Filtros : "FARAH, SHAKER CHUCK" "2012" Removido: "COVID-19" Limpar

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  • Source: Journal of Biological Chemistry. Unidade: IQ

    Subjects: FIBRONECTINAS, LEPTOSPIROSE

    Acesso à fonteDOIHow to cite
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    • ABNT

      HAUK, Pricila et al. Calcium binding to Leptospira outer membrane antigen LipL32 is not necessary for its interaction with plasma fibronectin, collagen type IV, and plasminogen. Journal of Biological Chemistry, v. 287, n. 7, p. 4826-4834 : + Supplementary materials ( S1-S7), 2012Tradução . . Disponível em: https://doi.org/10.1074/jbc.M111.277210. Acesso em: 02 ago. 2024.
    • APA

      Hauk, P., Barbosa, A. S., Ho, P. L., & Farah, C. S. (2012). Calcium binding to Leptospira outer membrane antigen LipL32 is not necessary for its interaction with plasma fibronectin, collagen type IV, and plasminogen. Journal of Biological Chemistry, 287( 7), 4826-4834 : + Supplementary materials ( S1-S7). doi:10.1074/jbc.M111.277210
    • NLM

      Hauk P, Barbosa AS, Ho PL, Farah CS. Calcium binding to Leptospira outer membrane antigen LipL32 is not necessary for its interaction with plasma fibronectin, collagen type IV, and plasminogen [Internet]. Journal of Biological Chemistry. 2012 ; 287( 7): 4826-4834 : + Supplementary materials ( S1-S7).[citado 2024 ago. 02 ] Available from: https://doi.org/10.1074/jbc.M111.277210
    • Vancouver

      Hauk P, Barbosa AS, Ho PL, Farah CS. Calcium binding to Leptospira outer membrane antigen LipL32 is not necessary for its interaction with plasma fibronectin, collagen type IV, and plasminogen [Internet]. Journal of Biological Chemistry. 2012 ; 287( 7): 4826-4834 : + Supplementary materials ( S1-S7).[citado 2024 ago. 02 ] Available from: https://doi.org/10.1074/jbc.M111.277210
  • Source: Insect Biochemistry and Molecular Biology. Unidades: ICB, IB, IQ

    Subjects: PROTEINASES, BESOUROS, SISTEMA DIGESTÓRIO, FISIOLOGIA MOLECULAR

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      BETON, Daniela et al. The 3D structure and function of digestive cathepsin L-like proteinases of Tenebrio molitor larval midgut. Insect Biochemistry and Molecular Biology, v. 42, n. 9, p. 655-664, 2012Tradução . . Disponível em: https://doi.org/10.1016/j.ibmb.2012.04.010. Acesso em: 02 ago. 2024.
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      Beton, D., Carvalho, C. R. G., Ribeiro, A. de F., Farah, C. S., & Terra, W. R. (2012). The 3D structure and function of digestive cathepsin L-like proteinases of Tenebrio molitor larval midgut. Insect Biochemistry and Molecular Biology, 42( 9), 655-664. doi:10.1016/j.ibmb.2012.04.010
    • NLM

      Beton D, Carvalho CRG, Ribeiro A de F, Farah CS, Terra WR. The 3D structure and function of digestive cathepsin L-like proteinases of Tenebrio molitor larval midgut [Internet]. Insect Biochemistry and Molecular Biology. 2012 ; 42( 9): 655-664.[citado 2024 ago. 02 ] Available from: https://doi.org/10.1016/j.ibmb.2012.04.010
    • Vancouver

      Beton D, Carvalho CRG, Ribeiro A de F, Farah CS, Terra WR. The 3D structure and function of digestive cathepsin L-like proteinases of Tenebrio molitor larval midgut [Internet]. Insect Biochemistry and Molecular Biology. 2012 ; 42( 9): 655-664.[citado 2024 ago. 02 ] Available from: https://doi.org/10.1016/j.ibmb.2012.04.010
  • Source: Program and Index. Conference titles: Annual Meeting of the Brazilian Biochemistry and Molecular Biology Society (SBBq). Unidade: IQ

    Subjects: CRISTALIZAÇÃO, ENZIMAS

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      SOUZA, V. P e FARAH, Chuck Shaker e MARANA, Sandro Roberto. Crystallization of a Beta-glucosidase from Spodoptera frujiperda. 2012, Anais.. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular (SBBq), 2012. . Acesso em: 02 ago. 2024.
    • APA

      Souza, V. P., Farah, C. S., & Marana, S. R. (2012). Crystallization of a Beta-glucosidase from Spodoptera frujiperda. In Program and Index. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular (SBBq).
    • NLM

      Souza VP, Farah CS, Marana SR. Crystallization of a Beta-glucosidase from Spodoptera frujiperda. Program and Index. 2012 ;[citado 2024 ago. 02 ]
    • Vancouver

      Souza VP, Farah CS, Marana SR. Crystallization of a Beta-glucosidase from Spodoptera frujiperda. Program and Index. 2012 ;[citado 2024 ago. 02 ]
  • Source: Program and Index. Conference titles: Annual Meeting of the Brazilian Biochemistry and Molecular Biology Society (SBBq). Unidade: IQ

    Subjects: XANTHOMONAS, SOLUBILIZAÇÃO

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      MALAVASI, Natália V et al. Solubilization of the Xantomonas axonopodis gene XAC2810 protein by high hydrostatic pressure application. 2012, Anais.. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular (SBBq), 2012. . Acesso em: 02 ago. 2024.
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      Malavasi, N. V., Oliveira, M. C., Santos, F. M., Pinto, G. L., Lemke, L. S., Rodrigues, D., et al. (2012). Solubilization of the Xantomonas axonopodis gene XAC2810 protein by high hydrostatic pressure application. In Program and Index. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular (SBBq).
    • NLM

