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  • Source: Biotechnology for Biofuels. Unidade: IFSC

    Subjects: BIOCOMBUSTÍVEIS, BAGAÇOS, CANA-DE-AÇÚCAR

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      TSUCHIDA, Jefferson Esquina et al. Nuclear magnetic resonance investigation of water accessibility in cellulose of pretreated sugarcane bagasse. Biotechnology for Biofuels, v. 7, p. 127-1-127-13, 2014Tradução . . Disponível em: https://doi.org/10.1186/s13068-014-0127-5. Acesso em: 04 jun. 2024.
    • APA

      Tsuchida, J. E., Rezende, C. A., Oliveira-Silva, R. de, Lima, M. A., D'Eurydice, M. N., Polikarpov, I., & Bonagamba, T. J. (2014). Nuclear magnetic resonance investigation of water accessibility in cellulose of pretreated sugarcane bagasse. Biotechnology for Biofuels, 7, 127-1-127-13. doi:10.1186/s13068-014-0127-5
    • NLM

      Tsuchida JE, Rezende CA, Oliveira-Silva R de, Lima MA, D'Eurydice MN, Polikarpov I, Bonagamba TJ. Nuclear magnetic resonance investigation of water accessibility in cellulose of pretreated sugarcane bagasse [Internet]. Biotechnology for Biofuels. 2014 ; 7 127-1-127-13.[citado 2024 jun. 04 ] Available from: https://doi.org/10.1186/s13068-014-0127-5
    • Vancouver

      Tsuchida JE, Rezende CA, Oliveira-Silva R de, Lima MA, D'Eurydice MN, Polikarpov I, Bonagamba TJ. Nuclear magnetic resonance investigation of water accessibility in cellulose of pretreated sugarcane bagasse [Internet]. Biotechnology for Biofuels. 2014 ; 7 127-1-127-13.[citado 2024 jun. 04 ] Available from: https://doi.org/10.1186/s13068-014-0127-5
  • Source: Biocatalysis and Biotransformation. Unidade: IFSC

    Subjects: ENZIMAS, DIFRAÇÃO POR RAIOS X, BIOMASSA, ASPERGILLUS (ESTUDO)

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      TONELOTTO, Mariana et al. Isolation and characterization of a β-galactosidase from a new Amazon forest strain of Aspergillus niger as a potential accessory enzyme for biomass conversion. Biocatalysis and Biotransformation, v. 32, n. 1, p. 13-22, 2014Tradução . . Disponível em: https://doi.org/10.3109/10242422.2013.801018. Acesso em: 04 jun. 2024.
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      Tonelotto, M., Pirota, R. D. P. B., Delabona, P. da S., Barros, G. de O. F., Golubev, A. M., Polikarpov, I., & Farinas, C. S. (2014). Isolation and characterization of a β-galactosidase from a new Amazon forest strain of Aspergillus niger as a potential accessory enzyme for biomass conversion. Biocatalysis and Biotransformation, 32( 1), 13-22. doi:10.3109/10242422.2013.801018
    • NLM

      Tonelotto M, Pirota RDPB, Delabona P da S, Barros G de OF, Golubev AM, Polikarpov I, Farinas CS. Isolation and characterization of a β-galactosidase from a new Amazon forest strain of Aspergillus niger as a potential accessory enzyme for biomass conversion [Internet]. Biocatalysis and Biotransformation. 2014 ; 32( 1): 13-22.[citado 2024 jun. 04 ] Available from: https://doi.org/10.3109/10242422.2013.801018
    • Vancouver

      Tonelotto M, Pirota RDPB, Delabona P da S, Barros G de OF, Golubev AM, Polikarpov I, Farinas CS. Isolation and characterization of a β-galactosidase from a new Amazon forest strain of Aspergillus niger as a potential accessory enzyme for biomass conversion [Internet]. Biocatalysis and Biotransformation. 2014 ; 32( 1): 13-22.[citado 2024 jun. 04 ] Available from: https://doi.org/10.3109/10242422.2013.801018
  • Source: Biotechnology for Biofuels. Unidade: IFSC

