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  • Unidades: IFSC, IQ, IF, FCFRP

    Assuntos: POLÍMEROS (QUÍMICA ORGÂNICA), EVENTOS

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      International Symposium on Polyelectrolytes -ISP, 14. . Campinas: Universidade Estadual de Campinas - UNICAMP. Disponível em: https://repositorio.usp.br/directbitstream/98820de3-e982-4262-a121-b09fee3363da/3271129.pdf. Acesso em: 24 nov. 2025. , 2025
    • APA

      International Symposium on Polyelectrolytes -ISP, 14. (2025). International Symposium on Polyelectrolytes -ISP, 14. Campinas: Universidade Estadual de Campinas - UNICAMP. Recuperado de https://repositorio.usp.br/directbitstream/98820de3-e982-4262-a121-b09fee3363da/3271129.pdf
    • NLM

      International Symposium on Polyelectrolytes -ISP, 14 [Internet]. 2025 ;[citado 2025 nov. 24 ] Available from: https://repositorio.usp.br/directbitstream/98820de3-e982-4262-a121-b09fee3363da/3271129.pdf
    • Vancouver

      International Symposium on Polyelectrolytes -ISP, 14 [Internet]. 2025 ;[citado 2025 nov. 24 ] Available from: https://repositorio.usp.br/directbitstream/98820de3-e982-4262-a121-b09fee3363da/3271129.pdf
  • Fonte: Comprehensive Computational Chemistry. Unidade: FCFRP

    Assuntos: ÁCIDOS, FÍSICO-QUÍMICA, ELETROSTÁTICA

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      SILVA, Fernando Luís Barroso da. Constant-pH simulation methods for biomolecular systems. Comprehensive Computational Chemistry. Tradução . Amsterdam: Elsevier, 2024. v. 3. . Disponível em: https://doi.org/10.1016/B978-0-12-821978-2.00090-8. Acesso em: 24 nov. 2025.
    • APA

      Silva, F. L. B. da. (2024). Constant-pH simulation methods for biomolecular systems. In Comprehensive Computational Chemistry (Vol. 3). Amsterdam: Elsevier. doi:10.1016/B978-0-12-821978-2.00090-8
    • NLM

      Silva FLB da. Constant-pH simulation methods for biomolecular systems [Internet]. In: Comprehensive Computational Chemistry. Amsterdam: Elsevier; 2024. [citado 2025 nov. 24 ] Available from: https://doi.org/10.1016/B978-0-12-821978-2.00090-8
    • Vancouver

      Silva FLB da. Constant-pH simulation methods for biomolecular systems [Internet]. In: Comprehensive Computational Chemistry. Amsterdam: Elsevier; 2024. [citado 2025 nov. 24 ] Available from: https://doi.org/10.1016/B978-0-12-821978-2.00090-8
  • Fonte: Frontiers in Medical Technology. Unidade: FCFRP

    Assuntos: BIOINFORMÁTICA, ANTICORPOS, COVID-19

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      LOUSA, Diana e SOARES, Cláudio M. e SILVA, Fernando Luís Barroso da. Computational approaches to foster innovation in the treatment and diagnosis of infectious diseases. [Editorial]. Frontiers in Medical Technology. Lausanne: Faculdade de Ciências Farmacêuticas de Ribeirão Preto, Universidade de São Paulo. Disponível em: https://doi.org/10.3389/fmedt.2022.841088. Acesso em: 24 nov. 2025. , 2022
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      Lousa, D., Soares, C. M., & Silva, F. L. B. da. (2022). Computational approaches to foster innovation in the treatment and diagnosis of infectious diseases. [Editorial]. Frontiers in Medical Technology. Lausanne: Faculdade de Ciências Farmacêuticas de Ribeirão Preto, Universidade de São Paulo. doi:10.3389/fmedt.2022.841088
    • NLM

      Lousa D, Soares CM, Silva FLB da. Computational approaches to foster innovation in the treatment and diagnosis of infectious diseases. [Editorial] [Internet]. Frontiers in Medical Technology. 2022 ; 4[citado 2025 nov. 24 ] Available from: https://doi.org/10.3389/fmedt.2022.841088
    • Vancouver

