Filtros : "Indexado no Science Citation Index" "Polikarpov, Igor" Removidos: "IFSC011" "AULER JUNIOR, JOSE OTAVIO COSTA" "ac" Limpar

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  • Fonte: Journal of Applied Animal Research. Unidade: IFSC

    Assuntos: BAGAÇOS, BIOMASSA, CANA-DE-AÇÚCAR

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      AHMADI, Farhad et al. Pre-treatment of sugarcane bagasse with a combination of sodium hydroxide and lime for improving the ruminal degradability: optimization of process parameters using response surface methodology. Journal of Applied Animal Research, v. 44 n. 1, p. 287-296, 2016Tradução . . Disponível em: https://doi.org/10.1080/09712119.2015.1031783. Acesso em: 05 nov. 2024.
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      Ahmadi, F., Zamiri, M. J., Khorvash, M., Ziaee, E., & Polikarpov, I. (2016). Pre-treatment of sugarcane bagasse with a combination of sodium hydroxide and lime for improving the ruminal degradability: optimization of process parameters using response surface methodology. Journal of Applied Animal Research, 44 n. 1, 287-296. doi:10.1080/09712119.2015.1031783
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      Ahmadi F, Zamiri MJ, Khorvash M, Ziaee E, Polikarpov I. Pre-treatment of sugarcane bagasse with a combination of sodium hydroxide and lime for improving the ruminal degradability: optimization of process parameters using response surface methodology [Internet]. Journal of Applied Animal Research. 2016 ; 44 n. 1 287-296.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1080/09712119.2015.1031783
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      Ahmadi F, Zamiri MJ, Khorvash M, Ziaee E, Polikarpov I. Pre-treatment of sugarcane bagasse with a combination of sodium hydroxide and lime for improving the ruminal degradability: optimization of process parameters using response surface methodology [Internet]. Journal of Applied Animal Research. 2016 ; 44 n. 1 287-296.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1080/09712119.2015.1031783
  • Fonte: Acta Crystallographica F. Unidade: IFSC

    Assuntos: CANA-DE-AÇÚCAR, RAIOS X, BIOCOMBUSTÍVEIS

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      GODOY, Andre S. et al. Crystal structure of a putative exo-b-1,3-galactanase from Bifidobacterium bifidum S17. Acta Crystallographica F, v. 72, p. 288-293, 2016Tradução . . Disponível em: https://doi.org/10.1107/S2053230X16003617. Acesso em: 05 nov. 2024.
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      Godoy, A. S., Lima, M. Z. T., Camilo, C. M., & Polikarpov, I. (2016). Crystal structure of a putative exo-b-1,3-galactanase from Bifidobacterium bifidum S17. Acta Crystallographica F, 72, 288-293. doi:10.1107/S2053230X16003617
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      Godoy AS, Lima MZT, Camilo CM, Polikarpov I. Crystal structure of a putative exo-b-1,3-galactanase from Bifidobacterium bifidum S17 [Internet]. Acta Crystallographica F. 2016 ; 72 288-293.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1107/S2053230X16003617
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      Godoy AS, Lima MZT, Camilo CM, Polikarpov I. Crystal structure of a putative exo-b-1,3-galactanase from Bifidobacterium bifidum S17 [Internet]. Acta Crystallographica F. 2016 ; 72 288-293.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1107/S2053230X16003617
  • Fonte: Enzyme and Microbial Technology. Unidade: IFSC

    Assuntos: ENZIMAS, HIDRÓLISE, ENZIMAS HIDROLÍTICAS

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      SILVA, Viviam M. et al. Non-productive adsorption of bacterial β-glucosidases on lignins is electrostatically modulated and depends on the presence offibronection type III-like domain. Enzyme and Microbial Technology, v. 87-88, p. 1-8, 2016Tradução . . Disponível em: https://doi.org/10.1016/j.enzmictec.2016.02.007. Acesso em: 05 nov. 2024.
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      Silva, V. M., Souza, A. S., Negrão, D. R., Polikarpov, I., Squina, F. M., Oliveira Neto, M. de, et al. (2016). Non-productive adsorption of bacterial β-glucosidases on lignins is electrostatically modulated and depends on the presence offibronection type III-like domain. Enzyme and Microbial Technology, 87-88, 1-8. doi:10.1016/j.enzmictec.2016.02.007
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      Silva VM, Souza AS, Negrão DR, Polikarpov I, Squina FM, Oliveira Neto M de, Muniz JRC, Garcia W. Non-productive adsorption of bacterial β-glucosidases on lignins is electrostatically modulated and depends on the presence offibronection type III-like domain [Internet]. Enzyme and Microbial Technology. 2016 ; 87-88 1-8.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1016/j.enzmictec.2016.02.007
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      Silva VM, Souza AS, Negrão DR, Polikarpov I, Squina FM, Oliveira Neto M de, Muniz JRC, Garcia W. Non-productive adsorption of bacterial β-glucosidases on lignins is electrostatically modulated and depends on the presence offibronection type III-like domain [Internet]. Enzyme and Microbial Technology. 2016 ; 87-88 1-8.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1016/j.enzmictec.2016.02.007
  • Fonte: Scientific Reports. Unidade: IFSC

