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  • Source: Protein Science. Unidades: IFSC, FFCLRP

    Subjects: PROTEÍNAS, ESPECTROSCOPIA, TRANSPORTE BIOLÓGICO, BIOFÍSICA

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      MENDES, Luis Felipe Santos et al. The potential role of liquid-liquid phase separation in the cellular fate of the compartments for unconventional protein secretion. Protein Science, v. 33, n. 7, p. e5085-1-e5085-16 + supporting information, 2024Tradução . . Disponível em: https://doi.org/10.1002/pro.5085. Acesso em: 10 ago. 2024.
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      Mendes, L. F. S., Oliveira, C. G., Silva, M. D. de O. da, Rout, S. K., Riek, R., & Costa Filho, A. J. da. (2024). The potential role of liquid-liquid phase separation in the cellular fate of the compartments for unconventional protein secretion. Protein Science, 33( 7), e5085-1-e5085-16 + supporting information. doi:10.1002/pro.5085
    • NLM

      Mendes LFS, Oliveira CG, Silva MD de O da, Rout SK, Riek R, Costa Filho AJ da. The potential role of liquid-liquid phase separation in the cellular fate of the compartments for unconventional protein secretion [Internet]. Protein Science. 2024 ; 33( 7): e5085-1-e5085-16 + supporting information.[citado 2024 ago. 10 ] Available from: https://doi.org/10.1002/pro.5085
    • Vancouver

      Mendes LFS, Oliveira CG, Silva MD de O da, Rout SK, Riek R, Costa Filho AJ da. The potential role of liquid-liquid phase separation in the cellular fate of the compartments for unconventional protein secretion [Internet]. Protein Science. 2024 ; 33( 7): e5085-1-e5085-16 + supporting information.[citado 2024 ago. 10 ] Available from: https://doi.org/10.1002/pro.5085
  • Source: Glycobiology. Conference titles: Annual Meeting of the Society for Glycobiology. Unidade: IFSC

    Subjects: GLICOPROTEÍNAS, IMUNIDADE

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      SASTRE, Diego e NAVARRO, Marcos Vicente de Albuquerque Salles e SUNDBERG, Eric J. Structural and molecular analysis of endoglycosidases and SusD-like proteins reveal a possible cooperation for the import of N-glycans in the gut microbiome. Glycobiology. Cary: Instituto de Física de São Carlos, Universidade de São Paulo. Disponível em: https://doi.org/10.1093/glycob/cwab121. Acesso em: 10 ago. 2024. , 2021
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      Sastre, D., Navarro, M. V. de A. S., & Sundberg, E. J. (2021). Structural and molecular analysis of endoglycosidases and SusD-like proteins reveal a possible cooperation for the import of N-glycans in the gut microbiome. Glycobiology. Cary: Instituto de Física de São Carlos, Universidade de São Paulo. doi:10.1093/glycob/cwab121
    • NLM

      Sastre D, Navarro MV de AS, Sundberg EJ. Structural and molecular analysis of endoglycosidases and SusD-like proteins reveal a possible cooperation for the import of N-glycans in the gut microbiome [Internet]. Glycobiology. 2021 ; 31( 12): 1677-1678.[citado 2024 ago. 10 ] Available from: https://doi.org/10.1093/glycob/cwab121
    • Vancouver

      Sastre D, Navarro MV de AS, Sundberg EJ. Structural and molecular analysis of endoglycosidases and SusD-like proteins reveal a possible cooperation for the import of N-glycans in the gut microbiome [Internet]. Glycobiology. 2021 ; 31( 12): 1677-1678.[citado 2024 ago. 10 ] Available from: https://doi.org/10.1093/glycob/cwab121
  • Source: Journal of Proteome Research. Unidade: IFSC