      Lousa D, Soares CM, Silva FLB da. Computational approaches to foster innovation in the treatment and diagnosis of infectious diseases. [Editorial] [Internet]. Frontiers in Medical Technology. 2022 ; 4[citado 2025 nov. 24 ] Available from: https://doi.org/10.3389/fmedt.2022.841088
  • Fonte: Journal of the American Chemical Society. Unidade: FCFRP

    Assuntos: QUÍMICA, ADSORÇÃO, PEPTÍDEOS, PROTEÍNAS, CARGA ELÉTRICA

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      LUNKAD, Raju e SILVA, Fernando Luís Barroso da e KOŠOVAN, Peter. Both charge-regulation and charge-patch distribution can drive adsorption on the wrong side of the isoelectric point. Journal of the American Chemical Society, v. 144, n. 4, p. 1813-1825, 2022Tradução . . Disponível em: https://doi.org/10.1021/jacs.1c11676. Acesso em: 24 nov. 2025.
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      Lunkad, R., Silva, F. L. B. da, & Košovan, P. (2022). Both charge-regulation and charge-patch distribution can drive adsorption on the wrong side of the isoelectric point. Journal of the American Chemical Society, 144( 4), 1813-1825. doi:10.1021/jacs.1c11676
    • NLM

      Lunkad R, Silva FLB da, Košovan P. Both charge-regulation and charge-patch distribution can drive adsorption on the wrong side of the isoelectric point [Internet]. Journal of the American Chemical Society. 2022 ; 144( 4): 1813-1825.[citado 2025 nov. 24 ] Available from: https://doi.org/10.1021/jacs.1c11676
    • Vancouver

      Lunkad R, Silva FLB da, Košovan P. Both charge-regulation and charge-patch distribution can drive adsorption on the wrong side of the isoelectric point [Internet]. Journal of the American Chemical Society. 2022 ; 144( 4): 1813-1825.[citado 2025 nov. 24 ] Available from: https://doi.org/10.1021/jacs.1c11676
  • Fonte: The Journal of Physical Chemistry B. Unidade: FCFRP

    Assuntos: COVID-19, ELETROSTÁTICA, ANGIOTENSINAS, PROTEÍNAS, BIOFÍSICA

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      SILVA, Fernando Luís Barroso da e GIRON, Carolina Corrêa e LAAKSONEN, Aatto. Electrostatic features for the receptor binding domain of SARS-COV-2 wildtype and its variants. Compass to the severity of the future variants with the charge-rule. The Journal of Physical Chemistry B, v. 126, n. 36, p. 6835-6852, 2022Tradução . . Disponível em: https://doi.org/10.1021/acs.jpcb.2c04225. Acesso em: 24 nov. 2025.
    • APA

      Silva, F. L. B. da, Giron, C. C., & Laaksonen, A. (2022). Electrostatic features for the receptor binding domain of SARS-COV-2 wildtype and its variants. Compass to the severity of the future variants with the charge-rule. The Journal of Physical Chemistry B, 126( 36), 6835-6852. doi:10.1021/acs.jpcb.2c04225
    • NLM

      Silva FLB da, Giron CC, Laaksonen A. Electrostatic features for the receptor binding domain of SARS-COV-2 wildtype and its variants. Compass to the severity of the future variants with the charge-rule [Internet]. The Journal of Physical Chemistry B. 2022 ; 126( 36): 6835-6852.[citado 2025 nov. 24 ] Available from: https://doi.org/10.1021/acs.jpcb.2c04225
    • Vancouver

      Silva FLB da, Giron CC, Laaksonen A. Electrostatic features for the receptor binding domain of SARS-COV-2 wildtype and its variants. Compass to the severity of the future variants with the charge-rule [Internet]. The Journal of Physical Chemistry B. 2022 ; 126( 36): 6835-6852.[citado 2025 nov. 24 ] Available from: https://doi.org/10.1021/acs.jpcb.2c04225
  • Fonte: Journal of Chemical Information and Modeling. Unidades: FCFRP, Interunidades em Bioinformática

