Filtros : "Indexado no BIOSIS" "ENZIMAS" Removido: "Richeldi, Luca" Limpar

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  • Source: Cellular and Molecular Life Sciences. Unidade: FMRP

    Subjects: NEOPLASIAS, PÂNCREAS, PANCREATOPATIAS, ENZIMAS

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      RUCKERT, Mariana Tannús et al. Protein tyrosine phosphatases: promising targets in pancreatic ductal adenocarcinoma. Cellular and Molecular Life Sciences, v. 76, n. 13, p. 2571-2592, 2019Tradução . . Disponível em: https://doi.org/10.1007/s00018-019-03095-4. Acesso em: 04 out. 2024.
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      Ruckert, M. T., Andrade, P. V. de, Santos, V. S., & Silveira, V. da S. (2019). Protein tyrosine phosphatases: promising targets in pancreatic ductal adenocarcinoma. Cellular and Molecular Life Sciences, 76( 13), 2571-2592. doi:10.1007/s00018-019-03095-4
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      Ruckert MT, Andrade PV de, Santos VS, Silveira V da S. Protein tyrosine phosphatases: promising targets in pancreatic ductal adenocarcinoma [Internet]. Cellular and Molecular Life Sciences. 2019 ; 76( 13): 2571-2592.[citado 2024 out. 04 ] Available from: https://doi.org/10.1007/s00018-019-03095-4
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      Ruckert MT, Andrade PV de, Santos VS, Silveira V da S. Protein tyrosine phosphatases: promising targets in pancreatic ductal adenocarcinoma [Internet]. Cellular and Molecular Life Sciences. 2019 ; 76( 13): 2571-2592.[citado 2024 out. 04 ] Available from: https://doi.org/10.1007/s00018-019-03095-4
  • Source: Applied Microbiology and Biotechnology. Unidade: FCFRP

    Subjects: VENENOS, ESCORPIÕES, ENZIMAS, LEVEDURAS

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      AMORIM, Fernanda Gobbi et al. Heterologous expression of rTsHyal-1: the first recombinant hyaluronidase of scorpion venom produced in Pichia pastoris system. Applied Microbiology and Biotechnology, v. 102, n. 7, p. 3145-3158, 2018Tradução . . Disponível em: https://doi.org/10.1007/s00253-018-8821-z. Acesso em: 04 out. 2024.
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      Amorim, F. G., Boldrini-França, J., Bordon, K. de C. F., Cardoso, I. A., Pauw, E. D., Quinton, L., et al. (2018). Heterologous expression of rTsHyal-1: the first recombinant hyaluronidase of scorpion venom produced in Pichia pastoris system. Applied Microbiology and Biotechnology, 102( 7), 3145-3158. doi:10.1007/s00253-018-8821-z
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      Amorim FG, Boldrini-França J, Bordon K de CF, Cardoso IA, Pauw ED, Quinton L, Kashima S, Braga ECA. Heterologous expression of rTsHyal-1: the first recombinant hyaluronidase of scorpion venom produced in Pichia pastoris system [Internet]. Applied Microbiology and Biotechnology. 2018 ; 102( 7): 3145-3158.[citado 2024 out. 04 ] Available from: https://doi.org/10.1007/s00253-018-8821-z
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      Amorim FG, Boldrini-França J, Bordon K de CF, Cardoso IA, Pauw ED, Quinton L, Kashima S, Braga ECA. Heterologous expression of rTsHyal-1: the first recombinant hyaluronidase of scorpion venom produced in Pichia pastoris system [Internet]. Applied Microbiology and Biotechnology. 2018 ; 102( 7): 3145-3158.[citado 2024 out. 04 ] Available from: https://doi.org/10.1007/s00253-018-8821-z
  • Source: Journal of Venomous Animals and Toxins including Tropical Diseases. Unidade: FCFRP

