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  • Source: Waste. Unidades: IFSC, EESC, EP

    Subjects: CANA-DE-AÇÚCAR, BAGAÇOS, ETANOL, REFINARIAS

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      PEIXOTO, Guilherme et al. Acidogenesis of pentose liquor to produce biohydrogen and organic acids integrated with 1G-2G ethanol production in sugarcane biorefineries. Waste, v. 1, n. 3, p. 672-688, 2023Tradução . . Disponível em: https://doi.org/10.3390/waste1030040. Acesso em: 05 jun. 2024.
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      Peixoto, G., Mockaitis, G., Moreira, W. K., Lima, D. M. F., Coral, M. A. de L., Ferreira, F. V., et al. (2023). Acidogenesis of pentose liquor to produce biohydrogen and organic acids integrated with 1G-2G ethanol production in sugarcane biorefineries. Waste, 1( 3), 672-688. doi:10.3390/waste1030040
    • NLM

      Peixoto G, Mockaitis G, Moreira WK, Lima DMF, Coral MA de L, Ferreira FV, Fuess LT, Polikarpov I, Zaiat M. Acidogenesis of pentose liquor to produce biohydrogen and organic acids integrated with 1G-2G ethanol production in sugarcane biorefineries [Internet]. Waste. 2023 ; 1( 3): 672-688.[citado 2024 jun. 05 ] Available from: https://doi.org/10.3390/waste1030040
    • Vancouver

      Peixoto G, Mockaitis G, Moreira WK, Lima DMF, Coral MA de L, Ferreira FV, Fuess LT, Polikarpov I, Zaiat M. Acidogenesis of pentose liquor to produce biohydrogen and organic acids integrated with 1G-2G ethanol production in sugarcane biorefineries [Internet]. Waste. 2023 ; 1( 3): 672-688.[citado 2024 jun. 05 ] Available from: https://doi.org/10.3390/waste1030040
  • Source: Journal of Molecular Modeling. Unidade: IFSC

    Subjects: XANTHOMONAS, ELASTICIDADE, CATÁLISE

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      SKAF, Munir Salomão e POLIKARPOV, Igor e STANKOVIC, Ivana M. A linker of the proline-threonine repeatingmotif sequence is bimodal. Journal of Molecular Modeling, v. 26, n. 8, p. 178-1-178-7, 2020Tradução . . Disponível em: https://doi.org/10.1007/s00894-020-04434-0. Acesso em: 05 jun. 2024.
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      Skaf, M. S., Polikarpov, I., & Stankovic, I. M. (2020). A linker of the proline-threonine repeatingmotif sequence is bimodal. Journal of Molecular Modeling, 26( 8), 178-1-178-7. doi:10.1007/s00894-020-04434-0
    • NLM

      Skaf MS, Polikarpov I, Stankovic IM. A linker of the proline-threonine repeatingmotif sequence is bimodal [Internet]. Journal of Molecular Modeling. 2020 ; 26( 8): 178-1-178-7.[citado 2024 jun. 05 ] Available from: https://doi.org/10.1007/s00894-020-04434-0
    • Vancouver

      Skaf MS, Polikarpov I, Stankovic IM. A linker of the proline-threonine repeatingmotif sequence is bimodal [Internet]. Journal of Molecular Modeling. 2020 ; 26( 8): 178-1-178-7.[citado 2024 jun. 05 ] Available from: https://doi.org/10.1007/s00894-020-04434-0
  • Source: Abstract book. Conference titles: Annual Meeting of the Brazilian Society for Biochemistry and Molecular Biology - SBBq. Unidade: IFSC

    Subjects: CELULOSE, ENZIMAS, BIOTECNOLOGIA

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      PELLEGRINI, Vanessa de Oliveira Arnoldi et al. Cellulose accessibility influences efficiency of enzymatic hydrolysis and impacts a synergy between cellulases. 2019, Anais.. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular - SBBq, 2019. Disponível em: http://www.sbbq.org.br/reuniao/2019/images/Livro_Resumos_2019.pdf. Acesso em: 05 jun. 2024.
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      Pellegrini, V. de O. A., Bernardes, A., Rezende, C., & Polikarpov, I. (2019). Cellulose accessibility influences efficiency of enzymatic hydrolysis and impacts a synergy between cellulases. In Abstract book. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular - SBBq. Recuperado de http://www.sbbq.org.br/reuniao/2019/images/Livro_Resumos_2019.pdf
    • NLM

      Pellegrini V de OA, Bernardes A, Rezende C, Polikarpov I. Cellulose accessibility influences efficiency of enzymatic hydrolysis and impacts a synergy between cellulases [Internet]. Abstract book. 2019 ;[citado 2024 jun. 05 ] Available from: http://www.sbbq.org.br/reuniao/2019/images/Livro_Resumos_2019.pdf
    • Vancouver

