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  • Source: Protein and Peptide Letters. Unidades: IFSC, FFCLRP

    Subjects: PEPTÍDEOS, ENZIMAS, LIPÍDEOS

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      VICENTE, Eduardo F. et al. N-terminal microdomain peptide from human dihydroorotate dehydrogenase: structure and model membrane interactions. Protein and Peptide Letters, v. 22, n. 2, p. 119-129 + supplementary materials: i-iii, 2015Tradução . . Disponível em: https://doi.org/10.2174/0929866521666140508125215. Acesso em: 03 set. 2024.
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      Vicente, E. F., Nobre-Pavinatto, T. M., Pavinatto, F. J., Oliveira Junior, O. N. de, Costa Filho, A. J. da, & Cilli, E. M. (2015). N-terminal microdomain peptide from human dihydroorotate dehydrogenase: structure and model membrane interactions. Protein and Peptide Letters, 22( 2), 119-129 + supplementary materials: i-iii. doi:10.2174/0929866521666140508125215
    • NLM

      Vicente EF, Nobre-Pavinatto TM, Pavinatto FJ, Oliveira Junior ON de, Costa Filho AJ da, Cilli EM. N-terminal microdomain peptide from human dihydroorotate dehydrogenase: structure and model membrane interactions [Internet]. Protein and Peptide Letters. 2015 ; 22( 2): 119-129 + supplementary materials: i-iii.[citado 2024 set. 03 ] Available from: https://doi.org/10.2174/0929866521666140508125215
    • Vancouver

      Vicente EF, Nobre-Pavinatto TM, Pavinatto FJ, Oliveira Junior ON de, Costa Filho AJ da, Cilli EM. N-terminal microdomain peptide from human dihydroorotate dehydrogenase: structure and model membrane interactions [Internet]. Protein and Peptide Letters. 2015 ; 22( 2): 119-129 + supplementary materials: i-iii.[citado 2024 set. 03 ] Available from: https://doi.org/10.2174/0929866521666140508125215
  • Source: Biochemical Journal. Unidades: IFSC, FFCLRP

    Subjects: ENZIMAS, CÉLULAS VEGETAIS, RESSONÂNCIA MAGNÉTICA NUCLEAR

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      SANTOS, Camila R. et al. Dissecting structure-function-stability relationships of a thermostable GH5-CBM3 cellulase from Bacillus subtilis 168. Biochemical Journal, v. 441, n. Ja 2012, p. 95-104, 2012Tradução . . Disponível em: https://doi.org/10.1042/BJ20110869. Acesso em: 03 set. 2024.
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      Santos, C. R., Paiva, J. H., Sforça, M. L., Neves, J. L., Navarro, R. Z., Cota, J., et al. (2012). Dissecting structure-function-stability relationships of a thermostable GH5-CBM3 cellulase from Bacillus subtilis 168. Biochemical Journal, 441( Ja 2012), 95-104. doi:10.1042/BJ20110869
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      Santos CR, Paiva JH, Sforça ML, Neves JL, Navarro RZ, Cota J, Akao PK, Hoffmam ZB, Meza AN, Smetana JH, Nogueira ML, Polikarpov I, Xavier-Neto J, Squina FM, Ward RJ, Ruller R, Zeri AC, Murakami MT. Dissecting structure-function-stability relationships of a thermostable GH5-CBM3 cellulase from Bacillus subtilis 168 [Internet]. Biochemical Journal. 2012 ; 441( Ja 2012): 95-104.[citado 2024 set. 03 ] Available from: https://doi.org/10.1042/BJ20110869
    • Vancouver

      Santos CR, Paiva JH, Sforça ML, Neves JL, Navarro RZ, Cota J, Akao PK, Hoffmam ZB, Meza AN, Smetana JH, Nogueira ML, Polikarpov I, Xavier-Neto J, Squina FM, Ward RJ, Ruller R, Zeri AC, Murakami MT. Dissecting structure-function-stability relationships of a thermostable GH5-CBM3 cellulase from Bacillus subtilis 168 [Internet]. Biochemical Journal. 2012 ; 441( Ja 2012): 95-104.[citado 2024 set. 03 ] Available from: https://doi.org/10.1042/BJ20110869
  • Source: Biophysical Journal. Conference titles: Annual Meeting of the Biophysical Society. Unidades: IFSC, FCFRP, FFCLRP