    Subjects: COBRAS, VENENOS, AMINOÁCIDOS, ENZIMAS, BIOTECNOLOGIA

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      COSTA, Tássia Rafaella et al. Kinetic investigations and stability studies of two Bothrops L-amino acid oxidases. Journal of Venomous Animals and Toxins including Tropical Diseases, v. 24, 2018Tradução . . Disponível em: https://doi.org/10.1186/s40409-018-0172-9. Acesso em: 04 out. 2024.
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      Costa, T. R., Carone, S. E. I., Tucci, L. F. F., Menaldo, D. L., Rosa-Garzon, N. G. da, Cabral, H., & Sampaio, S. V. (2018). Kinetic investigations and stability studies of two Bothrops L-amino acid oxidases. Journal of Venomous Animals and Toxins including Tropical Diseases, 24. doi:10.1186/s40409-018-0172-9
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      Costa TR, Carone SEI, Tucci LFF, Menaldo DL, Rosa-Garzon NG da, Cabral H, Sampaio SV. Kinetic investigations and stability studies of two Bothrops L-amino acid oxidases [Internet]. Journal of Venomous Animals and Toxins including Tropical Diseases. 2018 ; 24[citado 2024 out. 04 ] Available from: https://doi.org/10.1186/s40409-018-0172-9
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      Costa TR, Carone SEI, Tucci LFF, Menaldo DL, Rosa-Garzon NG da, Cabral H, Sampaio SV. Kinetic investigations and stability studies of two Bothrops L-amino acid oxidases [Internet]. Journal of Venomous Animals and Toxins including Tropical Diseases. 2018 ; 24[citado 2024 out. 04 ] Available from: https://doi.org/10.1186/s40409-018-0172-9
  • Source: International Journal of Biological Macromolecules. Unidades: FFCLRP, FMRP

    Subjects: ENZIMAS, HIDRÓLISE, OLIGOSSACARÍDEOS

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      CARNEIRO, Lara Aparecida Buffoni de Campos et al. Characterization of a β-galactosidase from Bacillus subtilis with transgalactosylation activity. International Journal of Biological Macromolecules, v. 120, p. 279-287, 2018Tradução . . Disponível em: https://doi.org/10.1016/j.ijbiomac.2018.07.116. Acesso em: 04 out. 2024.
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      Carneiro, L. A. B. de C., Yu, L., Dupree, P., & Ward, R. J. (2018). Characterization of a β-galactosidase from Bacillus subtilis with transgalactosylation activity. International Journal of Biological Macromolecules, 120, 279-287. doi:10.1016/j.ijbiomac.2018.07.116
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      Carneiro LAB de C, Yu L, Dupree P, Ward RJ. Characterization of a β-galactosidase from Bacillus subtilis with transgalactosylation activity [Internet]. International Journal of Biological Macromolecules. 2018 ; 120 279-287.[citado 2024 out. 04 ] Available from: https://doi.org/10.1016/j.ijbiomac.2018.07.116
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      Carneiro LAB de C, Yu L, Dupree P, Ward RJ. Characterization of a β-galactosidase from Bacillus subtilis with transgalactosylation activity [Internet]. International Journal of Biological Macromolecules. 2018 ; 120 279-287.[citado 2024 out. 04 ] Available from: https://doi.org/10.1016/j.ijbiomac.2018.07.116
  • Source: Process Biochemistry. Unidades: FCFRP, FFCLRP

    Subjects: ASPERGILLUS, ENZIMAS, BIOTECNOLOGIA

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      HEINEN, P. R. et al. Immobilized endo-xylanase of Aspergillus tamarii Kita: an interesting biological tool for production of xylooligosaccharides at high temperatures. Process Biochemistry, v. 53, p. 145-152, 2017Tradução . . Disponível em: https://doi.org/10.1016/j.procbio.2016.11.021. Acesso em: 04 out. 2024.
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      Heinen, P. R., Pereira, M. G., Vargas-Rechia, C. G., Almeida, P. Z., Monteiro, L. M. O., Pasin, T. M., et al. (2017). Immobilized endo-xylanase of Aspergillus tamarii Kita: an interesting biological tool for production of xylooligosaccharides at high temperatures. Process Biochemistry, 53, 145-152. doi:10.1016/j.procbio.2016.11.021
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      Heinen PR, Pereira MG, Vargas-Rechia CG, Almeida PZ, Monteiro LMO, Pasin TM, Messias JM, Cereia M, Kadowaki MK, Jorge JA, Polizeli M de LT de M. Immobilized endo-xylanase of Aspergillus tamarii Kita: an interesting biological tool for production of xylooligosaccharides at high temperatures [Internet]. Process Biochemistry. 2017 ; 53 145-152.[citado 2024 out. 04 ] Available from: https://doi.org/10.1016/j.procbio.2016.11.021
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      Heinen PR, Pereira MG, Vargas-Rechia CG, Almeida PZ, Monteiro LMO, Pasin TM, Messias JM, Cereia M, Kadowaki MK, Jorge JA, Polizeli M de LT de M. Immobilized endo-xylanase of Aspergillus tamarii Kita: an interesting biological tool for production of xylooligosaccharides at high temperatures [Internet]. Process Biochemistry. 2017 ; 53 145-152.[citado 2024 out. 04 ] Available from: https://doi.org/10.1016/j.procbio.2016.11.021
  • Source: Reproduction, Fertility and Development. Unidade: FMVZ