    Assuntos: ZIKA VÍRUS, VIRULÊNCIA, FLAVIVIRUS

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      POVEDA CUEVAS, Sergio Alejandro e SILVA, Fernando Luís Barroso da e ETCHEBEST, Catherine. How the strain origin of Zika Virus NS1 protein impacts its dynamics and implications to their differential virulence. Journal of Chemical Information and Modeling, v. 61, n. 3, p. 1516-1530, 2021Tradução . . Disponível em: https://doi.org/10.1021/acs.jcim.0c01377. Acesso em: 24 nov. 2025.
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      Poveda Cuevas, S. A., Silva, F. L. B. da, & Etchebest, C. (2021). How the strain origin of Zika Virus NS1 protein impacts its dynamics and implications to their differential virulence. Journal of Chemical Information and Modeling, 61( 3), 1516-1530. doi:10.1021/acs.jcim.0c01377
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      Poveda Cuevas SA, Silva FLB da, Etchebest C. How the strain origin of Zika Virus NS1 protein impacts its dynamics and implications to their differential virulence [Internet]. Journal of Chemical Information and Modeling. 2021 ; 61( 3): 1516-1530.[citado 2025 nov. 24 ] Available from: https://doi.org/10.1021/acs.jcim.0c01377
    • Vancouver

      Poveda Cuevas SA, Silva FLB da, Etchebest C. How the strain origin of Zika Virus NS1 protein impacts its dynamics and implications to their differential virulence [Internet]. Journal of Chemical Information and Modeling. 2021 ; 61( 3): 1516-1530.[citado 2025 nov. 24 ] Available from: https://doi.org/10.1021/acs.jcim.0c01377
  • Fonte: Frontiers in Medical Technology. Unidade: FCFRP

    Assuntos: CORONAVIRUS, EPITOPOS, MUTAÇÃO GENÉTICA, VIRULÊNCIA

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      GIRON, Carolina Corrêa e LAAKSONEM, Aatto e SILVA, Fernando Luís Barroso da. Up state of the SARS-COV-2 spike homotrimer favors an increased virulence for new variants. Frontiers in Medical Technology, v. 3, 2021Tradução . . Disponível em: https://doi.org/10.3389/fmedt.2021.694347. Acesso em: 24 nov. 2025.
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      Giron, C. C., Laaksonem, A., & Silva, F. L. B. da. (2021). Up state of the SARS-COV-2 spike homotrimer favors an increased virulence for new variants. Frontiers in Medical Technology, 3. doi:10.3389/fmedt.2021.694347
    • NLM

      Giron CC, Laaksonem A, Silva FLB da. Up state of the SARS-COV-2 spike homotrimer favors an increased virulence for new variants [Internet]. Frontiers in Medical Technology. 2021 ; 3[citado 2025 nov. 24 ] Available from: https://doi.org/10.3389/fmedt.2021.694347
    • Vancouver

      Giron CC, Laaksonem A, Silva FLB da. Up state of the SARS-COV-2 spike homotrimer favors an increased virulence for new variants [Internet]. Frontiers in Medical Technology. 2021 ; 3[citado 2025 nov. 24 ] Available from: https://doi.org/10.3389/fmedt.2021.694347
  • Fonte: Vaccines. Unidades: IFSC, FCFRP, ICB, Interunidades em Biotecnologia

    Assuntos: COVID-19, CORONAVIRUS, VACINAS VIRAIS, IMUNOLOGIA, VARIAÇÃO GENÉTICA, MUTAÇÃO GENÉTICA

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      SYED, Wasim Aluisio Prates et al. VLP-based COVID-19 vaccines: an adaptable technology against the threat of new variants. Vaccines, v. 9, n. 12, p. 1409-1-1409-17, 2021Tradução . . Disponível em: https://doi.org/10.3390/vaccines9121409. Acesso em: 24 nov. 2025.
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      Syed, W. A. P., Chaves, L. C. S., Crema, K. P., Vuitika, L., Lira, A., Cortês, N. de A., et al. (2021). VLP-based COVID-19 vaccines: an adaptable technology against the threat of new variants. Vaccines, 9( 12), 1409-1-1409-17. doi:10.3390/vaccines9121409
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      Syed WAP, Chaves LCS, Crema KP, Vuitika L, Lira A, Cortês N de A, Kersten V, Guimarães FEG, Sadraeian M, Silva FLB da, Cabral-Marques O, Barbuto JAM, Russo M, Câmara NOS, Miranda GC de. VLP-based COVID-19 vaccines: an adaptable technology against the threat of new variants [Internet]. Vaccines. 2021 ; 9( 12): 1409-1-1409-17.[citado 2025 nov. 24 ] Available from: https://doi.org/10.3390/vaccines9121409
    • Vancouver