    Subjects: ENZIMAS, CATÁLISE, BIODEGRADAÇÃO (ESTUDO), TOXINAS

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      MESQUITA, Nathalya C. et al. Understanding chlorocatechol 1,2-dioxygenase function: a promising player in bioremediation processes. Biophysical Journal. Saint Louis: Cell Press. Disponível em: https://doi.org/10.1016/j.bpj.2011.11.383. Acesso em: 03 set. 2024. , 2012
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      Mesquita, N. C., Rustiguel, J. K., Melo, F. A., Citadini, A. P., Pinto, A. P. A., Araújo, A. P. U. de, et al. (2012). Understanding chlorocatechol 1,2-dioxygenase function: a promising player in bioremediation processes. Biophysical Journal. Saint Louis: Cell Press. doi:10.1016/j.bpj.2011.11.383
    • NLM

      Mesquita NC, Rustiguel JK, Melo FA, Citadini AP, Pinto APA, Araújo APU de, Nonato MC, Costa Filho AJ da. Understanding chlorocatechol 1,2-dioxygenase function: a promising player in bioremediation processes [Internet]. Biophysical Journal. 2012 ; 102( Ja 2012): 64a-65a.[citado 2024 set. 03 ] Available from: https://doi.org/10.1016/j.bpj.2011.11.383
    • Vancouver

      Mesquita NC, Rustiguel JK, Melo FA, Citadini AP, Pinto APA, Araújo APU de, Nonato MC, Costa Filho AJ da. Understanding chlorocatechol 1,2-dioxygenase function: a promising player in bioremediation processes [Internet]. Biophysical Journal. 2012 ; 102( Ja 2012): 64a-65a.[citado 2024 set. 03 ] Available from: https://doi.org/10.1016/j.bpj.2011.11.383
  • Source: Biosensors and Bioelectronics. Unidades: IFSC, FFCLRP

    Subjects: CÉLULAS A COMBUSTÍVEL, ETANOL, ENZIMAS

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      AQUINO NETO, S. et al. Development of nanostructured bioanodes containing denrimers and dehydrogenases enzymes for application in ethanol biofuel cells. Biosensors and Bioelectronics, v. 26, n. 6, p. 2922-2926, 2011Tradução . . Disponível em: https://doi.org/10.1016/j.bios.2010.11.038. Acesso em: 03 set. 2024.
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      Aquino Neto, S., Forti, J. C., Zucolotto, V., Ciancaglini, P., & Andrade, A. R. (2011). Development of nanostructured bioanodes containing denrimers and dehydrogenases enzymes for application in ethanol biofuel cells. Biosensors and Bioelectronics, 26( 6), 2922-2926. doi:10.1016/j.bios.2010.11.038
    • NLM

      Aquino Neto S, Forti JC, Zucolotto V, Ciancaglini P, Andrade AR. Development of nanostructured bioanodes containing denrimers and dehydrogenases enzymes for application in ethanol biofuel cells [Internet]. Biosensors and Bioelectronics. 2011 ; 26( 6): 2922-2926.[citado 2024 set. 03 ] Available from: https://doi.org/10.1016/j.bios.2010.11.038
    • Vancouver

      Aquino Neto S, Forti JC, Zucolotto V, Ciancaglini P, Andrade AR. Development of nanostructured bioanodes containing denrimers and dehydrogenases enzymes for application in ethanol biofuel cells [Internet]. Biosensors and Bioelectronics. 2011 ; 26( 6): 2922-2926.[citado 2024 set. 03 ] Available from: https://doi.org/10.1016/j.bios.2010.11.038
  • Source: Process Biochemistry. Unidades: IFSC, FFCLRP

    Subjects: ENZIMAS, FILMES FINOS, BIOFÍSICA, ETANOL, ELETROQUÍMICA

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      AQUINO NETO, Sidney et al. The kinetic behavior of dehydrogenase enzymes in solution and immobilized onto nanostructured carbon platforms. Process Biochemistry, v. 46, n. 12, p. 2347-2352, 2011Tradução . . Disponível em: https://doi.org/10.1016/j.procbio.2011.09.019. Acesso em: 03 set. 2024.
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      Aquino Neto, S., Forti, J. C., Zucolotto, V., Ciancaglini, P., & Andrade, A. R. de. (2011). The kinetic behavior of dehydrogenase enzymes in solution and immobilized onto nanostructured carbon platforms. Process Biochemistry, 46( 12), 2347-2352. doi:10.1016/j.procbio.2011.09.019
    • NLM

