Filtros : "ICB" "Indexado na Base de Dados MEDLINE" "Palmisano, Giuseppe" Removidos: "Nunes, Maria Tereza" "Teixeira, S. A." "Saraceni Júnior, Guilherme" Limpar

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

    Subjects: TRYPANOSOMA CRUZI, GLICOPROTEÍNAS, ESPECTROMETRIA DE MASSAS

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      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: 22 maio 2024.
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      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 maio 22 ] 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 maio 22 ] Available from: https://doi.org/10.1016/j.jprot.2016.05.034
  • Source: Comparative Biochemistry and Physiology B. Unidades: ICB, IQ

    Subjects: HEMIPTERA, DIGESTÃO ANIMAL, ENZIMAS

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      PIMENTEL, André Coppe et al. Role of cathepsins D in the midgut of Dysdercus peruvianus. Comparative Biochemistry and Physiology B, v. 204, p. 45-52, 2017Tradução . . Disponível em: https://doi.org/10.1016/j.cbpb.2016.11.004. Acesso em: 22 maio 2024.
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      Pimentel, A. C., Fuzita, F. J., Palmisano, G., Ferreira, C., & Terra, W. R. (2017). Role of cathepsins D in the midgut of Dysdercus peruvianus. Comparative Biochemistry and Physiology B, 204, 45-52. doi:10.1016/j.cbpb.2016.11.004
    • NLM

      Pimentel AC, Fuzita FJ, Palmisano G, Ferreira C, Terra WR. Role of cathepsins D in the midgut of Dysdercus peruvianus [Internet]. Comparative Biochemistry and Physiology B. 2017 ; 204 45-52.[citado 2024 maio 22 ] Available from: https://doi.org/10.1016/j.cbpb.2016.11.004
    • Vancouver

      Pimentel AC, Fuzita FJ, Palmisano G, Ferreira C, Terra WR. Role of cathepsins D in the midgut of Dysdercus peruvianus [Internet]. Comparative Biochemistry and Physiology B. 2017 ; 204 45-52.[citado 2024 maio 22 ] Available from: https://doi.org/10.1016/j.cbpb.2016.11.004
  • Source: Scientific Reports. Unidade: ICB

    Subjects: PARASITOLOGIA, PROTEÍNAS, ESCHERICHIA COLI, GLICOPROTEÍNAS, ESPECTROMETRIA DE MASSAS

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      BOYSEN, Anders et al. A novel mass spectrometric strategy “BEMAP” reveals Extensive O-linked protein glycosylation in Enterotoxigenic Escherichia coli. Scientific Reports, v. 6, p. 1-13, 2016Tradução . . Disponível em: https://doi.org/10.1038/srep32016. Acesso em: 22 maio 2024.
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      Boysen, A., Palmisano, G., Krogh, T. J., Duggin, I. G., Larsen, M. R., & Møller-Jensen, J. (2016). A novel mass spectrometric strategy “BEMAP” reveals Extensive O-linked protein glycosylation in Enterotoxigenic Escherichia coli. Scientific Reports, 6, 1-13. doi:10.1038/srep32016
    • NLM

      Boysen A, Palmisano G, Krogh TJ, Duggin IG, Larsen MR, Møller-Jensen J. A novel mass spectrometric strategy “BEMAP” reveals Extensive O-linked protein glycosylation in Enterotoxigenic Escherichia coli [Internet]. Scientific Reports. 2016 ; 6 1-13.[citado 2024 maio 22 ] Available from: https://doi.org/10.1038/srep32016
    • Vancouver

      Boysen A, Palmisano G, Krogh TJ, Duggin IG, Larsen MR, Møller-Jensen J. A novel mass spectrometric strategy “BEMAP” reveals Extensive O-linked protein glycosylation in Enterotoxigenic Escherichia coli [Internet]. Scientific Reports. 2016 ; 6 1-13.[citado 2024 maio 22 ] Available from: https://doi.org/10.1038/srep32016
  • Source: Molecular and Cellular Proteomics. Unidade: ICB

    Subjects: PARASITOLOGIA, PEPTÍDEOS, CROMATOGRAFIA, ESPECTROMETRIA DE MASSAS

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      HUANG, Honggang et al. Simultaneous enrichment of cysteine-containing peptides and phosphopeptides using a cysteine-specific phosphonate adaptable Tag (CysPAT) in combination with titanium dioxide (TiO2) chromatography. Molecular and Cellular Proteomics, v. 15, n. 10, p. 3282-3296, 2016Tradução . . Disponível em: https://doi.org/10.1074/mcp.M115.054551. Acesso em: 22 maio 2024.
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      Huang, H., Petersen, M. H., Ibañez-Vea, M., Lassen, P. S., & Palmisano, G. (2016). Simultaneous enrichment of cysteine-containing peptides and phosphopeptides using a cysteine-specific phosphonate adaptable Tag (CysPAT) in combination with titanium dioxide (TiO2) chromatography. Molecular and Cellular Proteomics, 15( 10), 3282-3296. doi:10.1074/mcp.M115.054551
    • NLM