      Syed WAP, Chaves LCS, Crema KP, Vuitika L, Lira A, Cortês N de A, Kersten V, Guimarães FEG, Sadraeian M, Silva FLB da, Cabral-Marques O, Barbuto JAM, Russo M, Câmara NOS, Miranda GC de. VLP-based COVID-19 vaccines: an adaptable technology against the threat of new variants [Internet]. Vaccines. 2021 ; 9( 12): 1409-1-1409-17.[citado 2025 nov. 24 ] Available from: https://doi.org/10.3390/vaccines9121409
  • Fonte: Annual Review of Food Science and Technology. Unidade: FCFRP

    Assuntos: SIMULAÇÃO, PROTEÍNAS, DIETÉTICA, ALIMENTOS

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      SILVA, Fernando Luís Barroso da et al. Understanding and controlling food protein structure and function in foods: perspectives from experiments and computer simulations. Annual Review of Food Science and Technology, v. 11, p. 365-387, 2020Tradução . . Disponível em: https://doi.org/10.1146/annurev-food-032519-051640. Acesso em: 24 nov. 2025.
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      Silva, F. L. B. da, Carloni, P., Cheung, D., Cottone, G., Donnini, S., Foegeding, E. A., et al. (2020). Understanding and controlling food protein structure and function in foods: perspectives from experiments and computer simulations. Annual Review of Food Science and Technology, 11, 365-387. doi:10.1146/annurev-food-032519-051640
    • NLM

      Silva FLB da, Carloni P, Cheung D, Cottone G, Donnini S, Foegeding EA, Gulzar M, Jacquier JC, Lobaskin V, MacKernan D, Naveh ZMH, Radhakrishnan R, Santiso EE. Understanding and controlling food protein structure and function in foods: perspectives from experiments and computer simulations [Internet]. Annual Review of Food Science and Technology. 2020 ; 11 365-387.[citado 2025 nov. 24 ] Available from: https://doi.org/10.1146/annurev-food-032519-051640
    • Vancouver

      Silva FLB da, Carloni P, Cheung D, Cottone G, Donnini S, Foegeding EA, Gulzar M, Jacquier JC, Lobaskin V, MacKernan D, Naveh ZMH, Radhakrishnan R, Santiso EE. Understanding and controlling food protein structure and function in foods: perspectives from experiments and computer simulations [Internet]. Annual Review of Food Science and Technology. 2020 ; 11 365-387.[citado 2025 nov. 24 ] Available from: https://doi.org/10.1146/annurev-food-032519-051640
  • Fonte: Journal of Polymer Science. Unidade: FCFRP

    Assuntos: FÍSICO-QUÍMICA, PEPTÍDEOS, MACROMOLÉCULA, POLÍMEROS (MATERIAIS), BIOPOLÍMEROS

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      SMITH, Ryan J. et al. Exploring the physicochemical and morphological properties of peptide-hybridized dendrimers DendriPeps and their aggregates. Journal of Polymer Science, v. 58, n. 16, p. 2234-2247, 2020Tradução . . Disponível em: https://doi.org/10.1002/pol.20200277. Acesso em: 24 nov. 2025.
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      Smith, R. J., Fabiani, T., Wang, S., Ramesh, S., Khan, S., Santiso, E., et al. (2020). Exploring the physicochemical and morphological properties of peptide-hybridized dendrimers DendriPeps and their aggregates. Journal of Polymer Science, 58( 16), 2234-2247. doi:10.1002/pol.20200277
    • NLM

      Smith RJ, Fabiani T, Wang S, Ramesh S, Khan S, Santiso E, Silva FLB da, Gorman C, Menegatti S. Exploring the physicochemical and morphological properties of peptide-hybridized dendrimers DendriPeps and their aggregates [Internet]. Journal of Polymer Science. 2020 ; 58( 16): 2234-2247.[citado 2025 nov. 24 ] Available from: https://doi.org/10.1002/pol.20200277
    • Vancouver