    Subjects: BOVINOS (EMBRIOLOGIA), EMBRIOLOGIA ANIMAL, ENZIMAS, ESPECTROFOTOMETRIA

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      GONÇALVES, Roseli F et al. Analysis and characterisation of bovine oocyte and embryo biomarkers by matrix-assisted desorption ionisation mass spectrometry imaging. Reproduction, Fertility and Development, v. 28, n. 3, p. 293-301, 2016Tradução . . Disponível em: https://doi.org/10.1071/RD14047. Acesso em: 04 out. 2024.
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      Gonçalves, R. F., Ferreira, M. S., Oliveira, D. N. de, Canevarolo, R., Achilles, M. A., D’Ercole, D. L., et al. (2016). Analysis and characterisation of bovine oocyte and embryo biomarkers by matrix-assisted desorption ionisation mass spectrometry imaging. Reproduction, Fertility and Development, 28( 3), 293-301. doi:10.1071/RD14047
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      Gonçalves RF, Ferreira MS, Oliveira DN de, Canevarolo R, Achilles MA, D’Ercole DL, Bols PE, Visintin JA, Killian GJ, Catharino RR. Analysis and characterisation of bovine oocyte and embryo biomarkers by matrix-assisted desorption ionisation mass spectrometry imaging [Internet]. Reproduction, Fertility and Development. 2016 ; 28( 3): 293-301.[citado 2024 out. 04 ] Available from: https://doi.org/10.1071/RD14047
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      Gonçalves RF, Ferreira MS, Oliveira DN de, Canevarolo R, Achilles MA, D’Ercole DL, Bols PE, Visintin JA, Killian GJ, Catharino RR. Analysis and characterisation of bovine oocyte and embryo biomarkers by matrix-assisted desorption ionisation mass spectrometry imaging [Internet]. Reproduction, Fertility and Development. 2016 ; 28( 3): 293-301.[citado 2024 out. 04 ] Available from: https://doi.org/10.1071/RD14047
  • Source: Current Microbiology. Unidade: FMVZ

    Subjects: ENZIMAS, LEPTOSPIROSE ANIMAL, SUÍNOS

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      HARTLEBEN, Cláudia P et al. Serological analysis by enzyme-Linked immunosorbent assay using recombinant antigen LipL32 for the diagnosis of swine leptospirosis. Current Microbiology, v. 66, n. 2, p. 106-109, 2013Tradução . . Disponível em: https://doi.org/10.1007/s00284-012-0237-x. Acesso em: 04 out. 2024.
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      Hartleben, C. P., Leal, F. M. A., Monte, L. G., Hartwig, D. D., Seixas, F. K., Vasconcellos, S. A., et al. (2013). Serological analysis by enzyme-Linked immunosorbent assay using recombinant antigen LipL32 for the diagnosis of swine leptospirosis. Current Microbiology, 66( 2), 106-109. doi:10.1007/s00284-012-0237-x
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      Hartleben CP, Leal FMA, Monte LG, Hartwig DD, Seixas FK, Vasconcellos SA, Brihuega B, Dellagostin OA. Serological analysis by enzyme-Linked immunosorbent assay using recombinant antigen LipL32 for the diagnosis of swine leptospirosis [Internet]. Current Microbiology. 2013 ; 66( 2): 106-109.[citado 2024 out. 04 ] Available from: https://doi.org/10.1007/s00284-012-0237-x
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      Hartleben CP, Leal FMA, Monte LG, Hartwig DD, Seixas FK, Vasconcellos SA, Brihuega B, Dellagostin OA. Serological analysis by enzyme-Linked immunosorbent assay using recombinant antigen LipL32 for the diagnosis of swine leptospirosis [Internet]. Current Microbiology. 2013 ; 66( 2): 106-109.[citado 2024 out. 04 ] Available from: https://doi.org/10.1007/s00284-012-0237-x
  • Source: Revista Brasileira de Zootecnia. Unidade: FMVZ