    Subjects: CANA-DE-AÇÚCAR, BAGAÇOS, BIOCOMBUSTÍVEIS

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      CHANDEL, Anuj K. et al. Multi-scale structural and chemical analysis of sugarcane bagasse in the process of sequential acid-base pretreatment and ethanol production by Scheffersomyces shehatae and Saccharomyces cerevisiae. Biotechnology for Biofuels, v. 7, p. 63-1-63-17, 2014Tradução . . Disponível em: https://doi.org/10.1186/1754-6834-7-63. Acesso em: 04 jun. 2024.
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      Chandel, A. K., Antunes, F. A. F., Anjos, V., Bell, M. J. V., Rodrigues, L. N., Polikarpov, I., et al. (2014). Multi-scale structural and chemical analysis of sugarcane bagasse in the process of sequential acid-base pretreatment and ethanol production by Scheffersomyces shehatae and Saccharomyces cerevisiae. Biotechnology for Biofuels, 7, 63-1-63-17. doi:10.1186/1754-6834-7-63
    • NLM

      Chandel AK, Antunes FAF, Anjos V, Bell MJV, Rodrigues LN, Polikarpov I, Azevêdo ER de, Bernardinelli OD, Rosa CA, Pagnocca FC, Silva SS. Multi-scale structural and chemical analysis of sugarcane bagasse in the process of sequential acid-base pretreatment and ethanol production by Scheffersomyces shehatae and Saccharomyces cerevisiae [Internet]. Biotechnology for Biofuels. 2014 ; 7 63-1-63-17.[citado 2024 jun. 04 ] Available from: https://doi.org/10.1186/1754-6834-7-63
    • Vancouver

      Chandel AK, Antunes FAF, Anjos V, Bell MJV, Rodrigues LN, Polikarpov I, Azevêdo ER de, Bernardinelli OD, Rosa CA, Pagnocca FC, Silva SS. Multi-scale structural and chemical analysis of sugarcane bagasse in the process of sequential acid-base pretreatment and ethanol production by Scheffersomyces shehatae and Saccharomyces cerevisiae [Internet]. Biotechnology for Biofuels. 2014 ; 7 63-1-63-17.[citado 2024 jun. 04 ] Available from: https://doi.org/10.1186/1754-6834-7-63
  • Source: Acta Crystallographica F. Unidade: IFSC

    Subjects: CRISTALOGRAFIA, ASPERGILLUS, ENZIMAS (ESTUDO)

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      SEGATO, Fernando et al. Expression, purification, crystallization and preliminary X-ray diffraction analysis of Aspergillus terreus endo-β-1,4-glucanase from glycoside hydrolase family 12. Acta Crystallographica F, v. 70, p. 267-270, 2014Tradução . . Disponível em: https://doi.org/10.1107/S2053230X13034936. Acesso em: 04 jun. 2024.
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      Segato, F., Berto, G. L., Araújo, E. A. de, Muniz, J. R. C., & Polikarpov, I. (2014). Expression, purification, crystallization and preliminary X-ray diffraction analysis of Aspergillus terreus endo-β-1,4-glucanase from glycoside hydrolase family 12. Acta Crystallographica F, 70, 267-270. doi:10.1107/S2053230X13034936
    • NLM

      Segato F, Berto GL, Araújo EA de, Muniz JRC, Polikarpov I. Expression, purification, crystallization and preliminary X-ray diffraction analysis of Aspergillus terreus endo-β-1,4-glucanase from glycoside hydrolase family 12 [Internet]. Acta Crystallographica F. 2014 ; 70 267-270.[citado 2024 jun. 04 ] Available from: https://doi.org/10.1107/S2053230X13034936
    • Vancouver