      Smith RJ, Fabiani T, Wang S, Ramesh S, Khan S, Santiso E, Silva FLB da, Gorman C, Menegatti S. Exploring the physicochemical and morphological properties of peptide-hybridized dendrimers DendriPeps and their aggregates [Internet]. Journal of Polymer Science. 2020 ; 58( 16): 2234-2247.[citado 2025 nov. 24 ] Available from: https://doi.org/10.1002/pol.20200277
  • Fonte: Journal of Chemical Information and Modeling. Unidade: FCFRP

    Assuntos: BIOMATERIAIS, MÉTODO DE MONTE CARLO, INSULINA, QUITOSANA, ELETROSTÁTICA, MACROMOLÉCULA

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      PRUDKIN-SILVA, Cecilia et al. Combined experimental and molecular simulation study of insulin–chitosan complexation driven by electrostatic interactions. Journal of Chemical Information and Modeling, v. 60, n. 2, p. 854-865, 2020Tradução . . Disponível em: https://doi.org/10.1021/acs.jcim.9b00814. Acesso em: 24 nov. 2025.
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      Prudkin-Silva, C., Pérez, O. E., Martínez, K. D., & Silva, F. L. B. da. (2020). Combined experimental and molecular simulation study of insulin–chitosan complexation driven by electrostatic interactions. Journal of Chemical Information and Modeling, 60( 2), 854-865. doi:10.1021/acs.jcim.9b00814
    • NLM

      Prudkin-Silva C, Pérez OE, Martínez KD, Silva FLB da. Combined experimental and molecular simulation study of insulin–chitosan complexation driven by electrostatic interactions [Internet]. Journal of Chemical Information and Modeling. 2020 ; 60( 2): 854-865.[citado 2025 nov. 24 ] Available from: https://doi.org/10.1021/acs.jcim.9b00814
    • Vancouver

      Prudkin-Silva C, Pérez OE, Martínez KD, Silva FLB da. Combined experimental and molecular simulation study of insulin–chitosan complexation driven by electrostatic interactions [Internet]. Journal of Chemical Information and Modeling. 2020 ; 60( 2): 854-865.[citado 2025 nov. 24 ] Available from: https://doi.org/10.1021/acs.jcim.9b00814
  • Fonte: The Journal of Physical Chemistry B. Unidades: FCFRP, FFCLRP

    Assuntos: GENÉTICA, MATERIAIS NANOESTRUTURADOS, PEPTÍDEOS, PROTEÍNAS, DOENÇA DE ALZHEIMER

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      FRIGORI, Rafael B. et al. Occurrence of biased conformations as precursors of assembly states in fibril elongation of amyloid-β fibril variants: an in silico study. The Journal of Physical Chemistry B, v. 124, n. 14, p. 2798-2805, 2020Tradução . . Disponível em: https://doi.org/10.1021/acs.jpcb.0c01360. Acesso em: 24 nov. 2025.
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      Frigori, R. B., Silva, F. L. B. da, Carvalho, P. P. D., & Alves, N. A. (2020). Occurrence of biased conformations as precursors of assembly states in fibril elongation of amyloid-β fibril variants: an in silico study. The Journal of Physical Chemistry B, 124( 14), 2798-2805. doi:10.1021/acs.jpcb.0c01360
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      Frigori RB, Silva FLB da, Carvalho PPD, Alves NA. Occurrence of biased conformations as precursors of assembly states in fibril elongation of amyloid-β fibril variants: an in silico study [Internet]. The Journal of Physical Chemistry B. 2020 ; 124( 14): 2798-2805.[citado 2025 nov. 24 ] Available from: https://doi.org/10.1021/acs.jpcb.0c01360
    • Vancouver

      Frigori RB, Silva FLB da, Carvalho PPD, Alves NA. Occurrence of biased conformations as precursors of assembly states in fibril elongation of amyloid-β fibril variants: an in silico study [Internet]. The Journal of Physical Chemistry B. 2020 ; 124( 14): 2798-2805.[citado 2025 nov. 24 ] Available from: https://doi.org/10.1021/acs.jpcb.0c01360
  • Fonte: Virus Research. Unidade: FCFRP