    Subjects: AVES, ENZIMAS, EXCREÇÃO ANIMAL, FÓSFORO, SOJA

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      MARTINS, Bianca Almeida Brandão et al. Bioavailability and poultry fecal excretion of phosphorus from soybean-based diets supplemented with phytase. Revista Brasileira de Zootecnia, v. 42, n. 3, p. 174-182, 2013Tradução . . Disponível em: https://doi.org/10.1590/S1516-35982013000300005. Acesso em: 04 out. 2024.
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      Martins, B. A. B., Borgatti, L. M. O., Souza, L. W. de O., Robassini, S. L. D. A., & Albuquerque, R. de. (2013). Bioavailability and poultry fecal excretion of phosphorus from soybean-based diets supplemented with phytase. Revista Brasileira de Zootecnia, 42( 3), 174-182. doi:10.1590/S1516-35982013000300005
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      Martins BAB, Borgatti LMO, Souza LW de O, Robassini SLDA, Albuquerque R de. Bioavailability and poultry fecal excretion of phosphorus from soybean-based diets supplemented with phytase [Internet]. Revista Brasileira de Zootecnia. 2013 ; 42( 3): 174-182.[citado 2024 out. 04 ] Available from: https://doi.org/10.1590/S1516-35982013000300005
    • Vancouver

      Martins BAB, Borgatti LMO, Souza LW de O, Robassini SLDA, Albuquerque R de. Bioavailability and poultry fecal excretion of phosphorus from soybean-based diets supplemented with phytase [Internet]. Revista Brasileira de Zootecnia. 2013 ; 42( 3): 174-182.[citado 2024 out. 04 ] Available from: https://doi.org/10.1590/S1516-35982013000300005
  • Source: Revista Brasileira de Parasitologia. Unidade: FMVZ

    Subjects: INFECÇÃO EXPERIMENTAL ANIMAL, CÃES, ENZIMAS

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      COSTA, Marcio Machado et al. Rangelia vitalii: changes in the enzymes ALT, CK and AST during the acute phase of experimental infection in dogs. Revista Brasileira de Parasitologia, v. 21, n. 3, p. 243-248, 2012Tradução . . Disponível em: https://doi.org/10.1590/s1984-29612012000300012. Acesso em: 04 out. 2024.
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      Costa, M. M., França, R. T., Silva, A. S. da, Paim, C. B., Paim, F. C., Amaral, C. H. do, et al. (2012). Rangelia vitalii: changes in the enzymes ALT, CK and AST during the acute phase of experimental infection in dogs. Revista Brasileira de Parasitologia, 21( 3), 243-248. doi:10.1590/s1984-29612012000300012
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      Costa MM, França RT, Silva AS da, Paim CB, Paim FC, Amaral CH do, Dornelles GL, Cunha JPMCM da, Soares JF, Labruna MB, Mazzanti CMA, Monteiro SG, Lopes ST dos A. Rangelia vitalii: changes in the enzymes ALT, CK and AST during the acute phase of experimental infection in dogs [Internet]. Revista Brasileira de Parasitologia. 2012 ; 21( 3): 243-248.[citado 2024 out. 04 ] Available from: https://doi.org/10.1590/s1984-29612012000300012
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      Costa MM, França RT, Silva AS da, Paim CB, Paim FC, Amaral CH do, Dornelles GL, Cunha JPMCM da, Soares JF, Labruna MB, Mazzanti CMA, Monteiro SG, Lopes ST dos A. Rangelia vitalii: changes in the enzymes ALT, CK and AST during the acute phase of experimental infection in dogs [Internet]. Revista Brasileira de Parasitologia. 2012 ; 21( 3): 243-248.[citado 2024 out. 04 ] Available from: https://doi.org/10.1590/s1984-29612012000300012
  • Source: Applied Biochemistry and Biotechnology. Unidade: FCF

    Subjects: ÁCIDOS ASCÓRBICOS, ABÓBORA MORANGA, ENZIMAS

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      PORTO, Tatiana Souza et al. Extraction of ascorbate oxidase from Cucurbita maxima by continuous process in perforated rotating disc contactor using aqueous two-phase systems. Applied Biochemistry and Biotechnology, v. 160, n. 4, p. 1057-1064, 2010Tradução . . Disponível em: http://www.springerlink.com/content/b492j15r6474q637/fulltext.pdf. Acesso em: 04 out. 2024.
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      Porto, T. S., Marques, P. P., Porto, C. S., Moreira, K. A., Lima Filho, J. L. de, Converti, A., et al. (2010). Extraction of ascorbate oxidase from Cucurbita maxima by continuous process in perforated rotating disc contactor using aqueous two-phase systems. Applied Biochemistry and Biotechnology, 160( 4), 1057-1064. Recuperado de http://www.springerlink.com/content/b492j15r6474q637/fulltext.pdf
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      Porto TS, Marques PP, Porto CS, Moreira KA, Lima Filho JL de, Converti A, Pessoa Junior A, Porto ALF. Extraction of ascorbate oxidase from Cucurbita maxima by continuous process in perforated rotating disc contactor using aqueous two-phase systems [Internet]. Applied Biochemistry and Biotechnology. 2010 ; 160( 4): 1057-1064.[citado 2024 out. 04 ] Available from: http://www.springerlink.com/content/b492j15r6474q637/fulltext.pdf
    • Vancouver