      Pellegrini V de OA, Bernardes A, Rezende C, Polikarpov I. Cellulose accessibility influences efficiency of enzymatic hydrolysis and impacts a synergy between cellulases [Internet]. Abstract book. 2019 ;[citado 2024 jun. 05 ] Available from: http://www.sbbq.org.br/reuniao/2019/images/Livro_Resumos_2019.pdf
  • Source: Scientific Reports. Unidade: IFSC

    Subjects: ENZIMAS, RECEPTORES, CRISTALOGRAFIA ESTRUTURAL

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      GODOY, Andre S. et al. Structure, computational and biochemical analysis of PcCel45A endoglucanase from Phanerochaete chrysosporium and catalytic mechanisms of GH45 subfamily C members. Scientific Reports, v. 8, p. 3678-1-3678-14, 2018Tradução . . Disponível em: https://doi.org/10.1038/s41598-018-21798-9. Acesso em: 05 jun. 2024.
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      Godoy, A. S., Pereira, C. S., Ramia, M. P., Silveira, R. L., Camilo, C. M., Kadowaki, M. A., et al. (2018). Structure, computational and biochemical analysis of PcCel45A endoglucanase from Phanerochaete chrysosporium and catalytic mechanisms of GH45 subfamily C members. Scientific Reports, 8, 3678-1-3678-14. doi:10.1038/s41598-018-21798-9
    • NLM

      Godoy AS, Pereira CS, Ramia MP, Silveira RL, Camilo CM, Kadowaki MA, Lange L, Busk PK, Nascimento AS, Skaf MS, Polikarpov I. Structure, computational and biochemical analysis of PcCel45A endoglucanase from Phanerochaete chrysosporium and catalytic mechanisms of GH45 subfamily C members [Internet]. Scientific Reports. 2018 ; 8 3678-1-3678-14.[citado 2024 jun. 05 ] Available from: https://doi.org/10.1038/s41598-018-21798-9
    • Vancouver

      Godoy AS, Pereira CS, Ramia MP, Silveira RL, Camilo CM, Kadowaki MA, Lange L, Busk PK, Nascimento AS, Skaf MS, Polikarpov I. Structure, computational and biochemical analysis of PcCel45A endoglucanase from Phanerochaete chrysosporium and catalytic mechanisms of GH45 subfamily C members [Internet]. Scientific Reports. 2018 ; 8 3678-1-3678-14.[citado 2024 jun. 05 ] Available from: https://doi.org/10.1038/s41598-018-21798-9
  • Source: Cellulose. Unidade: IFSC

    Subjects: TRICHODERMA, MICROSCOPIA ELETRÔNICA DE VARREDURA, CELULOSE

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      PELLEGRINI, V. O. A. et al. Cellulose fiber size defines efficiency of enzymatic hydrolysis and impacts degree of synergy between endoand exoglucanases. Cellulose, v. 25, n. 3, p. 1865-1881, 2018Tradução . . Disponível em: https://doi.org/10.1007/s10570-018-1700-z. Acesso em: 05 jun. 2024.
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      Pellegrini, V. O. A., Bernardes, A., Rezenda, C. A., & Polikarpov, I. (2018). Cellulose fiber size defines efficiency of enzymatic hydrolysis and impacts degree of synergy between endoand exoglucanases. Cellulose, 25( 3), 1865-1881. doi:10.1007/s10570-018-1700-z
    • NLM

      Pellegrini VOA, Bernardes A, Rezenda CA, Polikarpov I. Cellulose fiber size defines efficiency of enzymatic hydrolysis and impacts degree of synergy between endoand exoglucanases [Internet]. Cellulose. 2018 ; 25( 3): 1865-1881.[citado 2024 jun. 05 ] Available from: https://doi.org/10.1007/s10570-018-1700-z
    • Vancouver

      Pellegrini VOA, Bernardes A, Rezenda CA, Polikarpov I. Cellulose fiber size defines efficiency of enzymatic hydrolysis and impacts degree of synergy between endoand exoglucanases [Internet]. Cellulose. 2018 ; 25( 3): 1865-1881.[citado 2024 jun. 05 ] Available from: https://doi.org/10.1007/s10570-018-1700-z
  • Source: Scientific Reports. Unidade: IFSC