    Assuntos: CORONAVIRUS, VÍRUS, ANTICORPOS MONOCLONAIS, EPITOPOS

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      GIRON, Carolina Corrêa e LAAKSONEN, Aatto e SILVA, Fernando Luís Barroso da. On the interactions of the receptor-binding domain of SARS-CoV-1 and SARS-CoV-2 spike proteins with monoclonal antibodies and the receptor ACE2. Virus Research, v. 285, p. 1-13, 2020Tradução . . Disponível em: https://doi.org/10.1016/j.virusres.2020.198021. Acesso em: 24 nov. 2025.
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      Giron, C. C., Laaksonen, A., & Silva, F. L. B. da. (2020). On the interactions of the receptor-binding domain of SARS-CoV-1 and SARS-CoV-2 spike proteins with monoclonal antibodies and the receptor ACE2. Virus Research, 285, 1-13. doi:10.1016/j.virusres.2020.198021
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      Giron CC, Laaksonen A, Silva FLB da. On the interactions of the receptor-binding domain of SARS-CoV-1 and SARS-CoV-2 spike proteins with monoclonal antibodies and the receptor ACE2 [Internet]. Virus Research. 2020 ; 285 1-13.[citado 2025 nov. 24 ] Available from: https://doi.org/10.1016/j.virusres.2020.198021
    • Vancouver

      Giron CC, Laaksonen A, Silva FLB da. On the interactions of the receptor-binding domain of SARS-CoV-1 and SARS-CoV-2 spike proteins with monoclonal antibodies and the receptor ACE2 [Internet]. Virus Research. 2020 ; 285 1-13.[citado 2025 nov. 24 ] Available from: https://doi.org/10.1016/j.virusres.2020.198021
  • Fonte: Journal of Biomolecular Structure and Dynamics. Unidade: FCFRP

    Assuntos: POLIMORFISMO, COVID-19, PROTEÍNAS, ANTICORPOS, MOLÉCULA

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      GIRON, Carolina Corrêa e LAAKSONEN, Aatto e SILVA, Fernando Luís Barroso da. Differences between Omicron SARS-CoV-2 RBD and other variants in their ability to interact with cell receptors and monoclonal antibodies. Journal of Biomolecular Structure and Dynamics, v. 41, n. 12, p. 5707-5727, 202ADTradução . . Disponível em: https://doi.org/10.1080/07391102.2022.2095305. Acesso em: 24 nov. 2025.
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      Giron, C. C., Laaksonen, A., & Silva, F. L. B. da. (202AD). Differences between Omicron SARS-CoV-2 RBD and other variants in their ability to interact with cell receptors and monoclonal antibodies. Journal of Biomolecular Structure and Dynamics, 41( 12), 5707-5727. doi:10.1080/07391102.2022.2095305
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      Giron CC, Laaksonen A, Silva FLB da. Differences between Omicron SARS-CoV-2 RBD and other variants in their ability to interact with cell receptors and monoclonal antibodies [Internet]. Journal of Biomolecular Structure and Dynamics. 202AD ; 41( 12): 5707-5727.[citado 2025 nov. 24 ] Available from: https://doi.org/10.1080/07391102.2022.2095305
    • Vancouver

      Giron CC, Laaksonen A, Silva FLB da. Differences between Omicron SARS-CoV-2 RBD and other variants in their ability to interact with cell receptors and monoclonal antibodies [Internet]. Journal of Biomolecular Structure and Dynamics. 202AD ; 41( 12): 5707-5727.[citado 2025 nov. 24 ] Available from: https://doi.org/10.1080/07391102.2022.2095305
  • Fonte: Cytoskeleton. Unidades: FCFRP, IFSC

    Assuntos: CITOESQUELETO, PROTEÍNAS, MAMÍFEROS

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      MENDONÇA, Deborah Cezar et al. A revised order of subunits in mammalian septin complexes. Cytoskeleton, v. 76, n. 9-10, p. 457-466, 2019Tradução . . Disponível em: https://doi.org/10.1002/cm.21569. Acesso em: 24 nov. 2025.
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      Mendonça, D. C., Macêdo, J. N. A., Guimarães, S. L., Silva, F. L. B. da, Cassago, A., Garratt, R. C., et al. (2019). A revised order of subunits in mammalian septin complexes. Cytoskeleton, 76( 9-10), 457-466. doi:10.1002/cm.21569
    • NLM

      Mendonça DC, Macêdo JNA, Guimarães SL, Silva FLB da, Cassago A, Garratt RC, Portugal RV, Araújo APU de. A revised order of subunits in mammalian septin complexes [Internet]. Cytoskeleton. 2019 ; 76( 9-10): 457-466.[citado 2025 nov. 24 ] Available from: https://doi.org/10.1002/cm.21569
    • Vancouver