      Aquino Neto S, Forti JC, Zucolotto V, Ciancaglini P, Andrade AR de. The kinetic behavior of dehydrogenase enzymes in solution and immobilized onto nanostructured carbon platforms [Internet]. Process Biochemistry. 2011 ; 46( 12): 2347-2352.[citado 2024 set. 03 ] Available from: https://doi.org/10.1016/j.procbio.2011.09.019
    • Vancouver

      Aquino Neto S, Forti JC, Zucolotto V, Ciancaglini P, Andrade AR de. The kinetic behavior of dehydrogenase enzymes in solution and immobilized onto nanostructured carbon platforms [Internet]. Process Biochemistry. 2011 ; 46( 12): 2347-2352.[citado 2024 set. 03 ] Available from: https://doi.org/10.1016/j.procbio.2011.09.019
  • Source: Biosensors and Bioelectronics. Unidades: IFSC, FFCLRP

    Subjects: CÉLULAS A COMBUSTÍVEL, ETANOL, ENZIMAS

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      FORTI, J. C. et al. Development of novel bioanodes for ethanol biofuel cell using PAMAM dendrimers as matrix for enzyme immobilization. Biosensors and Bioelectronics, v. 26, n. Ja 2011, p. 2675-2679, 2011Tradução . . Disponível em: https://doi.org/10.1016/j.bios.2010.05.011. Acesso em: 03 set. 2024.
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      Forti, J. C., Aquino Neto, S., Zucolotto, V., Ciancaglini, P., & Andrade, A. R. (2011). Development of novel bioanodes for ethanol biofuel cell using PAMAM dendrimers as matrix for enzyme immobilization. Biosensors and Bioelectronics, 26( Ja 2011), 2675-2679. doi:10.1016/j.bios.2010.05.011
    • NLM

      Forti JC, Aquino Neto S, Zucolotto V, Ciancaglini P, Andrade AR. Development of novel bioanodes for ethanol biofuel cell using PAMAM dendrimers as matrix for enzyme immobilization [Internet]. Biosensors and Bioelectronics. 2011 ; 26( Ja 2011): 2675-2679.[citado 2024 set. 03 ] Available from: https://doi.org/10.1016/j.bios.2010.05.011
    • Vancouver

      Forti JC, Aquino Neto S, Zucolotto V, Ciancaglini P, Andrade AR. Development of novel bioanodes for ethanol biofuel cell using PAMAM dendrimers as matrix for enzyme immobilization [Internet]. Biosensors and Bioelectronics. 2011 ; 26( Ja 2011): 2675-2679.[citado 2024 set. 03 ] Available from: https://doi.org/10.1016/j.bios.2010.05.011
  • Source: Applied Biochemistry and Biotechnology. Unidade: FFCLRP

    Subjects: HIDRÓLISE, ENZIMAS

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      DAMÁSIO, André Ricardo de Lima et al. Purification and partial characterization of an exo-polygalacturonase from paecilomyxes variotii liquid cultures. Applied Biochemistry and Biotechnology, v. 160, n. 5, p. 1496-1507, 2010Tradução . . Acesso em: 03 set. 2024.
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      Damásio, A. R. de L., Silva, T. M. da, Maller, A., Jorge, J. A., Terenzi, H. F., & Polizeli, M. de L. T. de M. (2010). Purification and partial characterization of an exo-polygalacturonase from paecilomyxes variotii liquid cultures. Applied Biochemistry and Biotechnology, 160( 5), 1496-1507.
    • NLM

      Damásio AR de L, Silva TM da, Maller A, Jorge JA, Terenzi HF, Polizeli M de LT de M. Purification and partial characterization of an exo-polygalacturonase from paecilomyxes variotii liquid cultures. Applied Biochemistry and Biotechnology. 2010 ; 160( 5): 1496-1507.[citado 2024 set. 03 ]
    • Vancouver

      Damásio AR de L, Silva TM da, Maller A, Jorge JA, Terenzi HF, Polizeli M de LT de M. Purification and partial characterization of an exo-polygalacturonase from paecilomyxes variotii liquid cultures. Applied Biochemistry and Biotechnology. 2010 ; 160( 5): 1496-1507.[citado 2024 set. 03 ]
  • Source: Biophysical Chemistry. Unidade: FFCLRP