    Assuntos: 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 nov. 2024.
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      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
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      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 nov. 05 ] Available from: https://doi.org/10.1038/srep23473
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      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 nov. 05 ] Available from: https://doi.org/10.1038/srep23473
  • Fonte: Applied Microbiology and Biotechnology. Unidade: IFSC

    Assuntos: 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 nov. 2024.
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      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
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      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 nov. 05 ] Available from: https://doi.org/10.1007/s00253-015-6772-1
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      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 nov. 05 ] Available from: https://doi.org/10.1007/s00253-015-6772-1
  • Fonte: Biotechnology Letters. Unidade: IFSC

    Assuntos: XANTHOMONAS, CELULOSE, BIOCOMBUSTÍVEIS

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      TOMAZINI, Atílio Júnior et al. Xanthomonas campestris expansin-like X domain is a structurally disordered beta-sheet macromolecule capable of synergistically enhancing enzymatic efficiency of cellulose hydrolysis. Biotechnology Letters, v. 37, n. 12, p. 2419-2426, 2015Tradução . . Disponível em: https://doi.org/10.1007/s10529-015-1927-9. Acesso em: 05 nov. 2024.
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      Tomazini, A. J., Dolce, L. G., Oliveira Neto, M. de, & Polikarpov, I. (2015). Xanthomonas campestris expansin-like X domain is a structurally disordered beta-sheet macromolecule capable of synergistically enhancing enzymatic efficiency of cellulose hydrolysis. Biotechnology Letters, 37( 12), 2419-2426. doi:10.1007/s10529-015-1927-9
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      Tomazini AJ, Dolce LG, Oliveira Neto M de, Polikarpov I. Xanthomonas campestris expansin-like X domain is a structurally disordered beta-sheet macromolecule capable of synergistically enhancing enzymatic efficiency of cellulose hydrolysis [Internet]. Biotechnology Letters. 2015 ; 37( 12): 2419-2426.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1007/s10529-015-1927-9
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      Tomazini AJ, Dolce LG, Oliveira Neto M de, Polikarpov I. Xanthomonas campestris expansin-like X domain is a structurally disordered beta-sheet macromolecule capable of synergistically enhancing enzymatic efficiency of cellulose hydrolysis [Internet]. Biotechnology Letters. 2015 ; 37( 12): 2419-2426.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1007/s10529-015-1927-9
  • Fonte: Trends in Biochemical Sciences. Unidade: IFSC

    Assuntos: BIOTECNOLOGIA, DOENÇAS METABÓLICAS, RECEPTORES

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      RASTINEJAD, Fraydoon e OLLENDORFF, Vincent e POLIKARPOV, Igor. Response to Moras et al. Trends in Biochemical Sciences. Oxford: Instituto de Física de São Carlos, Universidade de São Paulo. Disponível em: https://doi.org/10.1016/j.tibs.2015.03.008. Acesso em: 05 nov. 2024. , 2015
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      Rastinejad, F., Ollendorff, V., & Polikarpov, I. (2015). Response to Moras et al. Trends in Biochemical Sciences. Oxford: Instituto de Física de São Carlos, Universidade de São Paulo. doi:10.1016/j.tibs.2015.03.008
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      Rastinejad F, Ollendorff V, Polikarpov I. Response to Moras et al. [Internet]. Trends in Biochemical Sciences. 2015 ; 40( 6): 290-292.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1016/j.tibs.2015.03.008
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      Rastinejad F, Ollendorff V, Polikarpov I. Response to Moras et al. [Internet]. Trends in Biochemical Sciences. 2015 ; 40( 6): 290-292.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1016/j.tibs.2015.03.008
  • Fonte: Journal of Computational Biology. Unidade: IFSC