      Porto TS, Marques PP, Porto CS, Moreira KA, Lima Filho JL de, Converti A, Pessoa Junior A, Porto ALF. Extraction of ascorbate oxidase from Cucurbita maxima by continuous process in perforated rotating disc contactor using aqueous two-phase systems [Internet]. Applied Biochemistry and Biotechnology. 2010 ; 160( 4): 1057-1064.[citado 2024 out. 04 ] Available from: http://www.springerlink.com/content/b492j15r6474q637/fulltext.pdf
  • Source: Insect Biochemistry and Molecular Biology. Unidade: IQ

    Subjects: COLEOPTERA, DIGESTÃO ANIMAL, ENZIMAS

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      GENTA, Fernando Ariel et al. Purification, characterization and sequencing of the major 'beta'-1,3-glucanase from the midgut of Tenebrio molitor larvae. Insect Biochemistry and Molecular Biology, v. 39, n. 12, p. 861-874, 2009Tradução . . Disponível em: https://doi.org/10.1016/j.ibmb.2009.10.003. Acesso em: 04 out. 2024.
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      Genta, F. A., Bragatto, I., Terra, W. R., & Ferreira, C. (2009). Purification, characterization and sequencing of the major 'beta'-1,3-glucanase from the midgut of Tenebrio molitor larvae. Insect Biochemistry and Molecular Biology, 39( 12), 861-874. doi:10.1016/j.ibmb.2009.10.003
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      Genta FA, Bragatto I, Terra WR, Ferreira C. Purification, characterization and sequencing of the major 'beta'-1,3-glucanase from the midgut of Tenebrio molitor larvae [Internet]. Insect Biochemistry and Molecular Biology. 2009 ; 39( 12): 861-874.[citado 2024 out. 04 ] Available from: https://doi.org/10.1016/j.ibmb.2009.10.003
    • Vancouver

      Genta FA, Bragatto I, Terra WR, Ferreira C. Purification, characterization and sequencing of the major 'beta'-1,3-glucanase from the midgut of Tenebrio molitor larvae [Internet]. Insect Biochemistry and Molecular Biology. 2009 ; 39( 12): 861-874.[citado 2024 out. 04 ] Available from: https://doi.org/10.1016/j.ibmb.2009.10.003
  • Source: Journal of Chromatography B - Analytical Technologies in the Biomedical and Life Sciences. Unidade: FCF

    Subjects: EXTRAÇÃO DE LÍQUIDOS, ENZIMAS

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      FEITOSA, Eloi et al. Phase diagrams of a CTAB/organic solvent/buffer system applied to extraction of enzymes by reverse micelles. Journal of Chromatography B - Analytical Technologies in the Biomedical and Life Sciences, v. 862, n. 1-2, p. 58-63, 2008Tradução . . Disponível em: https://doi.org/10.1016/j.jchromb.2007.10.046. Acesso em: 04 out. 2024.
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      Feitosa, E., Catelam, K. T., Hasmann, F. A., Johansson, H. -O., Roberto, I. C., & Pessoa Junior, A. (2008). Phase diagrams of a CTAB/organic solvent/buffer system applied to extraction of enzymes by reverse micelles. Journal of Chromatography B - Analytical Technologies in the Biomedical and Life Sciences, 862( 1-2), 58-63. doi:10.1016/j.jchromb.2007.10.046
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      Feitosa E, Catelam KT, Hasmann FA, Johansson H-O, Roberto IC, Pessoa Junior A. Phase diagrams of a CTAB/organic solvent/buffer system applied to extraction of enzymes by reverse micelles [Internet]. Journal of Chromatography B - Analytical Technologies in the Biomedical and Life Sciences. 2008 ;862( 1-2): 58-63.[citado 2024 out. 04 ] Available from: https://doi.org/10.1016/j.jchromb.2007.10.046
    • Vancouver

      Feitosa E, Catelam KT, Hasmann FA, Johansson H-O, Roberto IC, Pessoa Junior A. Phase diagrams of a CTAB/organic solvent/buffer system applied to extraction of enzymes by reverse micelles [Internet]. Journal of Chromatography B - Analytical Technologies in the Biomedical and Life Sciences. 2008 ;862( 1-2): 58-63.[citado 2024 out. 04 ] Available from: https://doi.org/10.1016/j.jchromb.2007.10.046
  • Source: Insect Biochemistry and Molecular Biology. Unidade: IQ