    Subjects: ESTRADIOL, RECEPTORES, CRISTALOGRAFIA ESTRUTURAL

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      SOUZA, Paulo C. T. et al. An alternative conformation of ERβ bound to estradiol reveals H12 in a stable antagonist position. Scientific Reports, v. 7, p. 3509-1-3509-11, 2017Tradução . . Disponível em: https://doi.org/10.1038/s41598-017-03774-x. Acesso em: 05 jun. 2024.
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      Souza, P. C. T., Textor, L. C., Melo, D. C., Nascimento, A. S., Skaf, M. S., & Polikarpov, I. (2017). An alternative conformation of ERβ bound to estradiol reveals H12 in a stable antagonist position. Scientific Reports, 7, 3509-1-3509-11. doi:10.1038/s41598-017-03774-x
    • NLM

      Souza PCT, Textor LC, Melo DC, Nascimento AS, Skaf MS, Polikarpov I. An alternative conformation of ERβ bound to estradiol reveals H12 in a stable antagonist position [Internet]. Scientific Reports. 2017 ; 7 3509-1-3509-11.[citado 2024 jun. 05 ] Available from: https://doi.org/10.1038/s41598-017-03774-x
    • Vancouver

      Souza PCT, Textor LC, Melo DC, Nascimento AS, Skaf MS, Polikarpov I. An alternative conformation of ERβ bound to estradiol reveals H12 in a stable antagonist position [Internet]. Scientific Reports. 2017 ; 7 3509-1-3509-11.[citado 2024 jun. 05 ] Available from: https://doi.org/10.1038/s41598-017-03774-x
  • Source: Abstracts. Conference titles: Annual Meeting of the Brazilian Society for Biochemistry and Molecular Biology - SBBq. Unidades: IFSC, IQSC

    Assunto: PROTEÍNAS

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      MINARI, Karine et al. Thermodynamic signature of Hsp90 interaction with adenosine nucleotides. 2017, Anais.. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular - SBBq, 2017. Disponível em: https://repositorio.usp.br/directbitstream/8cb79fbf-a585-4d4f-834f-b9fd235f3d62/P17075.pdf. Acesso em: 05 jun. 2024.
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      Minari, K., Azevedo, É. C., Rodrigues, V. K. T., Batista, F., Nascimento, A. S., Ramos, C., & Borges, J. C. (2017). Thermodynamic signature of Hsp90 interaction with adenosine nucleotides. In Abstracts. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular - SBBq. Recuperado de https://repositorio.usp.br/directbitstream/8cb79fbf-a585-4d4f-834f-b9fd235f3d62/P17075.pdf
    • NLM

      Minari K, Azevedo ÉC, Rodrigues VKT, Batista F, Nascimento AS, Ramos C, Borges JC. Thermodynamic signature of Hsp90 interaction with adenosine nucleotides [Internet]. Abstracts. 2017 ;[citado 2024 jun. 05 ] Available from: https://repositorio.usp.br/directbitstream/8cb79fbf-a585-4d4f-834f-b9fd235f3d62/P17075.pdf
    • Vancouver

      Minari K, Azevedo ÉC, Rodrigues VKT, Batista F, Nascimento AS, Ramos C, Borges JC. Thermodynamic signature of Hsp90 interaction with adenosine nucleotides [Internet]. Abstracts. 2017 ;[citado 2024 jun. 05 ] Available from: https://repositorio.usp.br/directbitstream/8cb79fbf-a585-4d4f-834f-b9fd235f3d62/P17075.pdf
  • Source: Acta Crystallographica F. Unidade: IFSC

    Subjects: CLOROSE VARIEGADA DOS CITROS, DOENÇAS DE PLANTAS, PROTEÍNAS DO CHOQUE TÉRMICO

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      FONSECA, Emanuella Maria Barreto et al. Crystal structure of a small heat-shock protein from Xylella fastidiosa reveals a distinct high-order structure. Acta Crystallographica F, v. 73, p. 222-227, 2017Tradução . . Disponível em: https://doi.org/10.1107/S2053230X17004101. Acesso em: 05 jun. 2024.
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      Fonseca, E. M. B., Scorsato, V., Santos, M. L. dos, Tomazini Júnior, A., Tada, S. F. S., Santos, C. A. dos, et al. (2017). Crystal structure of a small heat-shock protein from Xylella fastidiosa reveals a distinct high-order structure. Acta Crystallographica F, 73, 222-227. doi:10.1107/S2053230X17004101
    • NLM

      Fonseca EMB, Scorsato V, Santos ML dos, Tomazini Júnior A, Tada SFS, Santos CA dos, Toledo MAS de, Souza AP de, Polikarpov I, Aparicio R. Crystal structure of a small heat-shock protein from Xylella fastidiosa reveals a distinct high-order structure [Internet]. Acta Crystallographica F. 2017 ; 73 222-227.[citado 2024 jun. 05 ] Available from: https://doi.org/10.1107/S2053230X17004101
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      Fonseca EMB, Scorsato V, Santos ML dos, Tomazini Júnior A, Tada SFS, Santos CA dos, Toledo MAS de, Souza AP de, Polikarpov I, Aparicio R. Crystal structure of a small heat-shock protein from Xylella fastidiosa reveals a distinct high-order structure [Internet]. Acta Crystallographica F. 2017 ; 73 222-227.[citado 2024 jun. 05 ] Available from: https://doi.org/10.1107/S2053230X17004101
  • Source: Extremophiles. Unidade: IFSC