      Segato F, Berto GL, Araújo EA de, Muniz JRC, Polikarpov I. Expression, purification, crystallization and preliminary X-ray diffraction analysis of Aspergillus terreus endo-β-1,4-glucanase from glycoside hydrolase family 12 [Internet]. Acta Crystallographica F. 2014 ; 70 267-270.[citado 2024 jun. 04 ] Available from: https://doi.org/10.1107/S2053230X13034936
  • 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: 04 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. 04 ] 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. 04 ] Available from: https://doi.org/10.1186/1754-6834-7-10
  • Source: PLOS ONE. Unidades: IFSC, IQ

    Subjects: ENZIMAS (ESTUDO), PROTEÍNAS, AMINOÁCIDOS

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      TAMAKI, Fábio K. et al. Sets of covariant residues modulate the activity and thermal stability of GH1 β-glucosidases. PLOS ONE, v. 9, n. 5, p. e96627-1-e96627-8, 2014Tradução . . Disponível em: https://doi.org/10.1371/journal.pone.0096627. Acesso em: 04 jun. 2024.
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      Tamaki, F. K., Textor, L. C., Polikarpov, I., & Marana, S. R. (2014). Sets of covariant residues modulate the activity and thermal stability of GH1 β-glucosidases. PLOS ONE, 9( 5), e96627-1-e96627-8. doi:10.1371/journal.pone.0096627
    • NLM

      Tamaki FK, Textor LC, Polikarpov I, Marana SR. Sets of covariant residues modulate the activity and thermal stability of GH1 β-glucosidases [Internet]. PLOS ONE. 2014 ; 9( 5): e96627-1-e96627-8.[citado 2024 jun. 04 ] Available from: https://doi.org/10.1371/journal.pone.0096627
    • Vancouver

      Tamaki FK, Textor LC, Polikarpov I, Marana SR. Sets of covariant residues modulate the activity and thermal stability of GH1 β-glucosidases [Internet]. PLOS ONE. 2014 ; 9( 5): e96627-1-e96627-8.[citado 2024 jun. 04 ] Available from: https://doi.org/10.1371/journal.pone.0096627
  • 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: 04 jun. 2024.
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      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. 04 ] 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. 04 ] Available from: https://doi.org/10.1111/febs.12894
  • Source: Materials. Unidade: IFSC

    Subjects: BIOFÍSICA, FUNGOS, ENZIMAS

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      MIOTTO, Lis S. et al. SAXS studies of the endoglucanase cel12A from Gloeophyllum trabeum show its monomeric structure and reveal the influence of temperature on the structural stability of the enzyme. Materials, v. 7, n. 7, p. 5202-5211, 2014Tradução . . Disponível em: https://doi.org/10.3390/ma7075202. Acesso em: 04 jun. 2024.
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      Miotto, L. S., Reis, C. V., Oliveira Neto, M. de, & Polikarpov, I. (2014). SAXS studies of the endoglucanase cel12A from Gloeophyllum trabeum show its monomeric structure and reveal the influence of temperature on the structural stability of the enzyme. Materials, 7( 7), 5202-5211. doi:10.3390/ma7075202
    • NLM

      Miotto LS, Reis CV, Oliveira Neto M de, Polikarpov I. SAXS studies of the endoglucanase cel12A from Gloeophyllum trabeum show its monomeric structure and reveal the influence of temperature on the structural stability of the enzyme [Internet]. Materials. 2014 ; 7( 7): 5202-5211.[citado 2024 jun. 04 ] Available from: https://doi.org/10.3390/ma7075202
    • Vancouver

      Miotto LS, Reis CV, Oliveira Neto M de, Polikarpov I. SAXS studies of the endoglucanase cel12A from Gloeophyllum trabeum show its monomeric structure and reveal the influence of temperature on the structural stability of the enzyme [Internet]. Materials. 2014 ; 7( 7): 5202-5211.[citado 2024 jun. 04 ] Available from: https://doi.org/10.3390/ma7075202
  • Source: Acta Crystallographica F. Unidade: IFSC