    Subjects: ENZIMAS, PROTEÍNAS, ESPECTROSCOPIA

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      RIGOS, Carolina Fortes et al. Cytoplasmatic domain of Na,K-ATPase 'alfa'-subunit is responsible for the aggregation of the enzyme in proteoliposomes. Biophysical Chemistry, v. 146, n. 1, p. 36-41, 2010Tradução . . Disponível em: https://doi.org/10.1016/j.bpc.2009.10.002. Acesso em: 03 set. 2024.
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      Rigos, C. F., Santos, H. de L., Yoneda, J. S., Montich, G., Maggio, B., & Ciancaglini, P. (2010). Cytoplasmatic domain of Na,K-ATPase 'alfa'-subunit is responsible for the aggregation of the enzyme in proteoliposomes. Biophysical Chemistry, 146( 1), 36-41. doi:10.1016/j.bpc.2009.10.002
    • NLM

      Rigos CF, Santos H de L, Yoneda JS, Montich G, Maggio B, Ciancaglini P. Cytoplasmatic domain of Na,K-ATPase 'alfa'-subunit is responsible for the aggregation of the enzyme in proteoliposomes [Internet]. Biophysical Chemistry. 2010 ; 146( 1): 36-41.[citado 2024 set. 03 ] Available from: https://doi.org/10.1016/j.bpc.2009.10.002
    • Vancouver

      Rigos CF, Santos H de L, Yoneda JS, Montich G, Maggio B, Ciancaglini P. Cytoplasmatic domain of Na,K-ATPase 'alfa'-subunit is responsible for the aggregation of the enzyme in proteoliposomes [Internet]. Biophysical Chemistry. 2010 ; 146( 1): 36-41.[citado 2024 set. 03 ] Available from: https://doi.org/10.1016/j.bpc.2009.10.002
  • Source: Journal of Photochemistry and Photobiology A. Unidades: IFSC, FFCLRP

    Subjects: FÁRMACOS (ESTUDO), FOTÔNICA (ANÁLISE), ENZIMAS, ABSORÇÃO DA LUZ

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      MAXIMIANO, R. V. et al. Excited-state absorption investigation of a cationic porphyrin derivative. Journal of Photochemistry and Photobiology A, v. 214, n. 2/3, p. 115-120, 2010Tradução . . Disponível em: https://doi.org/10.1016/j.jphotochem.2010.06.007. Acesso em: 03 set. 2024.
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      Maximiano, R. V., Piovesan, E., Zílio, S. C., Machado, A. E. H., De Paula, R., Cavaleiro, J. A. S., et al. (2010). Excited-state absorption investigation of a cationic porphyrin derivative. Journal of Photochemistry and Photobiology A, 214( 2/3), 115-120. doi:10.1016/j.jphotochem.2010.06.007
    • NLM

      Maximiano RV, Piovesan E, Zílio SC, Machado AEH, De Paula R, Cavaleiro JAS, Borissevitch I, Ito AS, Gonçalves PJ, Barbosa Neto NM. Excited-state absorption investigation of a cationic porphyrin derivative [Internet]. Journal of Photochemistry and Photobiology A. 2010 ; 214( 2/3): 115-120.[citado 2024 set. 03 ] Available from: https://doi.org/10.1016/j.jphotochem.2010.06.007
    • Vancouver

      Maximiano RV, Piovesan E, Zílio SC, Machado AEH, De Paula R, Cavaleiro JAS, Borissevitch I, Ito AS, Gonçalves PJ, Barbosa Neto NM. Excited-state absorption investigation of a cationic porphyrin derivative [Internet]. Journal of Photochemistry and Photobiology A. 2010 ; 214( 2/3): 115-120.[citado 2024 set. 03 ] Available from: https://doi.org/10.1016/j.jphotochem.2010.06.007
  • Source: Journal of the Brazilian Chemical Society. Unidades: IFSC, FFCLRP

    Subjects: FÁRMACOS (DESENVOLVIMENTO), TRYPANOSOMA CRUZI, ENZIMAS, PLANEJAMENTO DE FÁRMACOS, IMOBILIZAÇÃO, CINÉTICA (PARÂMETROS)

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      GUIDO, Rafael Victório Carvalho et al. Structural insights into the molecular basis responsible for the effects of immobilization on the kinetic parameters of glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma cruzi and human. Journal of the Brazilian Chemical Society, v. 21, n. 10, p. 1845-1853, 2010Tradução . . Disponível em: https://doi.org/10.1590/s0103-50532010001000008. Acesso em: 03 set. 2024.
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      Guido, R. V. C., Cardoso, C. L., Moraes, M. C. de, Andricopulo, A. D., Cass, Q. B., & Oliva, G. (2010). Structural insights into the molecular basis responsible for the effects of immobilization on the kinetic parameters of glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma cruzi and human. Journal of the Brazilian Chemical Society, 21( 10), 1845-1853. doi:10.1590/s0103-50532010001000008
    • NLM