    Subjects: MICROBIOLOGIA, BIOMASSA, ENZIMAS

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      MANDELLI, F. et al. Thermal adaptation strategies of the extremophile bacterium Thermus filiformis based on multi-omics analysis. Extremophiles, v. 21, n. 4, p. 775-788, 2017Tradução . . Disponível em: https://doi.org/10.1007/s00792-017-0942-2. Acesso em: 05 jun. 2024.
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      Mandelli, F., Couger, M. B., Paixão, D. A. A., Machado, C. B., Carnielli, C. M., Aricetti, J. A., et al. (2017). Thermal adaptation strategies of the extremophile bacterium Thermus filiformis based on multi-omics analysis. Extremophiles, 21( 4), 775-788. doi:10.1007/s00792-017-0942-2
    • NLM

      Mandelli F, Couger MB, Paixão DAA, Machado CB, Carnielli CM, Aricetti JA, Polikarpov I, Prade R, Caldana C, Leme AFP, Mercadante AZ, Riaño-Pachón DM, Squina FM. Thermal adaptation strategies of the extremophile bacterium Thermus filiformis based on multi-omics analysis [Internet]. Extremophiles. 2017 ; 21( 4): 775-788.[citado 2024 jun. 05 ] Available from: https://doi.org/10.1007/s00792-017-0942-2
    • Vancouver

      Mandelli F, Couger MB, Paixão DAA, Machado CB, Carnielli CM, Aricetti JA, Polikarpov I, Prade R, Caldana C, Leme AFP, Mercadante AZ, Riaño-Pachón DM, Squina FM. Thermal adaptation strategies of the extremophile bacterium Thermus filiformis based on multi-omics analysis [Internet]. Extremophiles. 2017 ; 21( 4): 775-788.[citado 2024 jun. 05 ] Available from: https://doi.org/10.1007/s00792-017-0942-2
  • Source: Proteins. Unidade: IFSC

    Subjects: CLOROSE VARIEGADA DOS CITROS, PROTEÍNAS, CRISTALOGRAFIA

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      MACHADO, Agnes Thiane Pereira et al. Conformational variability of the stationary phase survival protein E from Xylella fastidiosa revealed by X-ray crystallography, small-angle X-ray scattering studies, and normal mode analysis. Proteins, v. 85, n. 10, p. 1931-1943, 2017Tradução . . Disponível em: https://doi.org/10.1002/prot.25347. Acesso em: 05 jun. 2024.
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      Machado, A. T. P., Fonseca, E. M. B., Reis, M. A. dos, Saraiva, A. M., Santos, C. A. dos, Toledo, M. A. S. de, et al. (2017). Conformational variability of the stationary phase survival protein E from Xylella fastidiosa revealed by X-ray crystallography, small-angle X-ray scattering studies, and normal mode analysis. Proteins, 85( 10), 1931-1943. doi:10.1002/prot.25347
    • NLM

      Machado ATP, Fonseca EMB, Reis MA dos, Saraiva AM, Santos CA dos, Toledo MAS de, Polikarpov I, Souza AP de, Aparicio R, Iulek J. Conformational variability of the stationary phase survival protein E from Xylella fastidiosa revealed by X-ray crystallography, small-angle X-ray scattering studies, and normal mode analysis [Internet]. Proteins. 2017 ; 85( 10): 1931-1943.[citado 2024 jun. 05 ] Available from: https://doi.org/10.1002/prot.25347
    • Vancouver

      Machado ATP, Fonseca EMB, Reis MA dos, Saraiva AM, Santos CA dos, Toledo MAS de, Polikarpov I, Souza AP de, Aparicio R, Iulek J. Conformational variability of the stationary phase survival protein E from Xylella fastidiosa revealed by X-ray crystallography, small-angle X-ray scattering studies, and normal mode analysis [Internet]. Proteins. 2017 ; 85( 10): 1931-1943.[citado 2024 jun. 05 ] Available from: https://doi.org/10.1002/prot.25347
  • Source: Program Book. Conference titles: Brazilian MRS Meeting. Unidade: IFSC

