Filtros : "Indexado no Current Contents" "ENZIMAS" "FFCLRP" Removidos: "IME-MAT" "HU" Limpar

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  • Source: ChemElectroChem. Unidade: FFCLRP

    Subjects: ENZIMAS, OXIDAÇÃO

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      ANTONIO, Jesimiel Glaycon Rodrigues et al. Evaluation of TEMPO-NH2 and oxalate oxidase enzyme for complete ethylene glycol oxidation. ChemElectroChem, v. 9, n. 19, 2022Tradução . . Disponível em: https://doi.org/10.1002/celc.202200181. Acesso em: 21 jul. 2024.
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      Antonio, J. G. R., Franco, J. H., Almeida, P. Z. de, Polizeli, M. D. L. T. D. M., Minteer, S. D., & Andrade, A. R. de. (2022). Evaluation of TEMPO-NH2 and oxalate oxidase enzyme for complete ethylene glycol oxidation. ChemElectroChem, 9( 19). doi:10.1002/celc.202200181
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      Antonio JGR, Franco JH, Almeida PZ de, Polizeli MDLTDM, Minteer SD, Andrade AR de. Evaluation of TEMPO-NH2 and oxalate oxidase enzyme for complete ethylene glycol oxidation [Internet]. ChemElectroChem. 2022 ; 9( 19):[citado 2024 jul. 21 ] Available from: https://doi.org/10.1002/celc.202200181
    • Vancouver

      Antonio JGR, Franco JH, Almeida PZ de, Polizeli MDLTDM, Minteer SD, Andrade AR de. Evaluation of TEMPO-NH2 and oxalate oxidase enzyme for complete ethylene glycol oxidation [Internet]. ChemElectroChem. 2022 ; 9( 19):[citado 2024 jul. 21 ] Available from: https://doi.org/10.1002/celc.202200181
  • Source: Enzyme and Microbial Technology. Unidade: FFCLRP

    Subjects: BIOMASSA, ENZIMAS, EXPRESSÃO GÊNICA, HIDRÓLISE, LIGNINA, PROTEÍNAS, ENGENHARIA, PROTEÍNAS RECOMBINANTES

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      MARTINS, Manoela e DINAMARCO, Taisa Magnani e GOLDBECK, Rosana. Recombinant chimeric enzymes for lignocellulosic biomass hydrolysis. Enzyme and Microbial Technology, v. 140, 2020Tradução . . Disponível em: https://doi.org/10.1016/j.enzmictec.2020.109647. Acesso em: 21 jul. 2024.
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      Martins, M., Dinamarco, T. M., & Goldbeck, R. (2020). Recombinant chimeric enzymes for lignocellulosic biomass hydrolysis. Enzyme and Microbial Technology, 140. doi:10.1016/j.enzmictec.2020.109647
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      Martins M, Dinamarco TM, Goldbeck R. Recombinant chimeric enzymes for lignocellulosic biomass hydrolysis [Internet]. Enzyme and Microbial Technology. 2020 ; 140[citado 2024 jul. 21 ] Available from: https://doi.org/10.1016/j.enzmictec.2020.109647
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      Martins M, Dinamarco TM, Goldbeck R. Recombinant chimeric enzymes for lignocellulosic biomass hydrolysis [Internet]. Enzyme and Microbial Technology. 2020 ; 140[citado 2024 jul. 21 ] Available from: https://doi.org/10.1016/j.enzmictec.2020.109647
  • Source: Biotechnology Letters. Unidade: FFCLRP

    Subjects: BIOMASSA, CANA-DE-AÇÚCAR, SACARIFICAÇÃO, ENZIMAS

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      MACHADO, Carla Botelho et al. Increased biomass saccharification by supplementation of a commercial enzyme cocktail with endo-arabinanase from Bacillus licheniformis. Biotechnology Letters, v. 37, n. 7, p. 1455-1462, 2015Tradução . . Disponível em: https://doi.org/10.1007/s10529-015-1818-0. Acesso em: 21 jul. 2024.
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      Machado, C. B., Citadini, A. P., Goldbeck, R., Lima, E. A. de, Figueiredo, F. L., Silva, T. M. da, et al. (2015). Increased biomass saccharification by supplementation of a commercial enzyme cocktail with endo-arabinanase from Bacillus licheniformis. Biotechnology Letters, 37( 7), 1455-1462. doi:10.1007/s10529-015-1818-0
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      Machado CB, Citadini AP, Goldbeck R, Lima EA de, Figueiredo FL, Silva TM da, Hoffmam ZB, Sousa AS de, Squina FM, Polizeli M de LT de M, Ruller R, Ward RJ. Increased biomass saccharification by supplementation of a commercial enzyme cocktail with endo-arabinanase from Bacillus licheniformis [Internet]. Biotechnology Letters. 2015 ; 37( 7): 1455-1462.[citado 2024 jul. 21 ] Available from: https://doi.org/10.1007/s10529-015-1818-0
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      Machado CB, Citadini AP, Goldbeck R, Lima EA de, Figueiredo FL, Silva TM da, Hoffmam ZB, Sousa AS de, Squina FM, Polizeli M de LT de M, Ruller R, Ward RJ. Increased biomass saccharification by supplementation of a commercial enzyme cocktail with endo-arabinanase from Bacillus licheniformis [Internet]. Biotechnology Letters. 2015 ; 37( 7): 1455-1462.[citado 2024 jul. 21 ] Available from: https://doi.org/10.1007/s10529-015-1818-0
  • Source: Environmental and Experimental Botany. Unidade: FFCLRP