    Subjects: ENZIMAS, DIFRAÇÃO POR RAIOS X

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      EVANGELISTA, Danilo Elton et al. Expression, purification, crystallization and preliminary X-ray diffraction analysis of the pectin methylesterase from the sugar cane weevil Sphenophorus levis. Acta Crystallographica F, v. 70, p. 331-334, 2014Tradução . . Disponível em: https://doi.org/10.1107/S2053230X14001630. Acesso em: 04 jun. 2024.
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      Evangelista, D. E., Godoy, A. S. de, Paula, F. F. P. de, Silva, F. H., & Polikarpov, I. (2014). Expression, purification, crystallization and preliminary X-ray diffraction analysis of the pectin methylesterase from the sugar cane weevil Sphenophorus levis. Acta Crystallographica F, 70, 331-334. doi:10.1107/S2053230X14001630
    • NLM

      Evangelista DE, Godoy AS de, Paula FFP de, Silva FH, Polikarpov I. Expression, purification, crystallization and preliminary X-ray diffraction analysis of the pectin methylesterase from the sugar cane weevil Sphenophorus levis [Internet]. Acta Crystallographica F. 2014 ; 70 331-334.[citado 2024 jun. 04 ] Available from: https://doi.org/10.1107/S2053230X14001630
    • Vancouver

      Evangelista DE, Godoy AS de, Paula FFP de, Silva FH, Polikarpov I. Expression, purification, crystallization and preliminary X-ray diffraction analysis of the pectin methylesterase from the sugar cane weevil Sphenophorus levis [Internet]. Acta Crystallographica F. 2014 ; 70 331-334.[citado 2024 jun. 04 ] Available from: https://doi.org/10.1107/S2053230X14001630
  • Source: Protein Expression and Purification. Unidade: IFSC

    Subjects: CLONAGEM, ENZIMAS, PROTEÍNAS (CARACTERÍSTICAS)

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      CAMILO, Cesar M. e POLIKARPOV, Igor. High-throughput cloning, expression and purification of glycoside hydrolases using Ligation-Independent Cloning (LIC). Protein Expression and Purification, v. 99, p. 35-42, 2014Tradução . . Disponível em: https://doi.org/10.1016/j.pep.2014.03.008. Acesso em: 04 jun. 2024.
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      Camilo, C. M., & Polikarpov, I. (2014). High-throughput cloning, expression and purification of glycoside hydrolases using Ligation-Independent Cloning (LIC). Protein Expression and Purification, 99, 35-42. doi:10.1016/j.pep.2014.03.008
    • NLM

      Camilo CM, Polikarpov I. High-throughput cloning, expression and purification of glycoside hydrolases using Ligation-Independent Cloning (LIC) [Internet]. Protein Expression and Purification. 2014 ; 99 35-42.[citado 2024 jun. 04 ] Available from: https://doi.org/10.1016/j.pep.2014.03.008
    • Vancouver

      Camilo CM, Polikarpov I. High-throughput cloning, expression and purification of glycoside hydrolases using Ligation-Independent Cloning (LIC) [Internet]. Protein Expression and Purification. 2014 ; 99 35-42.[citado 2024 jun. 04 ] Available from: https://doi.org/10.1016/j.pep.2014.03.008
  • Source: PLOS ONE. Unidade: IFSC

    Subjects: ENZIMAS, FUNGOS, GENES, CANA-DE-AÇÚCAR, BAGAÇOS, BIOMASSA

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      HORTA, Maria Augusta Crivelente et al. Transcriptome profile of Trichoderma harzianum IOC- 3844 induced by sugarcane bagasse. PLOS ONE, v. 9, n. 2, p. e88689-1-ee88689-17, 2014Tradução . . Disponível em: https://doi.org/10.1371/journal.pone.0088689. Acesso em: 04 jun. 2024.
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      Horta, M. A. C., Vicentini, R., Delabona, P. da S., Laborda, P., Crucello, A., Freitas, S., et al. (2014). Transcriptome profile of Trichoderma harzianum IOC- 3844 induced by sugarcane bagasse. PLOS ONE, 9( 2), e88689-1-ee88689-17. doi:10.1371/journal.pone.0088689
    • NLM