    Subjects: BIOQUÍMICA, DIGESTÃO ANIMAL, ENZIMAS

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      SATO, Paloma Mieko et al. Subsite substrate specificity of midgut insect chymotrypsins. Insect Biochemistry and Molecular Biology, v. 38, n. 6, p. 628-633, 2008Tradução . . Disponível em: https://doi.org/10.1016/j.ibmb.2008.03.006. Acesso em: 04 out. 2024.
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      Sato, P. M., Lopes, A. R., Juliano, L., Juliano, M. A., & Terra, W. R. (2008). Subsite substrate specificity of midgut insect chymotrypsins. Insect Biochemistry and Molecular Biology, 38( 6), 628-633. doi:10.1016/j.ibmb.2008.03.006
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      Sato PM, Lopes AR, Juliano L, Juliano MA, Terra WR. Subsite substrate specificity of midgut insect chymotrypsins [Internet]. Insect Biochemistry and Molecular Biology. 2008 ;38( 6): 628-633.[citado 2024 out. 04 ] Available from: https://doi.org/10.1016/j.ibmb.2008.03.006
    • Vancouver

      Sato PM, Lopes AR, Juliano L, Juliano MA, Terra WR. Subsite substrate specificity of midgut insect chymotrypsins [Internet]. Insect Biochemistry and Molecular Biology. 2008 ;38( 6): 628-633.[citado 2024 out. 04 ] Available from: https://doi.org/10.1016/j.ibmb.2008.03.006
  • Source: Biochimica et Biophysica Acta - Molecular Basis of Disease. Unidade: IQ

    Subjects: BIOQUÍMICA, ENZIMAS

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      GENTA, Fernando Ariel et al. The interplay of processivity, substrate inhibition and a secondary substrate binding site of an insect exo-'beta'-1,3-glucanase. Biochimica et Biophysica Acta - Molecular Basis of Disease, v. 1774, n. 9, p. 1079-1091, 2007Tradução . . Disponível em: https://doi.org/10.1016/j.bbapap.2007.07.006. Acesso em: 04 out. 2024.
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      Genta, F. A., Dumont, A. F., Marana, S. R., Terra, W. R., & Ferreira, C. (2007). The interplay of processivity, substrate inhibition and a secondary substrate binding site of an insect exo-'beta'-1,3-glucanase. Biochimica et Biophysica Acta - Molecular Basis of Disease, 1774( 9), 1079-1091. doi:10.1016/j.bbapap.2007.07.006
    • NLM

      Genta FA, Dumont AF, Marana SR, Terra WR, Ferreira C. The interplay of processivity, substrate inhibition and a secondary substrate binding site of an insect exo-'beta'-1,3-glucanase [Internet]. Biochimica et Biophysica Acta - Molecular Basis of Disease. 2007 ; 1774( 9): 1079-1091.[citado 2024 out. 04 ] Available from: https://doi.org/10.1016/j.bbapap.2007.07.006
    • Vancouver

      Genta FA, Dumont AF, Marana SR, Terra WR, Ferreira C. The interplay of processivity, substrate inhibition and a secondary substrate binding site of an insect exo-'beta'-1,3-glucanase [Internet]. Biochimica et Biophysica Acta - Molecular Basis of Disease. 2007 ; 1774( 9): 1079-1091.[citado 2024 out. 04 ] Available from: https://doi.org/10.1016/j.bbapap.2007.07.006
  • Source: Enzyme and Microbial Technology. Unidade: FCF

    Subjects: OXIDAÇÃO, FERMENTAÇÃO, ENZIMAS

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      TOMOTANI, Ester Junko e VITOLO, Michele. Immobilized glucose oxidase as a catalyst to the conversion of glucose into gluconic acid using a membrane reactor. Enzyme and Microbial Technology, v. 40, n. 5, p. 1020-1025, 2007Tradução . . Disponível em: https://doi.org/10.1016/j.enzmictec.2006.07.039. Acesso em: 04 out. 2024.
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      Tomotani, E. J., & Vitolo, M. (2007). Immobilized glucose oxidase as a catalyst to the conversion of glucose into gluconic acid using a membrane reactor. Enzyme and Microbial Technology, 40( 5), 1020-1025. doi:10.1016/j.enzmictec.2006.07.039
    • NLM