      Guido RVC, Cardoso CL, Moraes MC de, Andricopulo AD, Cass QB, Oliva G. Structural insights into the molecular basis responsible for the effects of immobilization on the kinetic parameters of glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma cruzi and human [Internet]. Journal of the Brazilian Chemical Society. 2010 ; 21( 10): 1845-1853.[citado 2024 set. 03 ] Available from: https://doi.org/10.1590/s0103-50532010001000008
    • Vancouver

      Guido RVC, Cardoso CL, Moraes MC de, Andricopulo AD, Cass QB, Oliva G. Structural insights into the molecular basis responsible for the effects of immobilization on the kinetic parameters of glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma cruzi and human [Internet]. Journal of the Brazilian Chemical Society. 2010 ; 21( 10): 1845-1853.[citado 2024 set. 03 ] Available from: https://doi.org/10.1590/s0103-50532010001000008
  • Source: Inflammation Research. Unidades: FCFRP, FFCLRP

    Subjects: FOSFOLIPASES A, MACRÓFAGOS, ENZIMAS

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      ARAGÃO, Elisângela Aparecida et al. Suramin inhibitis macrophage activation by human group IIA phospholipase 'A IND.2', but does not affect bactericidal activity of the enzyme. Inflammation Research, v. 58, n. 4, p. 210-217, 2009Tradução . . Disponível em: https://doi.org/10.1007/s00011-008-8137-z. Acesso em: 03 set. 2024.
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      Aragão, E. A., Chioato, L., Ferreira, T. L., Medeiros, A. I. de, Secatto, A., Faccioli, L. H., & Ward, R. J. (2009). Suramin inhibitis macrophage activation by human group IIA phospholipase 'A IND.2', but does not affect bactericidal activity of the enzyme. Inflammation Research, 58( 4), 210-217. doi:10.1007/s00011-008-8137-z
    • NLM

      Aragão EA, Chioato L, Ferreira TL, Medeiros AI de, Secatto A, Faccioli LH, Ward RJ. Suramin inhibitis macrophage activation by human group IIA phospholipase 'A IND.2', but does not affect bactericidal activity of the enzyme [Internet]. Inflammation Research. 2009 ; 58( 4): 210-217.[citado 2024 set. 03 ] Available from: https://doi.org/10.1007/s00011-008-8137-z
    • Vancouver

      Aragão EA, Chioato L, Ferreira TL, Medeiros AI de, Secatto A, Faccioli LH, Ward RJ. Suramin inhibitis macrophage activation by human group IIA phospholipase 'A IND.2', but does not affect bactericidal activity of the enzyme [Internet]. Inflammation Research. 2009 ; 58( 4): 210-217.[citado 2024 set. 03 ] Available from: https://doi.org/10.1007/s00011-008-8137-z
  • Source: Journal of Physical Chemistry B. Unidades: FFCLRP, IFSC

    Subjects: FILMES FINOS, ESPECTROSCOPIA, MEMBRANAS CELULARES, ENZIMAS, PROTEÍNAS

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      NOBRE, Thatyane M. et al. Molecular view of the interaction between 'iota'-carrageenan and a phospholipid film and its role in enzyme immobilization. Journal of Physical Chemistry B, v. 113, n. 21, p. 7491-7497, 2009Tradução . . Disponível em: https://doi.org/10.1021/jp900841p. Acesso em: 03 set. 2024.
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      Nobre, T. M., Silva, H. de S. e, Furriel, R. dos P. M., Leone, F. de A., Miranda, P. B., & Zaniquelli, M. E. D. (2009). Molecular view of the interaction between 'iota'-carrageenan and a phospholipid film and its role in enzyme immobilization. Journal of Physical Chemistry B, 113( 21), 7491-7497. doi:10.1021/jp900841p
    • NLM

      Nobre TM, Silva H de S e, Furriel R dos PM, Leone F de A, Miranda PB, Zaniquelli MED. Molecular view of the interaction between 'iota'-carrageenan and a phospholipid film and its role in enzyme immobilization [Internet]. Journal of Physical Chemistry B. 2009 ; 113( 21): 7491-7497.[citado 2024 set. 03 ] Available from: https://doi.org/10.1021/jp900841p
    • Vancouver