      Horta MAC, Vicentini R, Delabona P da S, Laborda P, Crucello A, Freitas S, Kuroshu RM, Polikarpov I, Pradella JG da C, Souza AP. Transcriptome profile of Trichoderma harzianum IOC- 3844 induced by sugarcane bagasse [Internet]. PLOS ONE. 2014 ; 9( 2): e88689-1-ee88689-17.[citado 2024 jun. 04 ] Available from: https://doi.org/10.1371/journal.pone.0088689
    • Vancouver

      Horta MAC, Vicentini R, Delabona P da S, Laborda P, Crucello A, Freitas S, Kuroshu RM, Polikarpov I, Pradella JG da C, Souza AP. Transcriptome profile of Trichoderma harzianum IOC- 3844 induced by sugarcane bagasse [Internet]. PLOS ONE. 2014 ; 9( 2): e88689-1-ee88689-17.[citado 2024 jun. 04 ] Available from: https://doi.org/10.1371/journal.pone.0088689
  • Source: Molecular Endocrinology. Unidade: IFSC

    Subjects: NANOPARTÍCULAS, HORMÔNIOS TIREOIDIANOS, RECEPTORES HORMONAIS

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      SOUZA, P. C. T. et al. Identification of a new hormone-binding site on the surface of thyroid hormone receptor. Molecular Endocrinology, v. 28, n. 4, p. 534-545, 2014Tradução . . Disponível em: https://doi.org/10.1210/me.2013-1359. Acesso em: 04 jun. 2024.
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      Souza, P. C. T., Puhl, A. C., Martínez, L., Aparício, R., Nascimento, A. S., Figueira, A. C. M., et al. (2014). Identification of a new hormone-binding site on the surface of thyroid hormone receptor. Molecular Endocrinology, 28( 4), 534-545. doi:10.1210/me.2013-1359
    • NLM

      Souza PCT, Puhl AC, Martínez L, Aparício R, Nascimento AS, Figueira ACM, Nguyen P, Webb P, Skaf MS, Polikarpov I. Identification of a new hormone-binding site on the surface of thyroid hormone receptor [Internet]. Molecular Endocrinology. 2014 ; 28( 4): 534-545.[citado 2024 jun. 04 ] Available from: https://doi.org/10.1210/me.2013-1359
    • Vancouver

      Souza PCT, Puhl AC, Martínez L, Aparício R, Nascimento AS, Figueira ACM, Nguyen P, Webb P, Skaf MS, Polikarpov I. Identification of a new hormone-binding site on the surface of thyroid hormone receptor [Internet]. Molecular Endocrinology. 2014 ; 28( 4): 534-545.[citado 2024 jun. 04 ] Available from: https://doi.org/10.1210/me.2013-1359
  • Source: Acta Crystallographica F. Unidade: IFSC

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

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      CAMPOS, Bruna Medeia et al. Cloning, purification, crystallization and preliminary X-ray studies of a carbohydrate-binding module (CBM_E1) derived from sugarcane soil metagenome. Acta Crystallographica F, v. 70, p. 1232-1235, 2014Tradução . . Disponível em: https://doi.org/10.1107/S2053230X14015520. Acesso em: 04 jun. 2024.
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      Campos, B. M., Alvarez, T. M., Liberato, M. V., Polikarpov, I., Gilbert, H. J., Zeri, A. C. de M., & Squina, F. M. (2014). Cloning, purification, crystallization and preliminary X-ray studies of a carbohydrate-binding module (CBM_E1) derived from sugarcane soil metagenome. Acta Crystallographica F, 70, 1232-1235. doi:10.1107/S2053230X14015520
    • NLM

      Campos BM, Alvarez TM, Liberato MV, Polikarpov I, Gilbert HJ, Zeri AC de M, Squina FM. Cloning, purification, crystallization and preliminary X-ray studies of a carbohydrate-binding module (CBM_E1) derived from sugarcane soil metagenome [Internet]. Acta Crystallographica F. 2014 ; 70 1232-1235.[citado 2024 jun. 04 ] Available from: https://doi.org/10.1107/S2053230X14015520
    • Vancouver