    Subjects: SCHISTOSOMA MANSONI, ESQUISTOSSOMOSE (TRATAMENTO;ESTUDO), PROTEÔMICA

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      NEVES, Leandro X. et al. Quantitative proteomics of enriched esophageal and gut tissues from the human blood fluke Schistosoma mansoni pinpoints secreted proteins for vaccine development. Journal of Proteome Research, v. 19, n. Ja 2020, p. 314-326, 2020Tradução . . Disponível em: https://doi.org/10.1021/acs.jproteome.9b00531. Acesso em: 10 ago. 2024.
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      Neves, L. X., Wilson, R. A., Brownridge, P., Harman, V. M., Holman, S. W., Beynon, R. J., et al. (2020). Quantitative proteomics of enriched esophageal and gut tissues from the human blood fluke Schistosoma mansoni pinpoints secreted proteins for vaccine development. Journal of Proteome Research, 19( Ja 2020), 314-326. doi:10.1021/acs.jproteome.9b00531
    • NLM

      Neves LX, Wilson RA, Brownridge P, Harman VM, Holman SW, Beynon RJ, Eyers CE, De Marco R, Castro-Borges W. Quantitative proteomics of enriched esophageal and gut tissues from the human blood fluke Schistosoma mansoni pinpoints secreted proteins for vaccine development [Internet]. Journal of Proteome Research. 2020 ; 19( Ja 2020): 314-326.[citado 2024 ago. 10 ] Available from: https://doi.org/10.1021/acs.jproteome.9b00531
    • Vancouver

      Neves LX, Wilson RA, Brownridge P, Harman VM, Holman SW, Beynon RJ, Eyers CE, De Marco R, Castro-Borges W. Quantitative proteomics of enriched esophageal and gut tissues from the human blood fluke Schistosoma mansoni pinpoints secreted proteins for vaccine development [Internet]. Journal of Proteome Research. 2020 ; 19( Ja 2020): 314-326.[citado 2024 ago. 10 ] Available from: https://doi.org/10.1021/acs.jproteome.9b00531
  • Source: Schistosoma mansoni: methods and protocols. Unidade: IFSC

    Subjects: SCHISTOSOMA MANSONI, GENOMAS, BIOINFORMÁTICA

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      PHILIPPSEN, Gisele S. e DE MARCO, Ricardo. Identification of transposable elements in Schistosoma mansoni. Schistosoma mansoni: methods and protocols. Tradução . New York: Springer Nature, 2020. p. 276 . Disponível em: https://doi.org/10.1007/978-1-0716-0635-3_11. Acesso em: 10 ago. 2024.
    • APA

      Philippsen, G. S., & De Marco, R. (2020). Identification of transposable elements in Schistosoma mansoni. In Schistosoma mansoni: methods and protocols (p. 276 ). New York: Springer Nature. doi:10.1007/978-1-0716-0635-3_11
    • NLM

      Philippsen GS, De Marco R. Identification of transposable elements in Schistosoma mansoni [Internet]. In: Schistosoma mansoni: methods and protocols. New York: Springer Nature; 2020. p. 276 .[citado 2024 ago. 10 ] Available from: https://doi.org/10.1007/978-1-0716-0635-3_11
    • Vancouver

      Philippsen GS, De Marco R. Identification of transposable elements in Schistosoma mansoni [Internet]. In: Schistosoma mansoni: methods and protocols. New York: Springer Nature; 2020. p. 276 .[citado 2024 ago. 10 ] Available from: https://doi.org/10.1007/978-1-0716-0635-3_11
  • Source: PLOS ONE. Unidades: IFSC, IQSC

    Subjects: SCHISTOSOMA MANSONI, ENZIMAS, CRISTALOGRAFIA

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      TORINI, Juliana Roberta et al. The molecular structure of Schistosoma mansoni PNP isoform 2 provides insights into the nucleoside selectivity of PNPs. PLOS ONE, v. 13, n. 9, p. e0203532-1- e0203532-21, 2018Tradução . . Disponível em: https://doi.org/10.1371/journal.pone.0203532. Acesso em: 10 ago. 2024.
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      Torini, J. R., Romanello, L., Batista, F. A. H., Serrão, V. H. B., Faheem, M., Zeraik, A. E., et al. (2018). The molecular structure of Schistosoma mansoni PNP isoform 2 provides insights into the nucleoside selectivity of PNPs. PLOS ONE, 13( 9), e0203532-1- e0203532-21. doi:10.1371/journal.pone.0203532
    • NLM