      Nobre TM, Silva H de S e, Furriel R dos PM, Leone F de A, Miranda PB, Zaniquelli MED. Molecular view of the interaction between 'iota'-carrageenan and a phospholipid film and its role in enzyme immobilization [Internet]. Journal of Physical Chemistry B. 2009 ; 113( 21): 7491-7497.[citado 2024 set. 03 ] Available from: https://doi.org/10.1021/jp900841p
  • Source: Protein Expression and Purification. Unidades: FFCLRP, IQ

    Subjects: ESCHERICHIA COLI, ENZIMAS

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      ALMEIDA, Fabiana Maria de et al. Heterologous expression in Escherichia coli of Neurospora crassa neutral trehalase as an active enzyme. Protein Expression and Purification, v. 65, n. 2, p. 185-189, 2009Tradução . . Disponível em: https://doi.org/10.1016/j.pep.2008.11.010. Acesso em: 03 set. 2024.
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      Almeida, F. M. de, Bonini, B. M., Beton, D., Jorge, J. A., Terenzi, H. F., & Da Silva, A. M. (2009). Heterologous expression in Escherichia coli of Neurospora crassa neutral trehalase as an active enzyme. Protein Expression and Purification, 65( 2), 185-189. doi:10.1016/j.pep.2008.11.010
    • NLM

      Almeida FM de, Bonini BM, Beton D, Jorge JA, Terenzi HF, Da Silva AM. Heterologous expression in Escherichia coli of Neurospora crassa neutral trehalase as an active enzyme [Internet]. Protein Expression and Purification. 2009 ; 65( 2): 185-189.[citado 2024 set. 03 ] Available from: https://doi.org/10.1016/j.pep.2008.11.010
    • Vancouver

      Almeida FM de, Bonini BM, Beton D, Jorge JA, Terenzi HF, Da Silva AM. Heterologous expression in Escherichia coli of Neurospora crassa neutral trehalase as an active enzyme [Internet]. Protein Expression and Purification. 2009 ; 65( 2): 185-189.[citado 2024 set. 03 ] Available from: https://doi.org/10.1016/j.pep.2008.11.010
  • Source: Molecular Physics. Unidade: FFCLRP

    Subjects: ENZIMAS, BIOFÍSICA

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      VIEIRA, Davi Serradella e DEGRÈVE, Léo. An insight into the thermostability of a pair of xylanases: the role of hydrogen bonds. Molecular Physics, v. 107, n. 1, p. 59-69, 2009Tradução . . Disponível em: https://doi.org/10.1080/00268970902717959. Acesso em: 03 set. 2024.
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      Vieira, D. S., & Degrève, L. (2009). An insight into the thermostability of a pair of xylanases: the role of hydrogen bonds. Molecular Physics, 107( 1), 59-69. doi:10.1080/00268970902717959
    • NLM

      Vieira DS, Degrève L. An insight into the thermostability of a pair of xylanases: the role of hydrogen bonds [Internet]. Molecular Physics. 2009 ; 107( 1): 59-69.[citado 2024 set. 03 ] Available from: https://doi.org/10.1080/00268970902717959
    • Vancouver

      Vieira DS, Degrève L. An insight into the thermostability of a pair of xylanases: the role of hydrogen bonds [Internet]. Molecular Physics. 2009 ; 107( 1): 59-69.[citado 2024 set. 03 ] Available from: https://doi.org/10.1080/00268970902717959
  • Source: Proteins: Structure, Function, and Bioinformatics. Unidade: FFCLRP

    Subjects: BACILOS GRAM-POSITIVOS, PROTEÍNAS, ENZIMAS

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      RULLER, Roberto et al. Thermostable variants of the recombinant xylanase A from Bacillus subtilis produced by directed evolution show reduced heat capacity changes. Proteins: Structure, Function, and Bioinformatics, v. 70, n. 4, p. 1280-1293, 2008Tradução . . Disponível em: https://doi.org/10.1002/prot.21617. Acesso em: 03 set. 2024.
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      Ruller, R., Deliberto, L., Ferreira, T. L., & Ward, R. J. (2008). Thermostable variants of the recombinant xylanase A from Bacillus subtilis produced by directed evolution show reduced heat capacity changes. Proteins: Structure, Function, and Bioinformatics, 70( 4), 1280-1293. doi:10.1002/prot.21617
    • NLM

      Ruller R, Deliberto L, Ferreira TL, Ward RJ. Thermostable variants of the recombinant xylanase A from Bacillus subtilis produced by directed evolution show reduced heat capacity changes [Internet]. Proteins: Structure, Function, and Bioinformatics. 2008 ; 70( 4): 1280-1293.[citado 2024 set. 03 ] Available from: https://doi.org/10.1002/prot.21617
    • Vancouver