      Campos BM, Alvarez TM, Liberato MV, Polikarpov I, Gilbert HJ, Zeri AC de M, Squina FM. Cloning, purification, crystallization and preliminary X-ray studies of a carbohydrate-binding module (CBM_E1) derived from sugarcane soil metagenome [Internet]. Acta Crystallographica F. 2014 ; 70 1232-1235.[citado 2024 jun. 04 ] Available from: https://doi.org/10.1107/S2053230X14015520
  • Source: Journal of Biomedical Nanotechnology. Unidade: IFSC

    Subjects: NANOPARTÍCULAS, HORMÔNIOS TIREOIDIANOS, SENSORES BIOMÉDICOS

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      BENDO, Luana et al. Nanostructured sensors containing immobilized nuclear receptors for thyroid hormone detection. Journal of Biomedical Nanotechnology, v. 10, n. 5, p. 744-750, 2014Tradução . . Disponível em: https://doi.org/10.1166/jbn.2014.1774. Acesso em: 04 jun. 2024.
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      Bendo, L., Casanova, M., Figueira, A. C. M., Polikarpov, I., & Zucolotto, V. (2014). Nanostructured sensors containing immobilized nuclear receptors for thyroid hormone detection. Journal of Biomedical Nanotechnology, 10( 5), 744-750. doi:10.1166/jbn.2014.1774
    • NLM

      Bendo L, Casanova M, Figueira ACM, Polikarpov I, Zucolotto V. Nanostructured sensors containing immobilized nuclear receptors for thyroid hormone detection [Internet]. Journal of Biomedical Nanotechnology. 2014 ; 10( 5): 744-750.[citado 2024 jun. 04 ] Available from: https://doi.org/10.1166/jbn.2014.1774
    • Vancouver

      Bendo L, Casanova M, Figueira ACM, Polikarpov I, Zucolotto V. Nanostructured sensors containing immobilized nuclear receptors for thyroid hormone detection [Internet]. Journal of Biomedical Nanotechnology. 2014 ; 10( 5): 744-750.[citado 2024 jun. 04 ] Available from: https://doi.org/10.1166/jbn.2014.1774
  • Source: PLOS ONE. Unidade: IFSC

    Subjects: ENZIMAS (ESTUDO), BIOMASSA, BIOCOMBUSTÍVEIS

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      MIOTTO, Lis Schwartz et al. The characterization of the endoglucanase Cel12A from Gloeophyllum trabeum reveals an enzyme highly active on β-glucan. PLOS ONE, v. 9, n. 9, p. e108393-1-e108393-9, 2014Tradução . . Disponível em: https://doi.org/10.1371/journal.pone.0108393. Acesso em: 04 jun. 2024.
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      Miotto, L. S., Rezende, C. A. de, Bernardes, A., Serpa, V. I., Tsang, A., & Polikarpov, I. (2014). The characterization of the endoglucanase Cel12A from Gloeophyllum trabeum reveals an enzyme highly active on β-glucan. PLOS ONE, 9( 9), e108393-1-e108393-9. doi:10.1371/journal.pone.0108393
    • NLM

      Miotto LS, Rezende CA de, Bernardes A, Serpa VI, Tsang A, Polikarpov I. The characterization of the endoglucanase Cel12A from Gloeophyllum trabeum reveals an enzyme highly active on β-glucan [Internet]. PLOS ONE. 2014 ; 9( 9): e108393-1-e108393-9.[citado 2024 jun. 04 ] Available from: https://doi.org/10.1371/journal.pone.0108393
    • Vancouver

      Miotto LS, Rezende CA de, Bernardes A, Serpa VI, Tsang A, Polikarpov I. The characterization of the endoglucanase Cel12A from Gloeophyllum trabeum reveals an enzyme highly active on β-glucan [Internet]. PLOS ONE. 2014 ; 9( 9): e108393-1-e108393-9.[citado 2024 jun. 04 ] Available from: https://doi.org/10.1371/journal.pone.0108393
  • Source: Bioenergy Research. Unidade: IFSC