    Subjects: CELULOSE, ENZIMAS, BIOCOMBUSTÍVEIS

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      RICHENA, Marina et al. Visualizing cellulase action on cellulose substrates. 2016, Anais.. Rio de Janeiro: Sociedade Brasileira de Pesquisa em Materiais - SBPMat, 2016. Disponível em: http://www.eventweb.com.br/xvsbpmat/specific-files/grabFile.php?codigo=B6RT. Acesso em: 05 jun. 2024.
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      Richena, M., Pellegrini, V. de O. A., Polikarpov, I., & Rezende, C. A. de. (2016). Visualizing cellulase action on cellulose substrates. In Program Book. Rio de Janeiro: Sociedade Brasileira de Pesquisa em Materiais - SBPMat. Recuperado de http://www.eventweb.com.br/xvsbpmat/specific-files/grabFile.php?codigo=B6RT
    • NLM

      Richena M, Pellegrini V de OA, Polikarpov I, Rezende CA de. Visualizing cellulase action on cellulose substrates [Internet]. Program Book. 2016 ;[citado 2024 jun. 05 ] Available from: http://www.eventweb.com.br/xvsbpmat/specific-files/grabFile.php?codigo=B6RT
    • Vancouver

      Richena M, Pellegrini V de OA, Polikarpov I, Rezende CA de. Visualizing cellulase action on cellulose substrates [Internet]. Program Book. 2016 ;[citado 2024 jun. 05 ] Available from: http://www.eventweb.com.br/xvsbpmat/specific-files/grabFile.php?codigo=B6RT
  • Source: Abstracts. Conference titles: Annual Meeting of the Brazilian Society for Biochemistry and Molecular Biology - SBBq. Unidade: IFSC

    Subjects: ENZIMAS CELULOLÍTICAS, BIOMATERIAIS

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      LIBERATO, M. V. et al. Molecular characterization of a trimodular family 5 glycoside hydrolase reveals a unique conformational selection mechanism. 2016, Anais.. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular - SBBq, 2016. Disponível em: http://www.sbbq.org.br/arquivos/2016/cd2016/listaresumos.htm. Acesso em: 05 jun. 2024.
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      Liberato, M. V., Silveira, R. L., Prates, E. T., Araujo, E. A., Pellegrini, V. O. A., Camilo, C. M., et al. (2016). Molecular characterization of a trimodular family 5 glycoside hydrolase reveals a unique conformational selection mechanism. In Abstracts. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular - SBBq. Recuperado de http://www.sbbq.org.br/arquivos/2016/cd2016/listaresumos.htm
    • NLM

      Liberato MV, Silveira RL, Prates ET, Araujo EA, Pellegrini VOA, Camilo CM, Kadowaki MA, Neto MO, Popov A, Skaf MS, Polikarpov I. Molecular characterization of a trimodular family 5 glycoside hydrolase reveals a unique conformational selection mechanism [Internet]. Abstracts. 2016 ;[citado 2024 jun. 05 ] Available from: http://www.sbbq.org.br/arquivos/2016/cd2016/listaresumos.htm
    • Vancouver

      Liberato MV, Silveira RL, Prates ET, Araujo EA, Pellegrini VOA, Camilo CM, Kadowaki MA, Neto MO, Popov A, Skaf MS, Polikarpov I. Molecular characterization of a trimodular family 5 glycoside hydrolase reveals a unique conformational selection mechanism [Internet]. Abstracts. 2016 ;[citado 2024 jun. 05 ] Available from: http://www.sbbq.org.br/arquivos/2016/cd2016/listaresumos.htm
  • Source: Biomass and Bioenergy. Unidade: IFSC

    Subjects: BAGAÇOS, BIOMASSA, CANA-DE-AÇÚCAR, ETANOL

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      ZHU, Zongyuan et al. Efficient sugar production from sugarcane bagasse by microwave assisted acid and alkali pretreatment. Biomass and Bioenergy, v. 93, p. 269-278, 2016Tradução . . Disponível em: https://doi.org/10.1016/j.biombioe.2016.06.017. Acesso em: 05 jun. 2024.
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      Zhu, Z., Rezende, C. A., Simister, R., McQueen-Mason, S. J., Macquarrie, D. J., Polikarpov, I., & Gomez, L. D. (2016). Efficient sugar production from sugarcane bagasse by microwave assisted acid and alkali pretreatment. Biomass and Bioenergy, 93, 269-278. doi:10.1016/j.biombioe.2016.06.017
    • NLM

      Zhu Z, Rezende CA, Simister R, McQueen-Mason SJ, Macquarrie DJ, Polikarpov I, Gomez LD. Efficient sugar production from sugarcane bagasse by microwave assisted acid and alkali pretreatment [Internet]. Biomass and Bioenergy. 2016 ; 93 269-278.[citado 2024 jun. 05 ] Available from: https://doi.org/10.1016/j.biombioe.2016.06.017
    • Vancouver