      Torini JR, Romanello L, Batista FAH, Serrão VHB, Faheem M, Zeraik AE, Bird L, Nettleship J, Reddivari Y, Owens R, De Marco R, Borges JC, Brandão-Neto J, Pereira H d'M. The molecular structure of Schistosoma mansoni PNP isoform 2 provides insights into the nucleoside selectivity of PNPs [Internet]. PLOS ONE. 2018 ; 13( 9): e0203532-1- e0203532-21.[citado 2024 ago. 10 ] Available from: https://doi.org/10.1371/journal.pone.0203532
    • Vancouver

      Torini JR, Romanello L, Batista FAH, Serrão VHB, Faheem M, Zeraik AE, Bird L, Nettleship J, Reddivari Y, Owens R, De Marco R, Borges JC, Brandão-Neto J, Pereira H d'M. The molecular structure of Schistosoma mansoni PNP isoform 2 provides insights into the nucleoside selectivity of PNPs [Internet]. PLOS ONE. 2018 ; 13( 9): e0203532-1- e0203532-21.[citado 2024 ago. 10 ] Available from: https://doi.org/10.1371/journal.pone.0203532
  • Source: PLOS Neglected Tropical Diseases. Unidade: IFSC

    Subjects: EXPRESSÃO GÊNICA, ESQUISTOSSOMOSE (TRATAMENTO;ESTUDO), SANGUE, ESÔFAGO

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      LI, Xiao-Hong et al. Microexon gene transcriptional profiles and evolution provide insights into blood processing by the Schistosoma japonicum esophagus. PLOS Neglected Tropical Diseases, v. 12, n. 2, p. e0006235-1-e0006235-22, 2018Tradução . . Disponível em: https://doi.org/10.1371/journal.pntd.0006235. Acesso em: 10 ago. 2024.
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      Li, X. -H., De Marco, R., Neves, L. X., James, S. R., Newling, K., Ashton, P. D., et al. (2018). Microexon gene transcriptional profiles and evolution provide insights into blood processing by the Schistosoma japonicum esophagus. PLOS Neglected Tropical Diseases, 12( 2), e0006235-1-e0006235-22. doi:10.1371/journal.pntd.0006235
    • NLM

      Li X-H, De Marco R, Neves LX, James SR, Newling K, Ashton PD, Cao J-P, Wilson RA, Castro Borges W. Microexon gene transcriptional profiles and evolution provide insights into blood processing by the Schistosoma japonicum esophagus [Internet]. PLOS Neglected Tropical Diseases. 2018 ; 12( 2): e0006235-1-e0006235-22.[citado 2024 ago. 10 ] Available from: https://doi.org/10.1371/journal.pntd.0006235
    • Vancouver

      Li X-H, De Marco R, Neves LX, James SR, Newling K, Ashton PD, Cao J-P, Wilson RA, Castro Borges W. Microexon gene transcriptional profiles and evolution provide insights into blood processing by the Schistosoma japonicum esophagus [Internet]. PLOS Neglected Tropical Diseases. 2018 ; 12( 2): e0006235-1-e0006235-22.[citado 2024 ago. 10 ] Available from: https://doi.org/10.1371/journal.pntd.0006235
  • Source: Biophysical Journal. Conference titles: Annual Meeting of the Biophysical Society. Unidade: IFSC

    Subjects: SCHISTOSOMA MANSONI, ESQUISTOSSOMOSE, PLANEJAMENTO DE FÁRMACOS

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      ZERAIK, Ana Eliza et al. Characterization of the Calcium Release-Activated Calcium (CRAC) channel from the human pathogen Schistosoma mansoni. Biophysical Journal. Saint Louis: Cell Press. Disponível em: https://doi.org/10.1016/j.bpj.2017.11.1640. Acesso em: 10 ago. 2024. , 2018
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      Zeraik, A. E., Gudlur, A., De Marco, R., Araújo, A. P. U. de, & Hogan, P. (2018). Characterization of the Calcium Release-Activated Calcium (CRAC) channel from the human pathogen Schistosoma mansoni. Biophysical Journal. Saint Louis: Cell Press. doi:10.1016/j.bpj.2017.11.1640
    • NLM