    Assuntos: GENÔMICA, PRIMERS DO DNA

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      CAMILO, Cesar M. et al. HTP-oligodesigner: an online primer design tool for high-throughput gene cloning and site-directed mutagenesis. Journal of Computational Biology, v. 23, n. 1, p. 27-29, 2015Tradução . . Disponível em: https://doi.org/10.1089/cmb.2015.0148. Acesso em: 05 nov. 2024.
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      Camilo, C. M., Lima, G., Maluf, F. V., Guido, R. V. C., & Polikarpov, I. (2015). HTP-oligodesigner: an online primer design tool for high-throughput gene cloning and site-directed mutagenesis. Journal of Computational Biology, 23( 1), 27-29. doi:10.1089/cmb.2015.0148
    • NLM

      Camilo CM, Lima G, Maluf FV, Guido RVC, Polikarpov I. HTP-oligodesigner: an online primer design tool for high-throughput gene cloning and site-directed mutagenesis [Internet]. Journal of Computational Biology. 2015 ; 23( 1): 27-29.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1089/cmb.2015.0148
    • Vancouver

      Camilo CM, Lima G, Maluf FV, Guido RVC, Polikarpov I. HTP-oligodesigner: an online primer design tool for high-throughput gene cloning and site-directed mutagenesis [Internet]. Journal of Computational Biology. 2015 ; 23( 1): 27-29.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1089/cmb.2015.0148
  • Fonte: Biochimie. Unidade: IFSC

    Assuntos: PEROXIDASE, PALMEIRAS, CRISTALOGRAFIA

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      BERNARDES, Amanda et al. Crystal structure analysis of peroxidase from the palm tree Chamaerops excelsa. Biochimie, v. 111, p. 58-69, 2015Tradução . . Disponível em: https://doi.org/10.1016/j.biochi.2015.01.014. Acesso em: 05 nov. 2024.
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      Bernardes, A., Textor, L. C., Santos, J. C., Cuadrado, N. H., Kostetsky, E. Y., Roig, M. G., et al. (2015). Crystal structure analysis of peroxidase from the palm tree Chamaerops excelsa. Biochimie, 111, 58-69. doi:10.1016/j.biochi.2015.01.014
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      Bernardes A, Textor LC, Santos JC, Cuadrado NH, Kostetsky EY, Roig MG, Bavro VN, Muniz JRC, Shnyrov VL, Polikarpov I. Crystal structure analysis of peroxidase from the palm tree Chamaerops excelsa [Internet]. Biochimie. 2015 ; 111 58-69.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1016/j.biochi.2015.01.014
    • Vancouver

      Bernardes A, Textor LC, Santos JC, Cuadrado NH, Kostetsky EY, Roig MG, Bavro VN, Muniz JRC, Shnyrov VL, Polikarpov I. Crystal structure analysis of peroxidase from the palm tree Chamaerops excelsa [Internet]. Biochimie. 2015 ; 111 58-69.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1016/j.biochi.2015.01.014
  • Fonte: Acta Crystallographica F. Unidade: IFSC

    Assuntos: CANA-DE-AÇÚCAR, RAIOS X, BIOCOMBUSTÍVEIS

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      CAMPOS, B. M. et al. Cloning, purification, crystallization and preliminary X-ray studies of a carbohydrate-binding module from family 64 (StX). Acta Crystallographica F, v. 71, p. 311-314, 2015Tradução . . Disponível em: https://doi.org/10.1107/S2053230X15002198. Acesso em: 05 nov. 2024.
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      Campos, B. M., Liberato, M. V., Polikarpov, I., Zeri, A. C. M., & Squina, F. M. (2015). Cloning, purification, crystallization and preliminary X-ray studies of a carbohydrate-binding module from family 64 (StX). Acta Crystallographica F, 71, 311-314. doi:10.1107/S2053230X15002198
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      Campos BM, Liberato MV, Polikarpov I, Zeri ACM, Squina FM. Cloning, purification, crystallization and preliminary X-ray studies of a carbohydrate-binding module from family 64 (StX) [Internet]. Acta Crystallographica F. 2015 ; 71 311-314.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1107/S2053230X15002198
    • Vancouver

      Campos BM, Liberato MV, Polikarpov I, Zeri ACM, Squina FM. Cloning, purification, crystallization and preliminary X-ray studies of a carbohydrate-binding module from family 64 (StX) [Internet]. Acta Crystallographica F. 2015 ; 71 311-314.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1107/S2053230X15002198
  • Fonte: Industrial Crops and Products. Unidade: IFSC