      Huang H, Petersen MH, Ibañez-Vea M, Lassen PS, Palmisano G. Simultaneous enrichment of cysteine-containing peptides and phosphopeptides using a cysteine-specific phosphonate adaptable Tag (CysPAT) in combination with titanium dioxide (TiO2) chromatography [Internet]. Molecular and Cellular Proteomics. 2016 ; 15( 10): 3282-3296.[citado 2024 maio 22 ] Available from: https://doi.org/10.1074/mcp.M115.054551
    • Vancouver

      Huang H, Petersen MH, Ibañez-Vea M, Lassen PS, Palmisano G. Simultaneous enrichment of cysteine-containing peptides and phosphopeptides using a cysteine-specific phosphonate adaptable Tag (CysPAT) in combination with titanium dioxide (TiO2) chromatography [Internet]. Molecular and Cellular Proteomics. 2016 ; 15( 10): 3282-3296.[citado 2024 maio 22 ] Available from: https://doi.org/10.1074/mcp.M115.054551
  • Source: BMC Genomics. Unidade: ICB

    Subjects: PARASITOLOGIA, TRIGO, FUNGOS

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      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: 22 maio 2024.
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      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
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      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 maio 22 ] Available from: https://doi.org/10.1186/s12864-015-1549-6
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      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 maio 22 ] Available from: https://doi.org/10.1186/s12864-015-1549-6
  • Source: Journal of Proteomics. Unidade: ICB

    Subjects: PARASITOLOGIA, PROTEINAS

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      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: 22 maio 2024.
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      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
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      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 maio 22 ] Available from: https://doi.org/10.1016/j.jprot.2015.03.01
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      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 maio 22 ] Available from: https://doi.org/10.1016/j.jprot.2015.03.01
  • Source: Scientifc Reports. Unidade: ICB

    Assunto: PARASITOLOGIA

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      GABRIEL, Heloisa B. et al. Single-target high-throughput transcription analyses reveal high levels of alternative splicing present in the FPPS/GGPPS from Plasmodium falciparum. Scientifc Reports, v. 5, n. 184429, p. 1-13, 2015Tradução . . Disponível em: https://doi.org/10.1038/srep18429. Acesso em: 22 maio 2024.
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      Gabriel, H. B., Azevedo, M. F. de, Palmisano, G., Wunderlich, G., Kimura, E. A., Katzin, A. M., & Alves, J. M. P. (2015). Single-target high-throughput transcription analyses reveal high levels of alternative splicing present in the FPPS/GGPPS from Plasmodium falciparum. Scientifc Reports, 5( 184429), 1-13. doi:10.1038/srep18429
    • NLM

      Gabriel HB, Azevedo MF de, Palmisano G, Wunderlich G, Kimura EA, Katzin AM, Alves JMP. Single-target high-throughput transcription analyses reveal high levels of alternative splicing present in the FPPS/GGPPS from Plasmodium falciparum [Internet]. Scientifc Reports. 2015 ; 5( 184429): 1-13.[citado 2024 maio 22 ] Available from: https://doi.org/10.1038/srep18429
    • Vancouver

      Gabriel HB, Azevedo MF de, Palmisano G, Wunderlich G, Kimura EA, Katzin AM, Alves JMP. Single-target high-throughput transcription analyses reveal high levels of alternative splicing present in the FPPS/GGPPS from Plasmodium falciparum [Internet]. Scientifc Reports. 2015 ; 5( 184429): 1-13.[citado 2024 maio 22 ] Available from: https://doi.org/10.1038/srep18429
  • Source: Molecular and Cellular Proteomics. Unidade: ICB

    Assunto: PARASITOLOGIA

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      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: 22 maio 2024.
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      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
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      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 maio 22 ] Available from: https://doi.org/10.1074/mcp.M112.026898
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      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 maio 22 ] Available from: https://doi.org/10.1074/mcp.M112.026898
  • Source: Journal of Proteomics. Unidade: ICB

    Subjects: PARASITOLOGIA, PROTEINAS

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      HUANG, Honggang et al. Quantitative phosphoproteomic analysis of porcine muscle within 24 h postmortem. Journal of Proteomics, v. 106, p. 125-139, 2014Tradução . . Disponível em: https://doi.org/10.1016/j.jprot.2014.04.020. Acesso em: 22 maio 2024.
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      Huang, H., Larsen, M. R., Palmisano, G., Sai, J., & Lametsch, R. (2014). Quantitative phosphoproteomic analysis of porcine muscle within 24 h postmortem. Journal of Proteomics, 106, 125-139. doi:10.1016/j.jprot.2014.04.020
    • NLM

      Huang H, Larsen MR, Palmisano G, Sai J, Lametsch R. Quantitative phosphoproteomic analysis of porcine muscle within 24 h postmortem [Internet]. Journal of Proteomics. 2014 ; 106 125-139.[citado 2024 maio 22 ] Available from: https://doi.org/10.1016/j.jprot.2014.04.020
    • Vancouver

      Huang H, Larsen MR, Palmisano G, Sai J, Lametsch R. Quantitative phosphoproteomic analysis of porcine muscle within 24 h postmortem [Internet]. Journal of Proteomics. 2014 ; 106 125-139.[citado 2024 maio 22 ] Available from: https://doi.org/10.1016/j.jprot.2014.04.020

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