    Subjects: ENZIMAS, ANTIOXIDANTES, AQUECIMENTO GLOBAL, MUDANÇA CLIMÁTICA

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      MARTINEZ, Carlos Alberto et al. Moderate warming increases PSII performance, antioxidant scavenging systems and biomass production in Stylosanthes capitata Vogel. Environmental and Experimental Botany, v. 102, p. 58-67, 2014Tradução . . Disponível em: https://doi.org/10.1016/j.envexpbot.2014.02.001. Acesso em: 21 jul. 2024.
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      Martinez, C. A., Bianconi, M., Silva, L., Approbato, A., Lemos, M., Santos, L., et al. (2014). Moderate warming increases PSII performance, antioxidant scavenging systems and biomass production in Stylosanthes capitata Vogel. Environmental and Experimental Botany, 102, 58-67. doi:10.1016/j.envexpbot.2014.02.001
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      Martinez CA, Bianconi M, Silva L, Approbato A, Lemos M, Santos L, Curtarelli L, Rodrigues A, Mello T, Manchon F. Moderate warming increases PSII performance, antioxidant scavenging systems and biomass production in Stylosanthes capitata Vogel [Internet]. Environmental and Experimental Botany. 2014 ; 102 58-67.[citado 2024 jul. 21 ] Available from: https://doi.org/10.1016/j.envexpbot.2014.02.001
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      Martinez CA, Bianconi M, Silva L, Approbato A, Lemos M, Santos L, Curtarelli L, Rodrigues A, Mello T, Manchon F. Moderate warming increases PSII performance, antioxidant scavenging systems and biomass production in Stylosanthes capitata Vogel [Internet]. Environmental and Experimental Botany. 2014 ; 102 58-67.[citado 2024 jul. 21 ] Available from: https://doi.org/10.1016/j.envexpbot.2014.02.001
  • Source: Bioprocess and Biosystens Engineering. Unidade: FFCLRP

    Subjects: ASPERGILLUS, ENZIMAS

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      FACCHINI, Fernanda Dell Antonio et al. Production of fibrolytic enzymes by Aspergillus japonicus CO3 using agro-industrial residues with potential application as additives in animal feed. Bioprocess and Biosystens Engineering, v. 34, n. 3, p. 347-355, 2011Tradução . . Disponível em: https://doi.org/10.1007/s00449-010-0477-8. Acesso em: 21 jul. 2024.
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      Facchini, F. D. A., Vici, A. C., Reis, V. R. A., Jorge, J. A., Terenzi, H. F., Reis, R. A., & Polizeli, M. de L. T. de M. (2011). Production of fibrolytic enzymes by Aspergillus japonicus CO3 using agro-industrial residues with potential application as additives in animal feed. Bioprocess and Biosystens Engineering, 34( 3), 347-355. doi:10.1007/s00449-010-0477-8
    • NLM

      Facchini FDA, Vici AC, Reis VRA, Jorge JA, Terenzi HF, Reis RA, Polizeli M de LT de M. Production of fibrolytic enzymes by Aspergillus japonicus CO3 using agro-industrial residues with potential application as additives in animal feed [Internet]. Bioprocess and Biosystens Engineering. 2011 ; 34( 3): 347-355.[citado 2024 jul. 21 ] Available from: https://doi.org/10.1007/s00449-010-0477-8
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      Facchini FDA, Vici AC, Reis VRA, Jorge JA, Terenzi HF, Reis RA, Polizeli M de LT de M. Production of fibrolytic enzymes by Aspergillus japonicus CO3 using agro-industrial residues with potential application as additives in animal feed [Internet]. Bioprocess and Biosystens Engineering. 2011 ; 34( 3): 347-355.[citado 2024 jul. 21 ] Available from: https://doi.org/10.1007/s00449-010-0477-8
  • Source: Biochemical and Biophysical Research Communications. Unidades: FCFRP, FFCLRP

