade: IFSC

    Subjects: CRISTALOGRAFIA FÍSICA (ESTRUTURA), PEROXIDASE, SENSORES BIOMÉDICOS, BIOLOGIA MOLECULAR VEGETAL

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      WATANABE, Leandra et al. Crystal structure and statistical coupling analysis of highly glycosylated peroxidase from royal palm tree (Roystonea regia). Journal of Structural Biology, v. 169, n. 2, p. 226-242, 2010Tradução . . Disponível em: https://doi.org/10.1016/j.jsb.2009.10.009. Acesso em: 07 out. 2025.
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      Watanabe, L., Moura, P. R. de, Bleicher, L., Nascimento, A. S., Zamorano, L. S., Calvete, J. J., et al. (2010). Crystal structure and statistical coupling analysis of highly glycosylated peroxidase from royal palm tree (Roystonea regia). Journal of Structural Biology, 169( 2), 226-242. doi:10.1016/j.jsb.2009.10.009
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      Watanabe L, Moura PR de, Bleicher L, Nascimento AS, Zamorano LS, Calvete JJ, Sanz L, Pérez A, Bursakov S, Roig MG, Shnyrov VL, Polikarpov I. Crystal structure and statistical coupling analysis of highly glycosylated peroxidase from royal palm tree (Roystonea regia) [Internet]. Journal of Structural Biology. 2010 ; 169( 2): 226-242.[citado 2025 out. 07 ] Available from: https://doi.org/10.1016/j.jsb.2009.10.009
    • Vancouver

      Watanabe L, Moura PR de, Bleicher L, Nascimento AS, Zamorano LS, Calvete JJ, Sanz L, Pérez A, Bursakov S, Roig MG, Shnyrov VL, Polikarpov I. Crystal structure and statistical coupling analysis of highly glycosylated peroxidase from royal palm tree (Roystonea regia) [Internet]. Journal of Structural Biology. 2010 ; 169( 2): 226-242.[citado 2025 out. 07 ] Available from: https://doi.org/10.1016/j.jsb.2009.10.009
  • Source: Journal of Structural Biology. Unidade: IQ

    Subjects: XANTHOMONAS, CANCRO (DOENÇA DE PLANTA)

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      GALLO, Mariana et al. A new member of the ribbon-helix-helix transcription factor superfamily from the plant pathogen Xanthomonas axonopodis pv. citri. Journal of Structural Biology, v. 170, n. 1, p. 21-31, 2010Tradução . . Disponível em: https://doi.org/10.1016/j.jsb.2009.12.022. Acesso em: 07 out. 2025.
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      Gallo, M., Ferrari, E., Eliseo, T., Amata, I., Pertinhez, T. A., Katsuyama, A. M., et al. (2010). A new member of the ribbon-helix-helix transcription factor superfamily from the plant pathogen Xanthomonas axonopodis pv. citri. Journal of Structural Biology, 170( 1), 21-31. doi:10.1016/j.jsb.2009.12.022
    • NLM

      Gallo M, Ferrari E, Eliseo T, Amata I, Pertinhez TA, Katsuyama AM, Paci M, Farah CS, Spisni A, Cicero DO. A new member of the ribbon-helix-helix transcription factor superfamily from the plant pathogen Xanthomonas axonopodis pv. citri [Internet]. Journal of Structural Biology. 2010 ; 170( 1): 21-31.[citado 2025 out. 07 ] Available from: https://doi.org/10.1016/j.jsb.2009.12.022
    • Vancouver

      Gallo M, Ferrari E, Eliseo T, Amata I, Pertinhez TA, Katsuyama AM, Paci M, Farah CS, Spisni A, Cicero DO. A new member of the ribbon-helix-helix transcription factor superfamily from the plant pathogen Xanthomonas axonopodis pv. citri [Internet]. Journal of Structural Biology. 2010 ; 170( 1): 21-31.[citado 2025 out. 07 ] Available from: https://doi.org/10.1016/j.jsb.2009.12.022
  • Source: Journal of Structural Biology. Unidade: ICB

