Filtros : "Indexado no Biosis" "Inglaterra" Limpar

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  • Source: Clinical Nutrition. Unidades: FM, FCF

    Subjects: SUBSTITUTOS DO LEITE HUMANO, MACRÓFAGOS, GLUTAMINA, SUPLEMENTAÇÃO ALIMENTAR, HEMATOPOESE

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    • ABNT

      DIAS, Maria Carolina Gonçalves et al. Body weight changes and outcome of pregnancy after gastroplasty for morbid obesity. Clinical Nutrition, v. 28, n. 2, 2009Tradução . . Disponível em: https://doi.org/10.1016/j.clnu.2009.01.012. Acesso em: 13 ago. 2024.
    • APA

      Dias, M. C. G., Borelli, P., Vinolo, M. A. R., Fock, R. A., Pires, I. S. de O., & Tirapegui, J. (2009). Body weight changes and outcome of pregnancy after gastroplasty for morbid obesity. Clinical Nutrition, 28( 2). doi:10.1016/j.clnu.2009.01.012
    • NLM

      Dias MCG, Borelli P, Vinolo MAR, Fock RA, Pires IS de O, Tirapegui J. Body weight changes and outcome of pregnancy after gastroplasty for morbid obesity [Internet]. Clinical Nutrition. 2009 ; 28( 2):[citado 2024 ago. 13 ] Available from: https://doi.org/10.1016/j.clnu.2009.01.012
    • Vancouver

      Dias MCG, Borelli P, Vinolo MAR, Fock RA, Pires IS de O, Tirapegui J. Body weight changes and outcome of pregnancy after gastroplasty for morbid obesity [Internet]. Clinical Nutrition. 2009 ; 28( 2):[citado 2024 ago. 13 ] Available from: https://doi.org/10.1016/j.clnu.2009.01.012
  • Source: FEBS Journal. Unidade: IQ

    Subjects: TRYPANOSOMA CRUZI, GLÂNDULAS SALIVARES, BIOQUÍMICA

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      MARTINS, Rafael Miyazawa et al. A short proregion of trialysin, a pore-forming protein of Triatoma infestans salivary glands, controls activity by folding the N-terminal lytic motif. FEBS Journal, v. 275, n. 5, p. 994-1002, 2008Tradução . . Disponível em: https://doi.org/10.1111/j.1742-4658.2008.06260.x. Acesso em: 13 ago. 2024.
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      Martins, R. M., Amino, R., Daghastanli, K. R. P., Cuccovia, I. M., Juliano, M. A., & Schenkman, S. (2008). A short proregion of trialysin, a pore-forming protein of Triatoma infestans salivary glands, controls activity by folding the N-terminal lytic motif. FEBS Journal, 275( 5), 994-1002. doi:10.1111/j.1742-4658.2008.06260.x
    • NLM

      Martins RM, Amino R, Daghastanli KRP, Cuccovia IM, Juliano MA, Schenkman S. A short proregion of trialysin, a pore-forming protein of Triatoma infestans salivary glands, controls activity by folding the N-terminal lytic motif [Internet]. FEBS Journal. 2008 ;275( 5): 994-1002.[citado 2024 ago. 13 ] Available from: https://doi.org/10.1111/j.1742-4658.2008.06260.x
    • Vancouver

      Martins RM, Amino R, Daghastanli KRP, Cuccovia IM, Juliano MA, Schenkman S. A short proregion of trialysin, a pore-forming protein of Triatoma infestans salivary glands, controls activity by folding the N-terminal lytic motif [Internet]. FEBS Journal. 2008 ;275( 5): 994-1002.[citado 2024 ago. 13 ] Available from: https://doi.org/10.1111/j.1742-4658.2008.06260.x
  • Source: FEBS Journal. Unidade: IQ