      Ruller R, Deliberto L, Ferreira TL, Ward RJ. Thermostable variants of the recombinant xylanase A from Bacillus subtilis produced by directed evolution show reduced heat capacity changes [Internet]. Proteins: Structure, Function, and Bioinformatics. 2008 ; 70( 4): 1280-1293.[citado 2024 set. 03 ] Available from: https://doi.org/10.1002/prot.21617
  • Source: Journal of Colloid and Interface Science. Unidade: FFCLRP

    Subjects: ENZIMAS, DETERGENTES, ELASTICIDADE

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    • ABNT

      RIGOS, Carolina Fortes et al. The association of Na,K-ATPase subunits studied by circular dichroism, surface tension and dilatational elasticity. Journal of Colloid and Interface Science, v. 325, n. 2, p. 478-484, 2008Tradução . . Disponível em: https://doi.org/10.1016/j.jcis.2008.06.011. Acesso em: 03 set. 2024.
    • APA

      Rigos, C. F., Nobre, T. M., Zaniquelli, M. E. D., Ward, R. J., & Ciancaglini, P. (2008). The association of Na,K-ATPase subunits studied by circular dichroism, surface tension and dilatational elasticity. Journal of Colloid and Interface Science, 325( 2), 478-484. doi:10.1016/j.jcis.2008.06.011
    • NLM

      Rigos CF, Nobre TM, Zaniquelli MED, Ward RJ, Ciancaglini P. The association of Na,K-ATPase subunits studied by circular dichroism, surface tension and dilatational elasticity [Internet]. Journal of Colloid and Interface Science. 2008 ; 325( 2): 478-484.[citado 2024 set. 03 ] Available from: https://doi.org/10.1016/j.jcis.2008.06.011
    • Vancouver

      Rigos CF, Nobre TM, Zaniquelli MED, Ward RJ, Ciancaglini P. The association of Na,K-ATPase subunits studied by circular dichroism, surface tension and dilatational elasticity [Internet]. Journal of Colloid and Interface Science. 2008 ; 325( 2): 478-484.[citado 2024 set. 03 ] Available from: https://doi.org/10.1016/j.jcis.2008.06.011
  • Source: Analyst. Unidades: FFCLRP, IFSC

    Subjects: TRYPANOSOMA CRUZI, FÁRMACOS (DESENVOLVIMENTO), DOENÇA DE CHAGAS, ENZIMAS

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      CARDOSO, Carmen Lúcia et al. The development of an immobilized enzyme reactor containing glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma cruzy: the effect of species' specific differences on the immobilization. Analyst, v. 133, n. Ja 2008, p. 93-99, 2008Tradução . . Disponível em: https://doi.org/10.1039/b711145b. Acesso em: 03 set. 2024.
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      Cardoso, C. L., Moraes, M. C. de, Guido, R. V. C., Oliva, G., Andricopulo, A. D., Wainer, I. W., & Cass, Q. B. (2008). The development of an immobilized enzyme reactor containing glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma cruzy: the effect of species' specific differences on the immobilization. Analyst, 133( Ja 2008), 93-99. doi:10.1039/b711145b
    • NLM

      Cardoso CL, Moraes MC de, Guido RVC, Oliva G, Andricopulo AD, Wainer IW, Cass QB. The development of an immobilized enzyme reactor containing glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma cruzy: the effect of species' specific differences on the immobilization [Internet]. Analyst. 2008 ; 133( Ja 2008): 93-99.[citado 2024 set. 03 ] Available from: https://doi.org/10.1039/b711145b
    • Vancouver

      Cardoso CL, Moraes MC de, Guido RVC, Oliva G, Andricopulo AD, Wainer IW, Cass QB. The development of an immobilized enzyme reactor containing glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma cruzy: the effect of species' specific differences on the immobilization [Internet]. Analyst. 2008 ; 133( Ja 2008): 93-99.[citado 2024 set. 03 ] Available from: https://doi.org/10.1039/b711145b
  • Source: Química Nova. Unidade: FFCLRP

    Subjects: ENZIMAS, REATORES BIOQUÍMICOS, CROMATOGRAFIA DE AFINIDADE

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    • ABNT

      CARDOSO, Carmen Lúcia e CASS, Quezia Bezerra e MORAES, Marcela Cristina de. Imobilização de enzimas em suportes cromatográficos: uma ferramenta na busca por substâncias bioativas. Química Nova, v. 32, n. 1, p. 175-187, 2008Tradução . . Disponível em: https://doi.org/10.1590/s0100-40422009000100033. Acesso em: 03 set. 2024.
    • APA