      Zhu Z, Rezende CA, Simister R, McQueen-Mason SJ, Macquarrie DJ, Polikarpov I, Gomez LD. Efficient sugar production from sugarcane bagasse by microwave assisted acid and alkali pretreatment [Internet]. Biomass and Bioenergy. 2016 ; 93 269-278.[citado 2024 jun. 05 ] Available from: https://doi.org/10.1016/j.biombioe.2016.06.017
  • Source: Abstracts Book. Conference titles: Workshop on Second Generation Bioethanol. Unidade: IFSC

    Subjects: ETANOL, BIOCOMBUSTÍVEIS, ENZIMAS HIDROLÍTICAS

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      SILVEIRA, R. L. et al. Molecular characterization of a family 5 glycoside hydrolase. 2016, Anais.. Campinas: Centro Nacional de Pesquisa em Energia e Materiais - CNPEM - Ciência e Tecnologia do Bioetanol - CTBE, 2016. Disponível em: http://pages.cnpem.br/2gbioethanol/wp-content/uploads/sites/25/2014/07/Abstract-Book-Workshop-on-Second-Generation-Bioethanol-2016.pdf. Acesso em: 05 jun. 2024.
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      Silveira, R. L., Liberato, M. V., Prates, E. T., Polikarpov, I., & Skaf, M. S. (2016). Molecular characterization of a family 5 glycoside hydrolase. In Abstracts Book. Campinas: Centro Nacional de Pesquisa em Energia e Materiais - CNPEM - Ciência e Tecnologia do Bioetanol - CTBE. Recuperado de http://pages.cnpem.br/2gbioethanol/wp-content/uploads/sites/25/2014/07/Abstract-Book-Workshop-on-Second-Generation-Bioethanol-2016.pdf
    • NLM

      Silveira RL, Liberato MV, Prates ET, Polikarpov I, Skaf MS. Molecular characterization of a family 5 glycoside hydrolase [Internet]. Abstracts Book. 2016 ;[citado 2024 jun. 05 ] Available from: http://pages.cnpem.br/2gbioethanol/wp-content/uploads/sites/25/2014/07/Abstract-Book-Workshop-on-Second-Generation-Bioethanol-2016.pdf
    • Vancouver

      Silveira RL, Liberato MV, Prates ET, Polikarpov I, Skaf MS. Molecular characterization of a family 5 glycoside hydrolase [Internet]. Abstracts Book. 2016 ;[citado 2024 jun. 05 ] Available from: http://pages.cnpem.br/2gbioethanol/wp-content/uploads/sites/25/2014/07/Abstract-Book-Workshop-on-Second-Generation-Bioethanol-2016.pdf
  • Source: Scientific Reports. Unidade: IFSC

    Subjects: BIOTECNOLOGIA, MICROBIOLOGIA

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      LIBERATO, Marcelo V. et al. Molecular characterization of a family 5 glycoside hydrolase suggests an induced-fit enzymatic mechanism. Scientific Reports, v. 6, p. 23473-1-23473-15 + supplementary information, 2016Tradução . . Disponível em: https://doi.org/10.1038/srep23473. Acesso em: 05 jun. 2024.
    • APA

      Liberato, M. V., Silveira, R. L., Prates, É. T., Araujo, E. A., Pellegrini, V. O. A., Camilo, C. M., et al. (2016). Molecular characterization of a family 5 glycoside hydrolase suggests an induced-fit enzymatic mechanism. Scientific Reports, 6, 23473-1-23473-15 + supplementary information. doi:10.1038/srep23473
    • NLM

      Liberato MV, Silveira RL, Prates ÉT, Araujo EA, Pellegrini VOA, Camilo CM, Kadowaki MA, Neto M de O, Popov A, Skaf MS, Polikarpov I. Molecular characterization of a family 5 glycoside hydrolase suggests an induced-fit enzymatic mechanism [Internet]. Scientific Reports. 2016 ; 6 23473-1-23473-15 + supplementary information.[citado 2024 jun. 05 ] Available from: https://doi.org/10.1038/srep23473
    • Vancouver

      Liberato MV, Silveira RL, Prates ÉT, Araujo EA, Pellegrini VOA, Camilo CM, Kadowaki MA, Neto M de O, Popov A, Skaf MS, Polikarpov I. Molecular characterization of a family 5 glycoside hydrolase suggests an induced-fit enzymatic mechanism [Internet]. Scientific Reports. 2016 ; 6 23473-1-23473-15 + supplementary information.[citado 2024 jun. 05 ] Available from: https://doi.org/10.1038/srep23473
  • Source: Applied Microbiology and Biotechnology. Unidade: IFSC