    Subjects: SPINTRÔNICA, ENZIMAS, RESSONÂNCIA PARAMAGNÉTICA, ELETRÔNICA

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      COUTO, Sheila G. e NONATO, Maria Cristina e COSTA FILHO, Antônio José da. Site directed spin labeling studies of Escherichia coli dihydroorotate dehydrogenase N-terminal extension. Biochemical and Biophysical Research Communications, v. 414, n. 3, p. 487-492, 2011Tradução . . Disponível em: https://doi.org/10.1016/j.bbrc.2011.09.092. Acesso em: 21 jul. 2024.
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      Couto, S. G., Nonato, M. C., & Costa Filho, A. J. da. (2011). Site directed spin labeling studies of Escherichia coli dihydroorotate dehydrogenase N-terminal extension. Biochemical and Biophysical Research Communications, 414( 3), 487-492. doi:10.1016/j.bbrc.2011.09.092
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      Couto SG, Nonato MC, Costa Filho AJ da. Site directed spin labeling studies of Escherichia coli dihydroorotate dehydrogenase N-terminal extension [Internet]. Biochemical and Biophysical Research Communications. 2011 ; 414( 3): 487-492.[citado 2024 jul. 21 ] Available from: https://doi.org/10.1016/j.bbrc.2011.09.092
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      Couto SG, Nonato MC, Costa Filho AJ da. Site directed spin labeling studies of Escherichia coli dihydroorotate dehydrogenase N-terminal extension [Internet]. Biochemical and Biophysical Research Communications. 2011 ; 414( 3): 487-492.[citado 2024 jul. 21 ] Available from: https://doi.org/10.1016/j.bbrc.2011.09.092
  • 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: 21 jul. 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.
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      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 jul. 21 ]
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      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 jul. 21 ]
  • 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: 21 jul. 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 jul. 21 ] 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 jul. 21 ] Available from: https://doi.org/10.1016/j.bpc.2009.10.002
  • Source: Carbohydrate Research. Unidade: FFCLRP

    Subjects: FUNGOS, ENZIMAS, BIOQUÍMICA

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      MICHELIN, Michele et al. Purification and characterization of a thermostable α-amylase produced by the fungus Paecilomyces variotii. Carbohydrate Research, v. 345, n. 16, p. 2348-2353, 2010Tradução . . Disponível em: https://doi.org/10.1016/j.carres.2010.08.013. Acesso em: 21 jul. 2024.
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      Michelin, M., Silva, T. M. da, Benassi, V. M., Peixoto-Nogueira, S. de C., Moraes, L. A. B. de, Leão, J. M., et al. (2010). Purification and characterization of a thermostable α-amylase produced by the fungus Paecilomyces variotii. Carbohydrate Research, 345( 16), 2348-2353. doi:10.1016/j.carres.2010.08.013
    • NLM

      Michelin M, Silva TM da, Benassi VM, Peixoto-Nogueira S de C, Moraes LAB de, Leão JM, Jorge JA, Terenzi HF, Polizeli M de LT de M. Purification and characterization of a thermostable α-amylase produced by the fungus Paecilomyces variotii [Internet]. Carbohydrate Research. 2010 ; 345( 16): 2348-2353.[citado 2024 jul. 21 ] Available from: https://doi.org/10.1016/j.carres.2010.08.013
    • Vancouver

      Michelin M, Silva TM da, Benassi VM, Peixoto-Nogueira S de C, Moraes LAB de, Leão JM, Jorge JA, Terenzi HF, Polizeli M de LT de M. Purification and characterization of a thermostable α-amylase produced by the fungus Paecilomyces variotii [Internet]. Carbohydrate Research. 2010 ; 345( 16): 2348-2353.[citado 2024 jul. 21 ] Available from: https://doi.org/10.1016/j.carres.2010.08.013
  • Source: Journal of Physical Chemistry Part B. Unidades: FFCLRP, IF