    Subjects: CATÁLISE, ENZIMAS, BIOQUÍMICA

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      MENDONÇA, Lúcio Mário Ferreira de e MARANA, Sandro Roberto. The role in the substrate specificity and catalysis of residues forming the substrate aglycone-binding site of a 'beta'-glycosidase. FEBS Journal, v. 275, n. 10, p. 2536-2547, 2008Tradução . . Disponível em: https://doi.org/10.1111/j.1742-4658.2008.06402.x. Acesso em: 13 ago. 2024.
    • APA

      Mendonça, L. M. F. de, & Marana, S. R. (2008). The role in the substrate specificity and catalysis of residues forming the substrate aglycone-binding site of a 'beta'-glycosidase. FEBS Journal, 275( 10), 2536-2547. doi:10.1111/j.1742-4658.2008.06402.x
    • NLM

      Mendonça LMF de, Marana SR. The role in the substrate specificity and catalysis of residues forming the substrate aglycone-binding site of a 'beta'-glycosidase [Internet]. FEBS Journal. 2008 ;275( 10): 2536-2547.[citado 2024 ago. 13 ] Available from: https://doi.org/10.1111/j.1742-4658.2008.06402.x
    • Vancouver

      Mendonça LMF de, Marana SR. The role in the substrate specificity and catalysis of residues forming the substrate aglycone-binding site of a 'beta'-glycosidase [Internet]. FEBS Journal. 2008 ;275( 10): 2536-2547.[citado 2024 ago. 13 ] Available from: https://doi.org/10.1111/j.1742-4658.2008.06402.x
  • Source: Journal of Nanobiotechnology. Unidade: IQ

    Subjects: NANOPARTÍCULAS, NANOTECNOLOGIA, CANDIDA ALBICANS

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      VIEIRA, Débora Braga e CARMONA-RIBEIRO, Ana Maria. Cationic nanoparticles for delivery of amphotericin B: preparation, characterization and activity in vitro. Journal of Nanobiotechnology, v. 6, n. 6, p. online, 2008Tradução . . Disponível em: https://doi.org/10.1186/1477-3155-6-6. Acesso em: 13 ago. 2024.
    • APA

      Vieira, D. B., & Carmona-Ribeiro, A. M. (2008). Cationic nanoparticles for delivery of amphotericin B: preparation, characterization and activity in vitro. Journal of Nanobiotechnology, 6( 6), online. doi:10.1186/1477-3155-6-6
    • NLM

      Vieira DB, Carmona-Ribeiro AM. Cationic nanoparticles for delivery of amphotericin B: preparation, characterization and activity in vitro [Internet]. Journal of Nanobiotechnology. 2008 ; 6( 6): online.[citado 2024 ago. 13 ] Available from: https://doi.org/10.1186/1477-3155-6-6
    • Vancouver

      Vieira DB, Carmona-Ribeiro AM. Cationic nanoparticles for delivery of amphotericin B: preparation, characterization and activity in vitro [Internet]. Journal of Nanobiotechnology. 2008 ; 6( 6): online.[citado 2024 ago. 13 ] Available from: https://doi.org/10.1186/1477-3155-6-6
  • Source: Microbial Cell Factories. Unidade: IQ

    Subjects: SACCHAROMYCES, BIOQUÍMICA

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      BADOTTI, Fernanda et al. Switching the mode of sucrose utilization by Saccharomyces cerevisiae. Microbial Cell Factories, v. 7, n. 4, p. 1-11, 2008Tradução . . Disponível em: https://doi.org/10.1186/1475-2859-7-4. Acesso em: 13 ago. 2024.
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      Badotti, F., Dário, M. G., Alves Jr., S. L., Cordioli, M. L. A., Miletti, L. C., De Araujo, P. S., & Stambuk, B. J. C. U. (2008). Switching the mode of sucrose utilization by Saccharomyces cerevisiae. Microbial Cell Factories, 7( 4), 1-11. doi:10.1186/1475-2859-7-4
    • NLM

      Badotti F, Dário MG, Alves Jr. SL, Cordioli MLA, Miletti LC, De Araujo PS, Stambuk BJCU. Switching the mode of sucrose utilization by Saccharomyces cerevisiae [Internet]. Microbial Cell Factories. 2008 ; 7( 4): 1-11.[citado 2024 ago. 13 ] Available from: https://doi.org/10.1186/1475-2859-7-4
    • Vancouver