    Assuntos: 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 nov. 2024.
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      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
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      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 nov. 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 nov. 05 ] Available from: https://doi.org/10.1016/j.indcrop.2015.05.077
  • Fonte: Trends in Biochemical Sciences. Unidade: IFSC

    Assuntos: RAIOS X, CRISTALOGRAFIA

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      RASTINEJAD, Fraydoon e OLLENDORFF, Vincent e POLIKARPOV, Igor. Nuclear receptor full-length architectures: confronting myth and illusion with high resolution. Trends in Biochemical Sciences, v. 40, n. Ja 2015, p. 16-24, 2015Tradução . . Disponível em: https://doi.org/10.1016/j.tibs.2014.10.011. Acesso em: 05 nov. 2024.
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      Rastinejad, F., Ollendorff, V., & Polikarpov, I. (2015). Nuclear receptor full-length architectures: confronting myth and illusion with high resolution. Trends in Biochemical Sciences, 40( Ja 2015), 16-24. doi:10.1016/j.tibs.2014.10.011
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      Rastinejad F, Ollendorff V, Polikarpov I. Nuclear receptor full-length architectures: confronting myth and illusion with high resolution [Internet]. Trends in Biochemical Sciences. 2015 ; 40( Ja 2015): 16-24.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1016/j.tibs.2014.10.011
    • Vancouver

      Rastinejad F, Ollendorff V, Polikarpov I. Nuclear receptor full-length architectures: confronting myth and illusion with high resolution [Internet]. Trends in Biochemical Sciences. 2015 ; 40( Ja 2015): 16-24.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1016/j.tibs.2014.10.011
  • Fonte: Applied Biochemistry and Biotechnology. Unidade: IFSC

    Assuntos: CANA-DE-AÇÚCAR, ENZIMAS HIDROLÍTICAS

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      ALVAREZ, Thabata Maria et al. A novel member of GH16 family derived from sugarcane soil metagenome. Applied Biochemistry and Biotechnology, v. 177, n. 2, p. 304-317, 2015Tradução . . Disponível em: https://doi.org/10.1007/s12010-015-1743-7. Acesso em: 05 nov. 2024.
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      Alvarez, T. M., Liberato, M. V., Cairo, J. P. L. F., Paixão, D. A. A., Campos, B. M., Ferreira, M. R., et al. (2015). A novel member of GH16 family derived from sugarcane soil metagenome. Applied Biochemistry and Biotechnology, 177( 2), 304-317. doi:10.1007/s12010-015-1743-7
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      Alvarez TM, Liberato MV, Cairo JPLF, Paixão DAA, Campos BM, Ferreira MR, Almeida RF, Pereira IO, Bernardes A, Ematsu GCG, Chinaglia M, Polikarpov I, Oliveira Neto M de, Squina FM. A novel member of GH16 family derived from sugarcane soil metagenome [Internet]. Applied Biochemistry and Biotechnology. 2015 ; 177( 2): 304-317.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1007/s12010-015-1743-7
    • Vancouver

      Alvarez TM, Liberato MV, Cairo JPLF, Paixão DAA, Campos BM, Ferreira MR, Almeida RF, Pereira IO, Bernardes A, Ematsu GCG, Chinaglia M, Polikarpov I, Oliveira Neto M de, Squina FM. A novel member of GH16 family derived from sugarcane soil metagenome [Internet]. Applied Biochemistry and Biotechnology. 2015 ; 177( 2): 304-317.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1007/s12010-015-1743-7
  • Fonte: Biotechnology for Biofuels. Unidade: IFSC

    Assuntos: 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 nov. 2024.
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      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
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      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 nov. 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 nov. 05 ] Available from: https://doi.org/10.1186/s13068-015-0292-1
  • Fonte: Waste and Biomass Valorization. Unidade: IFSC

    Assuntos: PEROXIDASE, PALMEIRAS, CRISTALOGRAFIA

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      RAD, Abbas Rajaee et al. Combination of sodium hydroxide and lime as a pretreatment for conversion of date palm leaves into a promising ruminant feed: an optimization approach. Waste and Biomass Valorization, v. 6, n. 2, p. 243-252, 2015Tradução . . Disponível em: https://doi.org/10.1007/s12649-014-9340-5. Acesso em: 05 nov. 2024.
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      Rad, A. R., Ahmadi, F., Mohammadabadi, T., Ziaee , E., & Polikarpov, I. (2015). Combination of sodium hydroxide and lime as a pretreatment for conversion of date palm leaves into a promising ruminant feed: an optimization approach. Waste and Biomass Valorization, 6( 2), 243-252. doi:10.1007/s12649-014-9340-5
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      Rad AR, Ahmadi F, Mohammadabadi T, Ziaee E, Polikarpov I. Combination of sodium hydroxide and lime as a pretreatment for conversion of date palm leaves into a promising ruminant feed: an optimization approach [Internet]. Waste and Biomass Valorization. 2015 ; 6( 2): 243-252.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1007/s12649-014-9340-5
    • Vancouver