    Assunto: ENZIMAS

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      BARBOSA, Leandro Ramos Souza et al. Unraveling the NA,K-ATPase ‘alpha’4 subunit assembling induced by large amounts of 'C IND.12' 'E IND.8' by means of small-angle X-ray scattering. Journal of Physical Chemistry Part B, v. 114, n. 35, p. 11371-11376, 2010Tradução . . Disponível em: http://pubs.acs.org/doi/pdf/10.1021/jp1013829. Acesso em: 21 jul. 2024.
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      Barbosa, L. R. S., Rigos, C. F., Yoneda, J. S., Itri, R., & Ciancaglini, P. (2010). Unraveling the NA,K-ATPase ‘alpha’4 subunit assembling induced by large amounts of 'C IND.12' 'E IND.8' by means of small-angle X-ray scattering. Journal of Physical Chemistry Part B, 114( 35), 11371-11376. Recuperado de http://pubs.acs.org/doi/pdf/10.1021/jp1013829
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      Barbosa LRS, Rigos CF, Yoneda JS, Itri R, Ciancaglini P. Unraveling the NA,K-ATPase ‘alpha’4 subunit assembling induced by large amounts of 'C IND.12' 'E IND.8' by means of small-angle X-ray scattering [Internet]. Journal of Physical Chemistry Part B. 2010 ; 114( 35): 11371-11376.[citado 2024 jul. 21 ] Available from: http://pubs.acs.org/doi/pdf/10.1021/jp1013829
    • Vancouver

      Barbosa LRS, Rigos CF, Yoneda JS, Itri R, Ciancaglini P. Unraveling the NA,K-ATPase ‘alpha’4 subunit assembling induced by large amounts of 'C IND.12' 'E IND.8' by means of small-angle X-ray scattering [Internet]. Journal of Physical Chemistry Part B. 2010 ; 114( 35): 11371-11376.[citado 2024 jul. 21 ] Available from: http://pubs.acs.org/doi/pdf/10.1021/jp1013829
  • 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: 21 jul. 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 jul. 21 ] 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 jul. 21 ] Available from: https://doi.org/10.1007/s00011-008-8137-z
  • 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: 21 jul. 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
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      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 jul. 21 ] 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 jul. 21 ] 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: 21 jul. 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 jul. 21 ] 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 jul. 21 ] 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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      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: 21 jul. 2024.
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      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 jul. 21 ] 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 jul. 21 ] Available from: https://doi.org/10.1016/j.jcis.2008.06.011
  • Source: Cell Biochemistry and Biophysics. Unidade: FFCLRP

    Assunto: ENZIMAS

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      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: 21 jul. 2024.
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      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 jul. 21 ]
    • 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 jul. 21 ]
  • 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: 21 jul. 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 jul. 21 ] 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 jul. 21 ] Available from: https://doi.org/10.1016/j.bbagen.2005.02.011
  • Source: International Journal of Biochemistry and Cell Biology. Unidade: FFCLRP

    Subjects: CRUSTÁCEOS, ENZIMAS, BIOQUÍMICA

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    • ABNT

      MASUI, D. C. et al. Gill microsomal ('Na POT.+', 'K POT. +')-ATPase from the blue crab Callinectes danae: interactions at cationic sites. International Journal of Biochemistry and Cell Biology, v. 37, p. 2521-2535, 2005Tradução . . Acesso em: 21 jul. 2024.
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      Masui, D. C., Silva, E. C. C., Mantelatto, F. L. M., McNamara, J. C., Barrabin, H., Scofano, H. M., et al. (2005). Gill microsomal ('Na POT.+', 'K POT. +')-ATPase from the blue crab Callinectes danae: interactions at cationic sites. International Journal of Biochemistry and Cell Biology, 37, 2521-2535.
    • NLM

      Masui DC, Silva ECC, Mantelatto FLM, McNamara JC, Barrabin H, Scofano HM, Fontes CFL, Leone F de A. Gill microsomal ('Na POT.+', 'K POT. +')-ATPase from the blue crab Callinectes danae: interactions at cationic sites. International Journal of Biochemistry and Cell Biology. 2005 ; 37 2521-2535.[citado 2024 jul. 21 ]
    • Vancouver

      Masui DC, Silva ECC, Mantelatto FLM, McNamara JC, Barrabin H, Scofano HM, Fontes CFL, Leone F de A. Gill microsomal ('Na POT.+', 'K POT. +')-ATPase from the blue crab Callinectes danae: interactions at cationic sites. International Journal of Biochemistry and Cell Biology. 2005 ; 37 2521-2535.[citado 2024 jul. 21 ]
  • Source: Acta Crystallographica Section F. Unidade: FFCLRP

    Subjects: ENZIMAS, BACILOS GRAM-POSITIVOS

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      MURAKAMI, M. T. et al. Crystallization and preliminary x-ray crystallographic studies of the mesophilic xylanase a from Bacillus 1 a1. Acta Crystallographica Section F, v. F61, p. 219-220, 2005Tradução . . Acesso em: 21 jul. 2024.
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      Murakami, M. T., Ruller, R., Ward, R. J., & Arni, R. K. (2005). Crystallization and preliminary x-ray crystallographic studies of the mesophilic xylanase a from Bacillus 1 a1. Acta Crystallographica Section F, F61, 219-220.
    • NLM