      Badotti F, Dário MG, Alves Jr. SL, Cordioli MLA, Miletti LC, De Araujo PS, Stambuk BJCU. Switching the mode of sucrose utilization by Saccharomyces cerevisiae [Internet]. Microbial Cell Factories. 2008 ; 7( 4): 1-11.[citado 2024 ago. 13 ] Available from: https://doi.org/10.1186/1475-2859-7-4
  • Source: FEBS Journal. Unidade: IQ

    Subjects: BIOQUÍMICA, ENZIMAS

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      CRISTOFOLETTI, Plinio Tadeu et al. Characterization of a membrane-bound aminopeptidase purified from Acyrthosiphon pisum midgut cells. FEBS Journal, v. 273, n. 24, p. 5574-5588, 2006Tradução . . Disponível em: https://doi.org/10.1111/j.1742-4658.2006.05547.x. Acesso em: 13 ago. 2024.
    • APA

      Cristofoletti, P. T., Sousa, F. A. M. de, Rahbé, Y., & Terra, W. R. (2006). Characterization of a membrane-bound aminopeptidase purified from Acyrthosiphon pisum midgut cells. FEBS Journal, 273( 24), 5574-5588. doi:10.1111/j.1742-4658.2006.05547.x
    • NLM

      Cristofoletti PT, Sousa FAM de, Rahbé Y, Terra WR. Characterization of a membrane-bound aminopeptidase purified from Acyrthosiphon pisum midgut cells [Internet]. FEBS Journal. 2006 ; 273( 24): 5574-5588.[citado 2024 ago. 13 ] Available from: https://doi.org/10.1111/j.1742-4658.2006.05547.x
    • Vancouver

      Cristofoletti PT, Sousa FAM de, Rahbé Y, Terra WR. Characterization of a membrane-bound aminopeptidase purified from Acyrthosiphon pisum midgut cells [Internet]. FEBS Journal. 2006 ; 273( 24): 5574-5588.[citado 2024 ago. 13 ] Available from: https://doi.org/10.1111/j.1742-4658.2006.05547.x
  • Source: European Journal of Biochemistry. Unidade: IQ

    Subjects: BIOQUÍMICA, POLIMERIZAÇÃO, PROTEÍNAS MUSCULARES

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      PAULUCCI, Adriana Aparecida et al. A specific C-terminal deletion in tropomyosin results in a stronger head-to-tail interaction and increased polymerization. European Journal of Biochemistry, v. 271, n. 3, p. 589-600, 2004Tradução . . Disponível em: https://doi.org/10.1111/j.1432-1033.2003.03961.x. Acesso em: 13 ago. 2024.
    • APA

      Paulucci, A. A., Katsuyama, Â. M., Sousa, A. D. de, & Farah, C. S. (2004). A specific C-terminal deletion in tropomyosin results in a stronger head-to-tail interaction and increased polymerization. European Journal of Biochemistry, 271( 3), 589-600. doi:10.1111/j.1432-1033.2003.03961.x
    • NLM

      Paulucci AA, Katsuyama ÂM, Sousa AD de, Farah CS. A specific C-terminal deletion in tropomyosin results in a stronger head-to-tail interaction and increased polymerization [Internet]. European Journal of Biochemistry. 2004 ; 271( 3): 589-600.[citado 2024 ago. 13 ] Available from: https://doi.org/10.1111/j.1432-1033.2003.03961.x
    • Vancouver

      Paulucci AA, Katsuyama ÂM, Sousa AD de, Farah CS. A specific C-terminal deletion in tropomyosin results in a stronger head-to-tail interaction and increased polymerization [Internet]. European Journal of Biochemistry. 2004 ; 271( 3): 589-600.[citado 2024 ago. 13 ] Available from: https://doi.org/10.1111/j.1432-1033.2003.03961.x

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