    Subjects: BIOCOMBUSTÍVEIS, CANA-DE-AÇÚCAR

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      GÓMEZ, Leonardo D. et al. Side by side comparison of chemical compounds generated by aqueous pretreatments of maize stover, miscanthus and sugarcane bagasse. Bioenergy Research, v. 7, n. 4, p. 1466-1480, 2014Tradução . . Disponível em: https://doi.org/10.1007/s12155-014-9480-2. Acesso em: 04 jun. 2024.
    • APA

      Gómez, L. D., Vanholme, R., Bird, S., Goeminne, G., Trindade, L. M., Polikarpov, I., et al. (2014). Side by side comparison of chemical compounds generated by aqueous pretreatments of maize stover, miscanthus and sugarcane bagasse. Bioenergy Research, 7( 4), 1466-1480. doi:10.1007/s12155-014-9480-2
    • NLM

      Gómez LD, Vanholme R, Bird S, Goeminne G, Trindade LM, Polikarpov I, Simister R, Morreel K, Boerjan W, McQueen-Mason SJ. Side by side comparison of chemical compounds generated by aqueous pretreatments of maize stover, miscanthus and sugarcane bagasse [Internet]. Bioenergy Research. 2014 ; 7( 4): 1466-1480.[citado 2024 jun. 04 ] Available from: https://doi.org/10.1007/s12155-014-9480-2
    • Vancouver

      Gómez LD, Vanholme R, Bird S, Goeminne G, Trindade LM, Polikarpov I, Simister R, Morreel K, Boerjan W, McQueen-Mason SJ. Side by side comparison of chemical compounds generated by aqueous pretreatments of maize stover, miscanthus and sugarcane bagasse [Internet]. Bioenergy Research. 2014 ; 7( 4): 1466-1480.[citado 2024 jun. 04 ] Available from: https://doi.org/10.1007/s12155-014-9480-2
  • Source: Biotechnology for Biofuels. Unidade: IFSC

    Subjects: BIOCOMBUSTÍVEIS, CANA-DE-AÇÚCAR, BAGAÇOS, ETANOL, CELULOSE, LIGNINA

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      COLETTA, Vitor Carlos et al. Mapping the lignin distribution in pretreated sugarcane bagasse by confocal and fluorescence lifetime imaging microscopy. Biotechnology for Biofuels, v. 6, p. 43-1-43-10, 2013Tradução . . Disponível em: https://doi.org/10.1186/1754-6834-6-43. Acesso em: 04 jun. 2024.
    • APA

      Coletta, V. C., Rezende, C. A., Conceição, F. R. da, Polikarpov, I., & Guimarães, F. E. G. (2013). Mapping the lignin distribution in pretreated sugarcane bagasse by confocal and fluorescence lifetime imaging microscopy. Biotechnology for Biofuels, 6, 43-1-43-10. doi:10.1186/1754-6834-6-43
    • NLM

      Coletta VC, Rezende CA, Conceição FR da, Polikarpov I, Guimarães FEG. Mapping the lignin distribution in pretreated sugarcane bagasse by confocal and fluorescence lifetime imaging microscopy [Internet]. Biotechnology for Biofuels. 2013 ; 6 43-1-43-10.[citado 2024 jun. 04 ] Available from: https://doi.org/10.1186/1754-6834-6-43
    • Vancouver

      Coletta VC, Rezende CA, Conceição FR da, Polikarpov I, Guimarães FEG. Mapping the lignin distribution in pretreated sugarcane bagasse by confocal and fluorescence lifetime imaging microscopy [Internet]. Biotechnology for Biofuels. 2013 ; 6 43-1-43-10.[citado 2024 jun. 04 ] Available from: https://doi.org/10.1186/1754-6834-6-43
  • Source: Journal of Molecular Biology. Unidade: IFSC

