Filtros : "Larsen, Martin Rossel" Removido: "Stolf, Beatriz Simonsen" Limpar

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  • Fonte: Journal of Proteomics. Unidades: IQ, ICB

    Assuntos: TRYPANOSOMA CRUZI, GLICOPROTEÍNAS, ESPECTROMETRIA DE MASSAS

    Acesso à fonteDOIComo citar
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    • ABNT

      ALVES, Maria Júlia Manso et al. Comprehensive glycoprofiling of the epimastigote and trypomastigote stages of Trypanosoma cruzi. Journal of Proteomics, v. 151, p. 182-192, 2017Tradução . . Disponível em: https://doi.org/10.1016/j.jprot.2016.05.034. Acesso em: 08 nov. 2024.
    • APA

      Alves, M. J. M., Kawahara, R., Viner, R., Colli, W., Mattos, E. C., Thaysen Andersen, M., et al. (2017). Comprehensive glycoprofiling of the epimastigote and trypomastigote stages of Trypanosoma cruzi. Journal of Proteomics, 151, 182-192. doi:10.1016/j.jprot.2016.05.034
    • NLM

      Alves MJM, Kawahara R, Viner R, Colli W, Mattos EC, Thaysen Andersen M, Larsen MR, Palmisano G. Comprehensive glycoprofiling of the epimastigote and trypomastigote stages of Trypanosoma cruzi [Internet]. Journal of Proteomics. 2017 ; 151 182-192.[citado 2024 nov. 08 ] Available from: https://doi.org/10.1016/j.jprot.2016.05.034
    • Vancouver

      Alves MJM, Kawahara R, Viner R, Colli W, Mattos EC, Thaysen Andersen M, Larsen MR, Palmisano G. Comprehensive glycoprofiling of the epimastigote and trypomastigote stages of Trypanosoma cruzi [Internet]. Journal of Proteomics. 2017 ; 151 182-192.[citado 2024 nov. 08 ] Available from: https://doi.org/10.1016/j.jprot.2016.05.034
  • Fonte: BMC Genomics. Unidade: ICB

    Assuntos: PARASITOLOGIA, TRIGO, FUNGOS

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    • ABNT

      YANG, Fen et al. Unraveling incompatibility between wheat and the fungal pathogen Zymoseptoria tritici through apoplastic proteomics. BMC Genomics, v. 16, p. 1-12, 2015Tradução . . Disponível em: https://doi.org/10.1186/s12864-015-1549-6. Acesso em: 08 nov. 2024.
    • APA

      Yang, F., Li, W., Derbyshire, M., Larsen, M. R., Rudd, J. J., & Palmisano, G. (2015). Unraveling incompatibility between wheat and the fungal pathogen Zymoseptoria tritici through apoplastic proteomics. BMC Genomics, 16, 1-12. doi:10.1186/s12864-015-1549-6
    • NLM

      Yang F, Li W, Derbyshire M, Larsen MR, Rudd JJ, Palmisano G. Unraveling incompatibility between wheat and the fungal pathogen Zymoseptoria tritici through apoplastic proteomics [Internet]. BMC Genomics. 2015 ; 16 1-12.[citado 2024 nov. 08 ] Available from: https://doi.org/10.1186/s12864-015-1549-6
    • Vancouver

      Yang F, Li W, Derbyshire M, Larsen MR, Rudd JJ, Palmisano G. Unraveling incompatibility between wheat and the fungal pathogen Zymoseptoria tritici through apoplastic proteomics [Internet]. BMC Genomics. 2015 ; 16 1-12.[citado 2024 nov. 08 ] Available from: https://doi.org/10.1186/s12864-015-1549-6
  • Fonte: Journal of Proteomics. Unidade: ICB

    Assuntos: PARASITOLOGIA, PROTEINAS

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    • ABNT

      MILIOLI, Marco et al. Quantitative proteomics analysis of platelet-derived microparticles reveals distinct protein signatures when stimulated by different physiological agonists. Journal of Proteomics, v. 121, p. 56-66, 2015Tradução . . Disponível em: https://doi.org/10.1016/j.jprot.2015.03.01. Acesso em: 08 nov. 2024.
    • APA

      Milioli, M., Ibáñez-Vea, M., Sidoli, S., Palmisano, G., Careri, M., & Larsen, M. R. (2015). Quantitative proteomics analysis of platelet-derived microparticles reveals distinct protein signatures when stimulated by different physiological agonists. Journal of Proteomics, 121, 56-66. doi:10.1016/j.jprot.2015.03.01
    • NLM

      Milioli M, Ibáñez-Vea M, Sidoli S, Palmisano G, Careri M, Larsen MR. Quantitative proteomics analysis of platelet-derived microparticles reveals distinct protein signatures when stimulated by different physiological agonists [Internet]. Journal of Proteomics. 2015 ; 121 56-66.[citado 2024 nov. 08 ] Available from: https://doi.org/10.1016/j.jprot.2015.03.01
    • Vancouver

      Milioli M, Ibáñez-Vea M, Sidoli S, Palmisano G, Careri M, Larsen MR. Quantitative proteomics analysis of platelet-derived microparticles reveals distinct protein signatures when stimulated by different physiological agonists [Internet]. Journal of Proteomics. 2015 ; 121 56-66.[citado 2024 nov. 08 ] Available from: https://doi.org/10.1016/j.jprot.2015.03.01
  • Fonte: Molecular and Cellular Proteomics. Unidade: ICB

    Assunto: PARASITOLOGIA

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    • ABNT

      MELO-BRAGA, Marcella Nunes et al. Comprehensive quantitative comparison of the membrane proteome, phosphoproteome, and sialiome of human embryonic and neural stem cells. Molecular and Cellular Proteomics, v. 13, n. 1, p. 311-328, 2014Tradução . . Disponível em: https://doi.org/10.1074/mcp.M112.026898. Acesso em: 08 nov. 2024.
    • APA

      Melo-Braga, M. N., Schulz, M., Liu, Q., Swistowski, A., Palmisano, G., Engholm-Keller, K., et al. (2014). Comprehensive quantitative comparison of the membrane proteome, phosphoproteome, and sialiome of human embryonic and neural stem cells. Molecular and Cellular Proteomics, 13( 1), 311-328. doi:10.1074/mcp.M112.026898
    • NLM

      Melo-Braga MN, Schulz M, Liu Q, Swistowski A, Palmisano G, Engholm-Keller K, Jakobsen L, Zeng X, Larsen MR. Comprehensive quantitative comparison of the membrane proteome, phosphoproteome, and sialiome of human embryonic and neural stem cells [Internet]. Molecular and Cellular Proteomics. 2014 ; 13( 1): 311-328.[citado 2024 nov. 08 ] Available from: https://doi.org/10.1074/mcp.M112.026898
    • Vancouver

      Melo-Braga MN, Schulz M, Liu Q, Swistowski A, Palmisano G, Engholm-Keller K, Jakobsen L, Zeng X, Larsen MR. Comprehensive quantitative comparison of the membrane proteome, phosphoproteome, and sialiome of human embryonic and neural stem cells [Internet]. Molecular and Cellular Proteomics. 2014 ; 13( 1): 311-328.[citado 2024 nov. 08 ] Available from: https://doi.org/10.1074/mcp.M112.026898

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