      Cardoso, C. L., Cass, Q. B., & Moraes, M. C. de. (2008). Imobilização de enzimas em suportes cromatográficos: uma ferramenta na busca por substâncias bioativas. Química Nova, 32( 1), 175-187. doi:10.1590/s0100-40422009000100033
    • NLM

      Cardoso CL, Cass QB, Moraes MC de. Imobilização de enzimas em suportes cromatográficos: uma ferramenta na busca por substâncias bioativas [Internet]. Química Nova. 2008 ; 32( 1): 175-187.[citado 2024 set. 03 ] Available from: https://doi.org/10.1590/s0100-40422009000100033
    • Vancouver

      Cardoso CL, Cass QB, Moraes MC de. Imobilização de enzimas em suportes cromatográficos: uma ferramenta na busca por substâncias bioativas [Internet]. Química Nova. 2008 ; 32( 1): 175-187.[citado 2024 set. 03 ] Available from: https://doi.org/10.1590/s0100-40422009000100033
  • Source: Cell Biochemistry and Biophysics. Unidade: FFCLRP

    Assunto: ENZIMAS

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    • ABNT

      RIGOS, Carolina Fortes et al. Lipid bilayer stabilization of the Na, K-ATPase reconstituted in DPPC/DPPE. Cell Biochemistry and Biophysics, v. 44, n. 3, p. 438-445, 2006Tradução . . Acesso em: 03 set. 2024.
    • APA

      Rigos, C. F., Santos, H. de L., Ward, R. J., & Ciancaglini, P. (2006). Lipid bilayer stabilization of the Na, K-ATPase reconstituted in DPPC/DPPE. Cell Biochemistry and Biophysics, 44( 3), 438-445.
    • NLM

      Rigos CF, Santos H de L, Ward RJ, Ciancaglini P. Lipid bilayer stabilization of the Na, K-ATPase reconstituted in DPPC/DPPE. Cell Biochemistry and Biophysics. 2006 ; 44( 3): 438-445.[citado 2024 set. 03 ]
    • Vancouver

      Rigos CF, Santos H de L, Ward RJ, Ciancaglini P. Lipid bilayer stabilization of the Na, K-ATPase reconstituted in DPPC/DPPE. Cell Biochemistry and Biophysics. 2006 ; 44( 3): 438-445.[citado 2024 set. 03 ]
  • Source: Biochimica et Biophysica Acta. Unidade: FFCLRP

    Subjects: FUNGOS, ENZIMAS

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      LÚCIO-ETEROVIC, Agda Karina B. et al. Biochemical characterisation of the trehalase of thermophilic fungi: an enzyme with mixed properties of neutral and acid trehalase. Biochimica et Biophysica Acta, v. 1723, n. 1-3, p. 201-207, 2005Tradução . . Disponível em: https://doi.org/10.1016/j.bbagen.2005.02.011. Acesso em: 03 set. 2024.
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      Lúcio-Eterovic, A. K. B., Jorge, J. A., Polizeli, M. de L. T. de M., & Terenzi, H. F. (2005). Biochemical characterisation of the trehalase of thermophilic fungi: an enzyme with mixed properties of neutral and acid trehalase. Biochimica et Biophysica Acta, 1723( 1-3), 201-207. doi:10.1016/j.bbagen.2005.02.011
    • NLM

      Lúcio-Eterovic AKB, Jorge JA, Polizeli M de LT de M, Terenzi HF. Biochemical characterisation of the trehalase of thermophilic fungi: an enzyme with mixed properties of neutral and acid trehalase [Internet]. Biochimica et Biophysica Acta. 2005 ; 1723( 1-3): 201-207.[citado 2024 set. 03 ] Available from: https://doi.org/10.1016/j.bbagen.2005.02.011
    • Vancouver

      Lúcio-Eterovic AKB, Jorge JA, Polizeli M de LT de M, Terenzi HF. Biochemical characterisation of the trehalase of thermophilic fungi: an enzyme with mixed properties of neutral and acid trehalase [Internet]. Biochimica et Biophysica Acta. 2005 ; 1723( 1-3): 201-207.[citado 2024 set. 03 ] Available from: https://doi.org/10.1016/j.bbagen.2005.02.011

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