    Subjects: RECEPTORES (ESTUDO), PEROXISSOMOS, CRISTALOGRAFIA ESTRUTURAL

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      BERNARDES, Amanda et al. Molecular mechanism of peroxisome proliferator-activated receptor α activation by WY14643: a new mode of ligand recognition and receptor stabilization. Journal of Molecular Biology, v. 425, n. 16, p. 2878-2893, 2013Tradução . . Disponível em: https://doi.org/10.1016/j.jmb.2013.05.010. Acesso em: 04 jun. 2024.
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      Bernardes, A., Souza, P. C. T., Muniz, J. R. C., Ricci, C. G., Ayers, S. D., Parekh, N. M., et al. (2013). Molecular mechanism of peroxisome proliferator-activated receptor α activation by WY14643: a new mode of ligand recognition and receptor stabilization. Journal of Molecular Biology, 425( 16), 2878-2893. doi:10.1016/j.jmb.2013.05.010
    • NLM

      Bernardes A, Souza PCT, Muniz JRC, Ricci CG, Ayers SD, Parekh NM, Godoy AS, Trivella DBB, Reinach P, Webb P, Skaf MS, Polikarpov I. Molecular mechanism of peroxisome proliferator-activated receptor α activation by WY14643: a new mode of ligand recognition and receptor stabilization [Internet]. Journal of Molecular Biology. 2013 ; 425( 16): 2878-2893.[citado 2024 jun. 04 ] Available from: https://doi.org/10.1016/j.jmb.2013.05.010
    • Vancouver

      Bernardes A, Souza PCT, Muniz JRC, Ricci CG, Ayers SD, Parekh NM, Godoy AS, Trivella DBB, Reinach P, Webb P, Skaf MS, Polikarpov I. Molecular mechanism of peroxisome proliferator-activated receptor α activation by WY14643: a new mode of ligand recognition and receptor stabilization [Internet]. Journal of Molecular Biology. 2013 ; 425( 16): 2878-2893.[citado 2024 jun. 04 ] Available from: https://doi.org/10.1016/j.jmb.2013.05.010
  • Source: Journal of Biological Chemistry. Unidade: IFSC

    Subjects: ENZIMAS, BIOQUÍMICA

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      LIMA, Marisa A. et al. Aspergillus niger β-glucosidase has a cellulase-like tadpole molecular shape: insights into glycoside hydrolase family 3 (gh3) β-glucosidase structure and function. Journal of Biological Chemistry, v. No 2013, n. 46, p. 32991-33005, 2013Tradução . . Disponível em: https://doi.org/10.1074/jbc.M113.479279. Acesso em: 04 jun. 2024.
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      Lima, M. A., Oliveira Neto, M., Kadowaki, M. A. S., Rosseto, F. R., Prates, E. T., Squina, F. M., et al. (2013). Aspergillus niger β-glucosidase has a cellulase-like tadpole molecular shape: insights into glycoside hydrolase family 3 (gh3) β-glucosidase structure and function. Journal of Biological Chemistry, No 2013( 46), 32991-33005. doi:10.1074/jbc.M113.479279
    • NLM

      Lima MA, Oliveira Neto M, Kadowaki MAS, Rosseto FR, Prates ET, Squina FM, Leme AFP, Skaf MS, Polikarpov I. Aspergillus niger β-glucosidase has a cellulase-like tadpole molecular shape: insights into glycoside hydrolase family 3 (gh3) β-glucosidase structure and function [Internet]. Journal of Biological Chemistry. 2013 ; No 2013( 46): 32991-33005.[citado 2024 jun. 04 ] Available from: https://doi.org/10.1074/jbc.M113.479279
    • Vancouver

      Lima MA, Oliveira Neto M, Kadowaki MAS, Rosseto FR, Prates ET, Squina FM, Leme AFP, Skaf MS, Polikarpov I. Aspergillus niger β-glucosidase has a cellulase-like tadpole molecular shape: insights into glycoside hydrolase family 3 (gh3) β-glucosidase structure and function [Internet]. Journal of Biological Chemistry. 2013 ; No 2013( 46): 32991-33005.[citado 2024 jun. 04 ] Available from: https://doi.org/10.1074/jbc.M113.479279

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