      Tomotani EJ, Vitolo M. Immobilized glucose oxidase as a catalyst to the conversion of glucose into gluconic acid using a membrane reactor [Internet]. Enzyme and Microbial Technology. 2007 ; 40( 5): 1020-1025.[citado 2024 out. 04 ] Available from: https://doi.org/10.1016/j.enzmictec.2006.07.039
    • Vancouver

      Tomotani EJ, Vitolo M. Immobilized glucose oxidase as a catalyst to the conversion of glucose into gluconic acid using a membrane reactor [Internet]. Enzyme and Microbial Technology. 2007 ; 40( 5): 1020-1025.[citado 2024 out. 04 ] Available from: https://doi.org/10.1016/j.enzmictec.2006.07.039
  • Source: FEBS Letters. Unidade: IQ

    Subjects: ANGIOTENSINAS, PEPTÍDEOS, ENZIMAS

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    • ABNT

      TEIXEIRA, Luis Gustavo de Deus et al. Analogues containing the paramagnetic amino acid TOAC as substrates for angiotensin I-converting enzyme. FEBS Letters, v. 581, n. 13, p. 2411-2415, 2007Tradução . . Disponível em: https://doi.org/10.1016/j.febslet.2007.04.058. Acesso em: 04 out. 2024.
    • APA

      Teixeira, L. G. de D., Bersanetti, P. A., Schreier, S., Carmona, A. K., & Nakaie, C. R. (2007). Analogues containing the paramagnetic amino acid TOAC as substrates for angiotensin I-converting enzyme. FEBS Letters, 581( 13), 2411-2415. doi:10.1016/j.febslet.2007.04.058
    • NLM

      Teixeira LG de D, Bersanetti PA, Schreier S, Carmona AK, Nakaie CR. Analogues containing the paramagnetic amino acid TOAC as substrates for angiotensin I-converting enzyme [Internet]. FEBS Letters. 2007 ; 581( 13): 2411-2415.[citado 2024 out. 04 ] Available from: https://doi.org/10.1016/j.febslet.2007.04.058
    • Vancouver

      Teixeira LG de D, Bersanetti PA, Schreier S, Carmona AK, Nakaie CR. Analogues containing the paramagnetic amino acid TOAC as substrates for angiotensin I-converting enzyme [Internet]. FEBS Letters. 2007 ; 581( 13): 2411-2415.[citado 2024 out. 04 ] Available from: https://doi.org/10.1016/j.febslet.2007.04.058
  • Source: Enzyme and Microbial Technology. Unidade: FCF

    Subjects: BIOTECNOLOGIA, ENZIMAS

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    • ABNT

      GURPILHARES, Daniela de Borba et al. Optimization of glucose-6-phosphate dehydrogenase releasing from Candida guilliermondii by disruption with glass beads. Enzyme and Microbial Technology, v. 39, n. 4, p. 591-595, 2006Tradução . . Disponível em: https://doi.org/10.1016/j.enzmictec.2005.11.018. Acesso em: 04 out. 2024.
    • APA

      Gurpilhares, D. de B., Hasmann, F. A., Pessoa Junior, A., & Roberto, I. C. (2006). Optimization of glucose-6-phosphate dehydrogenase releasing from Candida guilliermondii by disruption with glass beads. Enzyme and Microbial Technology, 39( 4), 591-595. doi:10.1016/j.enzmictec.2005.11.018
    • NLM

      Gurpilhares D de B, Hasmann FA, Pessoa Junior A, Roberto IC. Optimization of glucose-6-phosphate dehydrogenase releasing from Candida guilliermondii by disruption with glass beads [Internet]. Enzyme and Microbial Technology. 2006 ; 39( 4): 591-595.[citado 2024 out. 04 ] Available from: https://doi.org/10.1016/j.enzmictec.2005.11.018
    • Vancouver

      Gurpilhares D de B, Hasmann FA, Pessoa Junior A, Roberto IC. Optimization of glucose-6-phosphate dehydrogenase releasing from Candida guilliermondii by disruption with glass beads [Internet]. Enzyme and Microbial Technology. 2006 ; 39( 4): 591-595.[citado 2024 out. 04 ] Available from: https://doi.org/10.1016/j.enzmictec.2005.11.018
  • Source: Journal of Insect Physiology. Unidade: IQ

    Subjects: ENZIMAS, PROTEÍNAS, FEROMÔNIOS

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    • ABNT

      GENTA, Fernando Ariel et al. Potential role for gut microbiota in cell wall digestion and glucoside detoxification in Tenebrio molitor larvae. Journal of Insect Physiology, v. 52, n. 6, p. 593-601, 2006Tradução . . Disponível em: https://doi.org/10.1016/j.jinsphys.2006.02.007. Acesso em: 04 out. 2024.
    • APA