      Mendonça DC, Macêdo JNA, Guimarães SL, Silva FLB da, Cassago A, Garratt RC, Portugal RV, Araújo APU de. A revised order of subunits in mammalian septin complexes [Internet]. Cytoskeleton. 2019 ; 76( 9-10): 457-466.[citado 2025 nov. 24 ] Available from: https://doi.org/10.1002/cm.21569
  • Fonte: Journal of Chemical Theory and Computation. Unidade: FCFRP

    Assuntos: SIMULAÇÃO, CRISTALOGRAFIA, CONFORMAÇÃO PROTEICA, PROTEÍNAS, QUÍMICA

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      SILVA, Fernando Luís Barroso da e STERPONE, Fabio e DERREUMAUX, Philippe. OPEP6: a new constant-pH molecular dynamics simulation scheme with OPEP coarse-grained force field. Journal of Chemical Theory and Computation, v. 15, n. 6, p. 3875-3888, 2019Tradução . . Disponível em: https://doi.org/10.1021/acs.jctc.9b00202. Acesso em: 24 nov. 2025.
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      Silva, F. L. B. da, Sterpone, F., & Derreumaux, P. (2019). OPEP6: a new constant-pH molecular dynamics simulation scheme with OPEP coarse-grained force field. Journal of Chemical Theory and Computation, 15( 6), 3875-3888. doi:10.1021/acs.jctc.9b00202
    • NLM

      Silva FLB da, Sterpone F, Derreumaux P. OPEP6: a new constant-pH molecular dynamics simulation scheme with OPEP coarse-grained force field [Internet]. Journal of Chemical Theory and Computation. 2019 ; 15( 6): 3875-3888.[citado 2025 nov. 24 ] Available from: https://doi.org/10.1021/acs.jctc.9b00202
    • Vancouver

      Silva FLB da, Sterpone F, Derreumaux P. OPEP6: a new constant-pH molecular dynamics simulation scheme with OPEP coarse-grained force field [Internet]. Journal of Chemical Theory and Computation. 2019 ; 15( 6): 3875-3888.[citado 2025 nov. 24 ] Available from: https://doi.org/10.1021/acs.jctc.9b00202
  • Fonte: Interface Focus. Unidade: FCFRP

    Assuntos: RNA, BIOFÍSICA, BIOINFORMÁTICA

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      PASQUALI, Samuela e FREZZA, Elisa e SILVA, Fernando Luís Barroso da. Coarse-grained dynamic RNA titration simulations. Interface Focus, v. 9, n. 3, 2019Tradução . . Disponível em: https://doi.org/10.1098/rsfs.2018.0066. Acesso em: 24 nov. 2025.
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      Pasquali, S., Frezza, E., & Silva, F. L. B. da. (2019). Coarse-grained dynamic RNA titration simulations. Interface Focus, 9( 3). doi:10.1098/rsfs.2018.0066
    • NLM

      Pasquali S, Frezza E, Silva FLB da. Coarse-grained dynamic RNA titration simulations [Internet]. Interface Focus. 2019 ; 9( 3):[citado 2025 nov. 24 ] Available from: https://doi.org/10.1098/rsfs.2018.0066
    • Vancouver

      Pasquali S, Frezza E, Silva FLB da. Coarse-grained dynamic RNA titration simulations [Internet]. Interface Focus. 2019 ; 9( 3):[citado 2025 nov. 24 ] Available from: https://doi.org/10.1098/rsfs.2018.0066
  • Fonte: Journal of Chemical Information and Modeling. Unidades: Interunidades em Bioinformática, FCFRP

    Assuntos: ANTÍGENOS, IMUNOLOGIA, FLAVIVIRUS

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      POVEDA CUEVAS, Sergio Alejandro e ETCHEBEST, Catherine e SILVA, Fernando Luís Barroso da. Identification of electrostatic epitopes in flavivirus by computer simulations: the PROCEEDpKa method. Journal of Chemical Information and Modeling, v. 60, n. 2, p. 944-963, 2019Tradução . . Disponível em: https://doi.org/10.1021/acs.jcim.9b00895. Acesso em: 24 nov. 2025.
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      Poveda Cuevas, S. A., Etchebest, C., & Silva, F. L. B. da. (2019). Identification of electrostatic epitopes in flavivirus by computer simulations: the PROCEEDpKa method. Journal of Chemical Information and Modeling, 60( 2), 944-963. doi:10.1021/acs.jcim.9b00895
    • NLM