      Malavasi NV, Oliveira MC, Santos FM, Pinto GL, Lemke LS, Rodrigues D, Chura-Chambi RM, Farah CS, Morganti L. Solubilization of the Xantomonas axonopodis gene XAC2810 protein by high hydrostatic pressure application. Program and Index. 2012 ;[citado 2024 ago. 02 ]
    • Vancouver

      Malavasi NV, Oliveira MC, Santos FM, Pinto GL, Lemke LS, Rodrigues D, Chura-Chambi RM, Farah CS, Morganti L. Solubilization of the Xantomonas axonopodis gene XAC2810 protein by high hydrostatic pressure application. Program and Index. 2012 ;[citado 2024 ago. 02 ]
  • Source: Molecular Plant Pathology. Unidade: IQ

    Subjects: XANTHOMONAS, PROTEÍNAS

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      DUNGER, German et al. Analysis of three Xanthomonas axonopodis pv. citri effector proteins in pathogenicity and their interactions with host plant proteins. Molecular Plant Pathology, v. 13, n. 8, p. 865-876, 2012Tradução . . Disponível em: https://doi.org/10.1111/j.1364-3703.2012.00797.x. Acesso em: 02 ago. 2024.
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      Dunger, G., Garofalo, C. G., Gottig, N., Garavaglia, B. S., Rosa, M. C. P., Farah, C. S., et al. (2012). Analysis of three Xanthomonas axonopodis pv. citri effector proteins in pathogenicity and their interactions with host plant proteins. Molecular Plant Pathology, 13( 8), 865-876. doi:10.1111/j.1364-3703.2012.00797.x
    • NLM

      Dunger G, Garofalo CG, Gottig N, Garavaglia BS, Rosa MCP, Farah CS, Orellano EG, Ottado J. Analysis of three Xanthomonas axonopodis pv. citri effector proteins in pathogenicity and their interactions with host plant proteins [Internet]. Molecular Plant Pathology. 2012 ; 13( 8): 865-876.[citado 2024 ago. 02 ] Available from: https://doi.org/10.1111/j.1364-3703.2012.00797.x
    • Vancouver

      Dunger G, Garofalo CG, Gottig N, Garavaglia BS, Rosa MCP, Farah CS, Orellano EG, Ottado J. Analysis of three Xanthomonas axonopodis pv. citri effector proteins in pathogenicity and their interactions with host plant proteins [Internet]. Molecular Plant Pathology. 2012 ; 13( 8): 865-876.[citado 2024 ago. 02 ] Available from: https://doi.org/10.1111/j.1364-3703.2012.00797.x
  • Source: Resumos. Conference titles: International Congress on Cell Biology. Unidades: ICB, IQ

    Assunto: HISTOLOGIA

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      LORENZON, Aline R. et al. Stromal Cell Derived Factor-2 (SDF-2) at maternal-fetal interface. 2012, Anais.. Rio de Janeiro: The Brazilian Society for Cell Biology / The International Federal for Cell Biology, 2012. . Acesso em: 02 ago. 2024.
    • APA

      Lorenzon, A. R., Farah, C. S., Fisher, S. J., & Bevilacqua, E. M. A. F. (2012). Stromal Cell Derived Factor-2 (SDF-2) at maternal-fetal interface. In Resumos. Rio de Janeiro: The Brazilian Society for Cell Biology / The International Federal for Cell Biology.
    • NLM

      Lorenzon AR, Farah CS, Fisher SJ, Bevilacqua EMAF. Stromal Cell Derived Factor-2 (SDF-2) at maternal-fetal interface. Resumos. 2012 ;[citado 2024 ago. 02 ]
    • Vancouver

      Lorenzon AR, Farah CS, Fisher SJ, Bevilacqua EMAF. Stromal Cell Derived Factor-2 (SDF-2) at maternal-fetal interface. Resumos. 2012 ;[citado 2024 ago. 02 ]
  • Source: Molecular Microbiology. Unidade: IQ

    Subjects: XANTHOMONAS, PROTEÍNAS

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      RYAN, Robert P et al. Dynamic complex formation between HD-GYP, GGDEF and PilZ domain proteins regulates motility in Xanthomonas campestris. Molecular Microbiology, v. 86, n. 3, p. 557-567, 2012Tradução . . Disponível em: https://doi.org/10.1111/mmi.12000. Acesso em: 02 ago. 2024.
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      Ryan, R. P., McCarthy, Y., Kiely, P. A., O'Connor, R., Farah, C. S., Armitage, J. P., & Dow, J. M. (2012). Dynamic complex formation between HD-GYP, GGDEF and PilZ domain proteins regulates motility in Xanthomonas campestris. Molecular Microbiology, 86( 3), 557-567. doi:10.1111/mmi.12000
    • NLM

      Ryan RP, McCarthy Y, Kiely PA, O'Connor R, Farah CS, Armitage JP, Dow JM. Dynamic complex formation between HD-GYP, GGDEF and PilZ domain proteins regulates motility in Xanthomonas campestris [Internet]. Molecular Microbiology. 2012 ; 86( 3): 557-567.[citado 2024 ago. 02 ] Available from: https://doi.org/10.1111/mmi.12000
    • Vancouver

      Ryan RP, McCarthy Y, Kiely PA, O'Connor R, Farah CS, Armitage JP, Dow JM. Dynamic complex formation between HD-GYP, GGDEF and PilZ domain proteins regulates motility in Xanthomonas campestris [Internet]. Molecular Microbiology. 2012 ; 86( 3): 557-567.[citado 2024 ago. 02 ] Available from: https://doi.org/10.1111/mmi.12000

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