    Subjects: CELULOSE, TRICHODERMA, BIOCOMBUSTÍVEIS

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      PELLEGRINI, Vanessa O. A. et al. Recombinant Trichoderma harzianum endoglucanase I (Cel7B) is a highly acidic and promiscuous carbohydrate-active enzyme. Applied Microbiology and Biotechnology, v. No 2015, n. 22, p. 9591-9604, 2015Tradução . . Disponível em: https://doi.org/10.1007/s00253-015-6772-1. Acesso em: 05 jun. 2024.
    • APA

      Pellegrini, V. O. A., Serpa, V. I., Godoy, A. S., Camilo, C. M., Bernardes, A., Rezende, C. A., et al. (2015). Recombinant Trichoderma harzianum endoglucanase I (Cel7B) is a highly acidic and promiscuous carbohydrate-active enzyme. Applied Microbiology and Biotechnology, No 2015( 22), 9591-9604. doi:10.1007/s00253-015-6772-1
    • NLM

      Pellegrini VOA, Serpa VI, Godoy AS, Camilo CM, Bernardes A, Rezende CA, Pereira Junior N, Cairo JPLF, Squina FM, Polikarpov I. Recombinant Trichoderma harzianum endoglucanase I (Cel7B) is a highly acidic and promiscuous carbohydrate-active enzyme [Internet]. Applied Microbiology and Biotechnology. 2015 ; No 2015( 22): 9591-9604.[citado 2024 jun. 05 ] Available from: https://doi.org/10.1007/s00253-015-6772-1
    • Vancouver

      Pellegrini VOA, Serpa VI, Godoy AS, Camilo CM, Bernardes A, Rezende CA, Pereira Junior N, Cairo JPLF, Squina FM, Polikarpov I. Recombinant Trichoderma harzianum endoglucanase I (Cel7B) is a highly acidic and promiscuous carbohydrate-active enzyme [Internet]. Applied Microbiology and Biotechnology. 2015 ; No 2015( 22): 9591-9604.[citado 2024 jun. 05 ] Available from: https://doi.org/10.1007/s00253-015-6772-1
  • Source: Industrial Crops and Products. Unidade: IFSC

    Subjects: CANA-DE-AÇÚCAR, EXTRAÇÃO COM FLUÍDO SUPERCRÍTICO, DIÓXIDO DE CARBONO, CERA

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      ATTARD, Thomas M. et al. Sugarcane waste as a valuable source of lipophilic molecules. Industrial Crops and Products, v. 76, p. 95-103, 2015Tradução . . Disponível em: https://doi.org/10.1016/j.indcrop.2015.05.077. Acesso em: 05 jun. 2024.
    • APA

      Attard, T. M., McElroy, C. R., Rezende, C. A., Polikarpov, I., Clark, J. H., & Hunt, A. J. (2015). Sugarcane waste as a valuable source of lipophilic molecules. Industrial Crops and Products, 76, 95-103. doi:10.1016/j.indcrop.2015.05.077
    • NLM

      Attard TM, McElroy CR, Rezende CA, Polikarpov I, Clark JH, Hunt AJ. Sugarcane waste as a valuable source of lipophilic molecules [Internet]. Industrial Crops and Products. 2015 ; 76 95-103.[citado 2024 jun. 05 ] Available from: https://doi.org/10.1016/j.indcrop.2015.05.077
    • Vancouver

      Attard TM, McElroy CR, Rezende CA, Polikarpov I, Clark JH, Hunt AJ. Sugarcane waste as a valuable source of lipophilic molecules [Internet]. Industrial Crops and Products. 2015 ; 76 95-103.[citado 2024 jun. 05 ] Available from: https://doi.org/10.1016/j.indcrop.2015.05.077
  • Source: Biotechnology for Biofuels. Unidade: IFSC

    Subjects: BIOCOMBUSTÍVEIS, CANA-DE-AÇÚCAR, BIOMASSA, RESSONÂNCIA MAGNÉTICA NUCLEAR

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      BERNARDINELLI, Oigres Daniel et al. Quantitative 13C MultiCP solid‑state NMR as a tool for evaluation of cellulose crystallinity index measured directly inside sugarcane biomass. Biotechnology for Biofuels, v. 8, p. 110-1-110-11, 2015Tradução . . Disponível em: https://doi.org/10.1186/s13068-015-0292-1. Acesso em: 05 jun. 2024.
    • APA

      Bernardinelli, O. D., Lima, M. A., Rezende, C. A., Polikarpov, I., & Azevêdo, E. R. de. (2015). Quantitative 13C MultiCP solid‑state NMR as a tool for evaluation of cellulose crystallinity index measured directly inside sugarcane biomass. Biotechnology for Biofuels, 8, 110-1-110-11. doi:10.1186/s13068-015-0292-1
    • NLM