    Assunto: HISTOLOGIA

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      MORISCOT, Anselmo Sigari et al. MuRF1 is a muscle fiber-type II associated factor and together with MuRF2 regulates type-II fiber trophicity and maintenance. Journal of Structural Biology, v. 170, n. 2, p. 344-353, 2010Tradução . . Disponível em: https://doi.org/10.1016/j.jsb.2010.02.001. Acesso em: 07 out. 2025.
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      Moriscot, A. S., Baptista, I. L., Bogomolovas, J., Witt, C., Hirner, S., Granzier, H., & Labeit, S. (2010). MuRF1 is a muscle fiber-type II associated factor and together with MuRF2 regulates type-II fiber trophicity and maintenance. Journal of Structural Biology, 170( 2), 344-353. doi:10.1016/j.jsb.2010.02.001
    • NLM

      Moriscot AS, Baptista IL, Bogomolovas J, Witt C, Hirner S, Granzier H, Labeit S. MuRF1 is a muscle fiber-type II associated factor and together with MuRF2 regulates type-II fiber trophicity and maintenance [Internet]. Journal of Structural Biology. 2010 ; 170( 2): 344-353.[citado 2025 out. 07 ] Available from: https://doi.org/10.1016/j.jsb.2010.02.001
    • Vancouver

      Moriscot AS, Baptista IL, Bogomolovas J, Witt C, Hirner S, Granzier H, Labeit S. MuRF1 is a muscle fiber-type II associated factor and together with MuRF2 regulates type-II fiber trophicity and maintenance [Internet]. Journal of Structural Biology. 2010 ; 170( 2): 344-353.[citado 2025 out. 07 ] Available from: https://doi.org/10.1016/j.jsb.2010.02.001
  • Source: Journal of Structural Biology. Unidade: FCFRP

    Subjects: CRISTALOGRAFIA DE RAIOS X, FOSFOLIPASES A, VENENOS DE ORIGEM ANIMAL

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      SANTOS, Juliana I. dos e SOARES, Andreimar Martins e FONTES, Marcos R. M. Comparative structural studies on Lys49-phosphopipases 'A IND.2' from Bothrops genus reveal their myotoxic site. Journal of Structural Biology, v. 167, n. 2, p. 106-116, 2009Tradução . . Disponível em: https://doi.org/10.1016/j.jsb.2009.04.003. Acesso em: 07 out. 2025.
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      Santos, J. I. dos, Soares, A. M., & Fontes, M. R. M. (2009). Comparative structural studies on Lys49-phosphopipases 'A IND.2' from Bothrops genus reveal their myotoxic site. Journal of Structural Biology, 167( 2), 106-116. doi:10.1016/j.jsb.2009.04.003
    • NLM

      Santos JI dos, Soares AM, Fontes MRM. Comparative structural studies on Lys49-phosphopipases 'A IND.2' from Bothrops genus reveal their myotoxic site [Internet]. Journal of Structural Biology. 2009 ; 167( 2): 106-116.[citado 2025 out. 07 ] Available from: https://doi.org/10.1016/j.jsb.2009.04.003
    • Vancouver

      Santos JI dos, Soares AM, Fontes MRM. Comparative structural studies on Lys49-phosphopipases 'A IND.2' from Bothrops genus reveal their myotoxic site [Internet]. Journal of Structural Biology. 2009 ; 167( 2): 106-116.[citado 2025 out. 07 ] Available from: https://doi.org/10.1016/j.jsb.2009.04.003
  • Source: Journal of Structural Biology. Unidade: IQ