      Rad AR, Ahmadi F, Mohammadabadi T, Ziaee E, Polikarpov I. Combination of sodium hydroxide and lime as a pretreatment for conversion of date palm leaves into a promising ruminant feed: an optimization approach [Internet]. Waste and Biomass Valorization. 2015 ; 6( 2): 243-252.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1007/s12649-014-9340-5
  • Fonte: Molecular Biotechnology. Unidade: IFSC

    Assuntos: BIOMASSA, ENZIMAS HIDROLÍTICAS

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    • ABNT

      KADOWAKI, Marco Antonio Seiki et al. Functional characterization and low-resolution structure of an endoglucanase Cel45A from the filamentous fungus Neurospora crassa OR74A: thermostable enzyme with high activity toward lichenan and b-glucan. Molecular Biotechnology, v. 57, n. 6, p. 574-588, 2015Tradução . . Disponível em: https://doi.org/10.1007/s12033-015-9851-8. Acesso em: 05 nov. 2024.
    • APA

      Kadowaki, M. A. S., Camilo, C. M., Muniz, A. B., & Polikarpov, I. (2015). Functional characterization and low-resolution structure of an endoglucanase Cel45A from the filamentous fungus Neurospora crassa OR74A: thermostable enzyme with high activity toward lichenan and b-glucan. Molecular Biotechnology, 57( 6), 574-588. doi:10.1007/s12033-015-9851-8
    • NLM

      Kadowaki MAS, Camilo CM, Muniz AB, Polikarpov I. Functional characterization and low-resolution structure of an endoglucanase Cel45A from the filamentous fungus Neurospora crassa OR74A: thermostable enzyme with high activity toward lichenan and b-glucan [Internet]. Molecular Biotechnology. 2015 ; 57( 6): 574-588.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1007/s12033-015-9851-8
    • Vancouver

      Kadowaki MAS, Camilo CM, Muniz AB, Polikarpov I. Functional characterization and low-resolution structure of an endoglucanase Cel45A from the filamentous fungus Neurospora crassa OR74A: thermostable enzyme with high activity toward lichenan and b-glucan [Internet]. Molecular Biotechnology. 2015 ; 57( 6): 574-588.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1007/s12033-015-9851-8
  • Fonte: Molecular Endocrinology. Unidade: IFSC

    Assuntos: BIOTECNOLOGIA, DOENÇAS (TRATAMENTO)

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      FATTORI, Juliana et al. RXR agonist modulates TR: corepressor dissociation upon 9-cis retinoic acid treatment. Molecular Endocrinology, v. 29, n. 2, p. 258-273, 2015Tradução . . Disponível em: https://doi.org/10.1210/me.2014-125. Acesso em: 05 nov. 2024.
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      Fattori, J., Campos, J. L. O., Doratioto, T. R., Assis, L. M., Vitorino, M. T., Polikarpov, I., & Xavier-Neto, J. (2015). RXR agonist modulates TR: corepressor dissociation upon 9-cis retinoic acid treatment. Molecular Endocrinology, 29( 2), 258-273. doi:10.1210/me.2014-125
    • NLM

      Fattori J, Campos JLO, Doratioto TR, Assis LM, Vitorino MT, Polikarpov I, Xavier-Neto J. RXR agonist modulates TR: corepressor dissociation upon 9-cis retinoic acid treatment [Internet]. Molecular Endocrinology. 2015 ; 29( 2): 258-273.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1210/me.2014-125
    • Vancouver

      Fattori J, Campos JLO, Doratioto TR, Assis LM, Vitorino MT, Polikarpov I, Xavier-Neto J. RXR agonist modulates TR: corepressor dissociation upon 9-cis retinoic acid treatment [Internet]. Molecular Endocrinology. 2015 ; 29( 2): 258-273.[citado 2024 nov. 05 ] Available from: https://doi.org/10.1210/me.2014-125
  • Fonte: Journal of Structural Biology. Unidade: IFSC

    Assuntos: 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: 05 nov. 2024.
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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
    • NLM

      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 2024 nov. 05 ] 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 2024 nov. 05 ] Available from: https://doi.org/10.1016/j.jsb.2015.07.006

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