      Bernardinelli OD, Lima MA, Rezende CA, Polikarpov I, Azevêdo ER de. Quantitative 13C MultiCP solid‑state NMR as a tool for evaluation of cellulose crystallinity index measured directly inside sugarcane biomass [Internet]. Biotechnology for Biofuels. 2015 ; 8 110-1-110-11.[citado 2024 jun. 05 ] Available from: https://doi.org/10.1186/s13068-015-0292-1
    • Vancouver

      Bernardinelli OD, Lima MA, Rezende CA, Polikarpov I, Azevêdo ER de. Quantitative 13C MultiCP solid‑state NMR as a tool for evaluation of cellulose crystallinity index measured directly inside sugarcane biomass [Internet]. Biotechnology for Biofuels. 2015 ; 8 110-1-110-11.[citado 2024 jun. 05 ] Available from: https://doi.org/10.1186/s13068-015-0292-1
  • Source: Biotechnology for Biofuels. Unidades: ESALQ, IFSC

    Subjects: BIOCOMBUSTÍVEIS, BAGAÇOS, CANA-DE-AÇÚCAR

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      LIMA, Marisa A. et al. Evaluating the composition and processing potential of novel sources of Brazilian biomass for sustainable biorenewables production. Biotechnology for Biofuels, v. 7, n. Ja 2014, p. 10-1-10-19, 2014Tradução . . Disponível em: https://doi.org/10.1186/1754-6834-7-10. Acesso em: 05 jun. 2024.
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      Lima, M. A., Gomez, L. D., Steele-King, C. G., Simister, R., Bernardinelli, O. D., Carvalho, M. A., et al. (2014). Evaluating the composition and processing potential of novel sources of Brazilian biomass for sustainable biorenewables production. Biotechnology for Biofuels, 7( Ja 2014), 10-1-10-19. doi:10.1186/1754-6834-7-10
    • NLM

      Lima MA, Gomez LD, Steele-King CG, Simister R, Bernardinelli OD, Carvalho MA, Rezende CA, Labate CA, Azevêdo ER de, McQueen-Mason SJ, Polikarpov I. Evaluating the composition and processing potential of novel sources of Brazilian biomass for sustainable biorenewables production [Internet]. Biotechnology for Biofuels. 2014 ; 7( Ja 2014): 10-1-10-19.[citado 2024 jun. 05 ] Available from: https://doi.org/10.1186/1754-6834-7-10
    • Vancouver

      Lima MA, Gomez LD, Steele-King CG, Simister R, Bernardinelli OD, Carvalho MA, Rezende CA, Labate CA, Azevêdo ER de, McQueen-Mason SJ, Polikarpov I. Evaluating the composition and processing potential of novel sources of Brazilian biomass for sustainable biorenewables production [Internet]. Biotechnology for Biofuels. 2014 ; 7( Ja 2014): 10-1-10-19.[citado 2024 jun. 05 ] Available from: https://doi.org/10.1186/1754-6834-7-10
  • Source: FEBS Journal. Unidade: IFSC

    Subjects: TRICHODERMA (ESTUDO), ENZIMAS, HIDRÓLISE

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      NASCIMENTO, Alessandro Silva et al. Insights into the structure and function of fungal β-mannosidases from glycoside hydrolase family 2 based on multiple crystal structures of the Trichoderma harzianum enzyme. FEBS Journal, v. 281, n. 18, p. 4165-4178, 2014Tradução . . Disponível em: https://doi.org/10.1111/febs.12894. Acesso em: 05 jun. 2024.
    • APA

      Nascimento, A. S., Muniz, J. R. C., Aparício, R., Golubev, A. M., & Polikarpov, I. (2014). Insights into the structure and function of fungal β-mannosidases from glycoside hydrolase family 2 based on multiple crystal structures of the Trichoderma harzianum enzyme. FEBS Journal, 281( 18), 4165-4178. doi:10.1111/febs.12894
    • NLM

      Nascimento AS, Muniz JRC, Aparício R, Golubev AM, Polikarpov I. Insights into the structure and function of fungal β-mannosidases from glycoside hydrolase family 2 based on multiple crystal structures of the Trichoderma harzianum enzyme [Internet]. FEBS Journal. 2014 ; 281( 18): 4165-4178.[citado 2024 jun. 05 ] Available from: https://doi.org/10.1111/febs.12894
    • Vancouver

      Nascimento AS, Muniz JRC, Aparício R, Golubev AM, Polikarpov I. Insights into the structure and function of fungal β-mannosidases from glycoside hydrolase family 2 based on multiple crystal structures of the Trichoderma harzianum enzyme [Internet]. FEBS Journal. 2014 ; 281( 18): 4165-4178.[citado 2024 jun. 05 ] Available from: https://doi.org/10.1111/febs.12894

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