    Subjects: LISOZIMAS, BIOQUÍMICA

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    • ABNT

      CANÇADO, Fabiane Chaves et al. The crystal structure of a lysozyme c from housefly Musca domestica, the first structure of a digestive lysozyme. Journal of Structural Biology, v. 160, n. 1, p. 83-92, 2007Tradução . . Disponível em: https://doi.org/10.1016/j.jsb.2007.07.008. Acesso em: 07 out. 2025.
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      Cançado, F. C., Valério, A. A., Marana, S. R., & Barbosa, J. A. R. G. (2007). The crystal structure of a lysozyme c from housefly Musca domestica, the first structure of a digestive lysozyme. Journal of Structural Biology, 160( 1), 83-92. doi:10.1016/j.jsb.2007.07.008
    • NLM

      Cançado FC, Valério AA, Marana SR, Barbosa JARG. The crystal structure of a lysozyme c from housefly Musca domestica, the first structure of a digestive lysozyme [Internet]. Journal of Structural Biology. 2007 ; 160( 1): 83-92.[citado 2025 out. 07 ] Available from: https://doi.org/10.1016/j.jsb.2007.07.008
    • Vancouver

      Cançado FC, Valério AA, Marana SR, Barbosa JARG. The crystal structure of a lysozyme c from housefly Musca domestica, the first structure of a digestive lysozyme [Internet]. Journal of Structural Biology. 2007 ; 160( 1): 83-92.[citado 2025 out. 07 ] Available from: https://doi.org/10.1016/j.jsb.2007.07.008
  • Source: Journal of Structural Biology. Unidade: IB

    Assunto: FISIOLOGIA ANIMAL

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      GARCIA, Célia Regina da Silva. Imaging Plasmodium fasciparium-infested ghost and parasite by atomic force microscopy. Journal of Structural Biology, v. 119, p. 92-98, 1997Tradução . . Acesso em: 07 out. 2025.
    • APA

      Garcia, C. R. da S. (1997). Imaging Plasmodium fasciparium-infested ghost and parasite by atomic force microscopy. Journal of Structural Biology, 119, 92-98.
    • NLM

      Garcia CR da S. Imaging Plasmodium fasciparium-infested ghost and parasite by atomic force microscopy. Journal of Structural Biology. 1997 ; 119 92-98.[citado 2025 out. 07 ]
    • Vancouver

      Garcia CR da S. Imaging Plasmodium fasciparium-infested ghost and parasite by atomic force microscopy. Journal of Structural Biology. 1997 ; 119 92-98.[citado 2025 out. 07 ]
  • Source: Journal of Structural Biology. Unidade: ICB

    Assunto: HISTOLOGIA

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      ZORN, T M T e OLIVEIRA, S. F. e ABRAHAMSOHN, Paulo Alexandre. Organization of intermediate filaments and their association with collagen - containing phagosomes in mouse decidual cells. Journal of Structural Biology, v. 103, n. 1 , p. 23-33, 1990Tradução . . Disponível em: https://doi.org/10.1016/1047-8477(90)90082-n. Acesso em: 07 out. 2025.
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      Zorn, T. M. T., Oliveira, S. F., & Abrahamsohn, P. A. (1990). Organization of intermediate filaments and their association with collagen - containing phagosomes in mouse decidual cells. Journal of Structural Biology, 103( 1 ), 23-33. doi:10.1016/1047-8477(90)90082-n
    • NLM

      Zorn TMT, Oliveira SF, Abrahamsohn PA. Organization of intermediate filaments and their association with collagen - containing phagosomes in mouse decidual cells [Internet]. Journal of Structural Biology. 1990 ;103( 1 ): 23-33.[citado 2025 out. 07 ] Available from: https://doi.org/10.1016/1047-8477(90)90082-n
    • Vancouver

      Zorn TMT, Oliveira SF, Abrahamsohn PA. Organization of intermediate filaments and their association with collagen - containing phagosomes in mouse decidual cells [Internet]. Journal of Structural Biology. 1990 ;103( 1 ): 23-33.[citado 2025 out. 07 ] Available from: https://doi.org/10.1016/1047-8477(90)90082-n

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