      Poveda Cuevas SA, Etchebest C, Silva FLB da. Identification of electrostatic epitopes in flavivirus by computer simulations: the PROCEEDpKa method [Internet]. Journal of Chemical Information and Modeling. 2019 ; 60( 2): 944-963.[citado 2025 nov. 24 ] Available from: https://doi.org/10.1021/acs.jcim.9b00895
    • Vancouver

      Poveda Cuevas SA, Etchebest C, Silva FLB da. Identification of electrostatic epitopes in flavivirus by computer simulations: the PROCEEDpKa method [Internet]. Journal of Chemical Information and Modeling. 2019 ; 60( 2): 944-963.[citado 2025 nov. 24 ] Available from: https://doi.org/10.1021/acs.jcim.9b00895
  • Fonte: International Journal of Biological Macromolecules. Unidade: FCFRP

    Assuntos: CARRAGENINA, QUINOA, ADSORÇÃO

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      DURAN, Natalia Montellano et al. A combined experimental and molecular simulation study of factors influencing interaction of quinoa proteins–carrageenan. International Journal of Biological Macromolecules, v. 107, p. 949-956, 2018Tradução . . Disponível em: https://doi.org/10.1016/j.ijbiomac.2017.09.076. Acesso em: 24 nov. 2025.
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      Duran, N. M., Spelzini, D., Wayllace, N., Boeris, V., & Silva, F. L. B. (2018). A combined experimental and molecular simulation study of factors influencing interaction of quinoa proteins–carrageenan. International Journal of Biological Macromolecules, 107, 949-956. doi:10.1016/j.ijbiomac.2017.09.076
    • NLM

      Duran NM, Spelzini D, Wayllace N, Boeris V, Silva FLB. A combined experimental and molecular simulation study of factors influencing interaction of quinoa proteins–carrageenan [Internet]. International Journal of Biological Macromolecules. 2018 ; 107 949-956.[citado 2025 nov. 24 ] Available from: https://doi.org/10.1016/j.ijbiomac.2017.09.076
    • Vancouver

      Duran NM, Spelzini D, Wayllace N, Boeris V, Silva FLB. A combined experimental and molecular simulation study of factors influencing interaction of quinoa proteins–carrageenan [Internet]. International Journal of Biological Macromolecules. 2018 ; 107 949-956.[citado 2025 nov. 24 ] Available from: https://doi.org/10.1016/j.ijbiomac.2017.09.076
  • Fonte: Biochemical and Biophysical Research Communications. Unidade: FCFRP

    Assuntos: MÉTODO DE MONTE CARLO, IONS, ELETROSTÁTICA, RNA

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    • ABNT

      SILVA, Fernando Luis Barroso e DERREUMAUX, Philippe e PASQUALI, Samuela. Protein-RNA complexation driven by the charge regulation mechanism. Biochemical and Biophysical Research Communications, v. 498, n. 2, p. 264-273, 2018Tradução . . Disponível em: https://doi.org/10.1016/j.bbrc.2017.07.027. Acesso em: 24 nov. 2025.
    • APA

      Silva, F. L. B., Derreumaux, P., & Pasquali, S. (2018). Protein-RNA complexation driven by the charge regulation mechanism. Biochemical and Biophysical Research Communications, 498( 2), 264-273. doi:10.1016/j.bbrc.2017.07.027
    • NLM

      Silva FLB, Derreumaux P, Pasquali S. Protein-RNA complexation driven by the charge regulation mechanism [Internet]. Biochemical and Biophysical Research Communications. 2018 ; 498( 2): 264-273.[citado 2025 nov. 24 ] Available from: https://doi.org/10.1016/j.bbrc.2017.07.027
    • Vancouver

      Silva FLB, Derreumaux P, Pasquali S. Protein-RNA complexation driven by the charge regulation mechanism [Internet]. Biochemical and Biophysical Research Communications. 2018 ; 498( 2): 264-273.[citado 2025 nov. 24 ] Available from: https://doi.org/10.1016/j.bbrc.2017.07.027

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