      Murakami MT, Ruller R, Ward RJ, Arni RK. Crystallization and preliminary x-ray crystallographic studies of the mesophilic xylanase a from Bacillus 1 a1. Acta Crystallographica Section F. 2005 ; F61 219-220.[citado 2024 jul. 21 ]
    • Vancouver

      Murakami MT, Ruller R, Ward RJ, Arni RK. Crystallization and preliminary x-ray crystallographic studies of the mesophilic xylanase a from Bacillus 1 a1. Acta Crystallographica Section F. 2005 ; F61 219-220.[citado 2024 jul. 21 ]
  • Source: FEMS Microbiology Letters. Unidade: FFCLRP

    Subjects: FUNGOS, ENZIMAS, IMUNOQUÍMICA

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      AQUINO, Ana Carla M. M. de et al. Characterisation of an acid trehalase produced by the thermotolerant fungus Rhizopus microsporus var. rhizopodiformis: biochemical properties and immunochemical localisation. FEMS Microbiology Letters, v. 251, n. 1, p. 169-175, 2005Tradução . . Disponível em: https://doi.org/10.1016/j.femsle.2005.07.045. Acesso em: 21 jul. 2024.
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      Aquino, A. C. M. M. de, Peixoto-Nogueira, S. C., Jorge, J. A., Terenzi, H. F., & Polizeli, M. de L. T. de M. (2005). Characterisation of an acid trehalase produced by the thermotolerant fungus Rhizopus microsporus var. rhizopodiformis: biochemical properties and immunochemical localisation. FEMS Microbiology Letters, 251( 1), 169-175. doi:10.1016/j.femsle.2005.07.045
    • NLM

      Aquino ACMM de, Peixoto-Nogueira SC, Jorge JA, Terenzi HF, Polizeli M de LT de M. Characterisation of an acid trehalase produced by the thermotolerant fungus Rhizopus microsporus var. rhizopodiformis: biochemical properties and immunochemical localisation [Internet]. FEMS Microbiology Letters. 2005 ; 251( 1): 169-175.[citado 2024 jul. 21 ] Available from: https://doi.org/10.1016/j.femsle.2005.07.045
    • Vancouver

      Aquino ACMM de, Peixoto-Nogueira SC, Jorge JA, Terenzi HF, Polizeli M de LT de M. Characterisation of an acid trehalase produced by the thermotolerant fungus Rhizopus microsporus var. rhizopodiformis: biochemical properties and immunochemical localisation [Internet]. FEMS Microbiology Letters. 2005 ; 251( 1): 169-175.[citado 2024 jul. 21 ] Available from: https://doi.org/10.1016/j.femsle.2005.07.045
  • Source: Biotechnology and Applied Biochemistry. Unidade: FFCLRP

    Subjects: ASPERGILLUS, BIOQUÍMICA, ENZIMAS

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      GUIMARÃES, Luis Henrique Souza et al. Characterization and properties of acid phosphatases with phytase activity produced by Aspergillus caespitosus. Biotechnology and Applied Biochemistry, v. 39, p. 1-7, 2004Tradução . . Disponível em: https://doi.org/10.1042/ba20030208. Acesso em: 21 jul. 2024.
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      Guimarães, L. H. S., Terenzi, H. F., Jorge, J. A., Leone, F. de A., & Polizeli, M. de L. T. de M. (2004). Characterization and properties of acid phosphatases with phytase activity produced by Aspergillus caespitosus. Biotechnology and Applied Biochemistry, 39, 1-7. doi:10.1042/ba20030208
    • NLM

      Guimarães LHS, Terenzi HF, Jorge JA, Leone F de A, Polizeli M de LT de M. Characterization and properties of acid phosphatases with phytase activity produced by Aspergillus caespitosus [Internet]. Biotechnology and Applied Biochemistry. 2004 ; 39 1-7.[citado 2024 jul. 21 ] Available from: https://doi.org/10.1042/ba20030208
    • Vancouver

      Guimarães LHS, Terenzi HF, Jorge JA, Leone F de A, Polizeli M de LT de M. Characterization and properties of acid phosphatases with phytase activity produced by Aspergillus caespitosus [Internet]. Biotechnology and Applied Biochemistry. 2004 ; 39 1-7.[citado 2024 jul. 21 ] Available from: https://doi.org/10.1042/ba20030208

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