      Genta, F. A., Dillon, R. J., Terra, W. R., & Ferreira, C. (2006). Potential role for gut microbiota in cell wall digestion and glucoside detoxification in Tenebrio molitor larvae. Journal of Insect Physiology, 52( 6), 593-601. doi:10.1016/j.jinsphys.2006.02.007
    • NLM

      Genta FA, Dillon RJ, Terra WR, Ferreira C. Potential role for gut microbiota in cell wall digestion and glucoside detoxification in Tenebrio molitor larvae [Internet]. Journal of Insect Physiology. 2006 ; 52( 6): 593-601.[citado 2024 out. 04 ] Available from: https://doi.org/10.1016/j.jinsphys.2006.02.007
    • Vancouver

      Genta FA, Dillon RJ, Terra WR, Ferreira C. Potential role for gut microbiota in cell wall digestion and glucoside detoxification in Tenebrio molitor larvae [Internet]. Journal of Insect Physiology. 2006 ; 52( 6): 593-601.[citado 2024 out. 04 ] Available from: https://doi.org/10.1016/j.jinsphys.2006.02.007
  • Source: Process Biochemistry. Unidade: FCF

    Subjects: BIOTECNOLOGIA, ENZIMAS, FERMENTAÇÃO (PROCESSOS)

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    • ABNT

      GURPILHARES, Daniela de Borba e PESSOA JUNIOR, Adalberto e ROBERTO, Inês Conceição. Glucose-6-phosphate dehydrogenase and xylitol production by Candida guilliermondii FTI 20037 using statistical experimental design. Process Biochemistry, v. 41, n. 3, p. 631-637, 2006Tradução . . Disponível em: https://doi.org/10.1016/j.procbio.2005.08.008. Acesso em: 04 out. 2024.
    • APA

      Gurpilhares, D. de B., Pessoa Junior, A., & Roberto, I. C. (2006). Glucose-6-phosphate dehydrogenase and xylitol production by Candida guilliermondii FTI 20037 using statistical experimental design. Process Biochemistry, 41( 3), 631-637. doi:10.1016/j.procbio.2005.08.008
    • NLM

      Gurpilhares D de B, Pessoa Junior A, Roberto IC. Glucose-6-phosphate dehydrogenase and xylitol production by Candida guilliermondii FTI 20037 using statistical experimental design [Internet]. Process Biochemistry. 2006 ; 41( 3): 631-637.[citado 2024 out. 04 ] Available from: https://doi.org/10.1016/j.procbio.2005.08.008
    • Vancouver

      Gurpilhares D de B, Pessoa Junior A, Roberto IC. Glucose-6-phosphate dehydrogenase and xylitol production by Candida guilliermondii FTI 20037 using statistical experimental design [Internet]. Process Biochemistry. 2006 ; 41( 3): 631-637.[citado 2024 out. 04 ] Available from: https://doi.org/10.1016/j.procbio.2005.08.008
  • Source: Anais da Academia Brasileira de Ciências. Unidade: IQ

    Subjects: BIOQUÍMICA, ENZIMAS

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    • ABNT

      TERRA, Walter Ribeiro e COSTA, Rita H. e FERREIRA, Clélia. Plasma membranes from insect midgut cells. Anais da Academia Brasileira de Ciências, v. 78, n. 2, p. 255-269, 2006Tradução . . Disponível em: https://doi.org/10.1590/s0001-37652006000200007. Acesso em: 04 out. 2024.
    • APA

      Terra, W. R., Costa, R. H., & Ferreira, C. (2006). Plasma membranes from insect midgut cells. Anais da Academia Brasileira de Ciências, 78( 2), 255-269. doi:10.1590/s0001-37652006000200007
    • NLM

      Terra WR, Costa RH, Ferreira C. Plasma membranes from insect midgut cells [Internet]. Anais da Academia Brasileira de Ciências. 2006 ; 78( 2): 255-269.[citado 2024 out. 04 ] Available from: https://doi.org/10.1590/s0001-37652006000200007
    • Vancouver

      Terra WR, Costa RH, Ferreira C. Plasma membranes from insect midgut cells [Internet]. Anais da Academia Brasileira de Ciências. 2006 ; 78( 2): 255-269.[citado 2024 out. 04 ] Available from: https://doi.org/10.1590/s0001-37652006000200007

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