      Zeraik AE, Gudlur A, De Marco R, Araújo APU de, Hogan P. Characterization of the Calcium Release-Activated Calcium (CRAC) channel from the human pathogen Schistosoma mansoni [Internet]. Biophysical Journal. 2018 ; 114( 3): 286a.[citado 2024 ago. 10 ] Available from: https://doi.org/10.1016/j.bpj.2017.11.1640
    • Vancouver

      Zeraik AE, Gudlur A, De Marco R, Araújo APU de, Hogan P. Characterization of the Calcium Release-Activated Calcium (CRAC) channel from the human pathogen Schistosoma mansoni [Internet]. Biophysical Journal. 2018 ; 114( 3): 286a.[citado 2024 ago. 10 ] Available from: https://doi.org/10.1016/j.bpj.2017.11.1640
  • Source: Protein Science. Unidade: IFSC

    Subjects: RADIAÇÃO SINCROTRON, PROTEÍNAS

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      YONEDA, Juliana Sakamoto et al. Differential dehydration effects on globular proteins and intrinsically disordered proteins during film formation. Protein Science, v. 26, n. 4, p. 718-726, 2017Tradução . . Disponível em: https://doi.org/10.1002/pro.3118. Acesso em: 10 ago. 2024.
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      Yoneda, J. S., Miles, A. J., Araújo, A. P. U. de, & Wallace, B. A. (2017). Differential dehydration effects on globular proteins and intrinsically disordered proteins during film formation. Protein Science, 26( 4), 718-726. doi:10.1002/pro.3118
    • NLM

      Yoneda JS, Miles AJ, Araújo APU de, Wallace BA. Differential dehydration effects on globular proteins and intrinsically disordered proteins during film formation [Internet]. Protein Science. 2017 ; 26( 4): 718-726.[citado 2024 ago. 10 ] Available from: https://doi.org/10.1002/pro.3118
    • Vancouver

      Yoneda JS, Miles AJ, Araújo APU de, Wallace BA. Differential dehydration effects on globular proteins and intrinsically disordered proteins during film formation [Internet]. Protein Science. 2017 ; 26( 4): 718-726.[citado 2024 ago. 10 ] Available from: https://doi.org/10.1002/pro.3118
  • Source: Journal of Physical Chemistry B. Unidades: IFSC, FFCLRP

    Subjects: MEMBRANA PLASMÁTICA, LIPÍDEOS DA MEMBRANA, ENZIMAS, PREVENÇÃO DE DOENÇAS

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      VICENTE, Eduardo F. et al. HsDHODH microdomain-membrane interactions influenced by the lipid composition. Journal of Physical Chemistry B, v. 121, n. 49, p. 11085-11095, 2017Tradução . . Disponível em: https://doi.org/10.1021/acs.jpcb.7b09642. Acesso em: 10 ago. 2024.
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      Vicente, E. F., Sahu, I. D., Crusca Junior, E., Basso, L. G. M., Munte, C. E., Costa Filho, A. J. da, et al. (2017). HsDHODH microdomain-membrane interactions influenced by the lipid composition. Journal of Physical Chemistry B, 121( 49), 11085-11095. doi:10.1021/acs.jpcb.7b09642
    • NLM

      Vicente EF, Sahu ID, Crusca Junior E, Basso LGM, Munte CE, Costa Filho AJ da, Lorigan GA, Cilli EM. HsDHODH microdomain-membrane interactions influenced by the lipid composition [Internet]. Journal of Physical Chemistry B. 2017 ; 121( 49): 11085-11095.[citado 2024 ago. 10 ] Available from: https://doi.org/10.1021/acs.jpcb.7b09642
    • Vancouver

      Vicente EF, Sahu ID, Crusca Junior E, Basso LGM, Munte CE, Costa Filho AJ da, Lorigan GA, Cilli EM. HsDHODH microdomain-membrane interactions influenced by the lipid composition [Internet]. Journal of Physical Chemistry B. 2017 ; 121( 49): 11085-11095.[citado 2024 ago. 10 ] Available from: https://doi.org/10.1021/acs.jpcb.7b09642
  • Source: c-di-GMP Signaling. Unidade: IFSC

    Subjects: PROTEÍNAS, BIOFÍSICA

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      MATSUYAMA, Bruno Y. e KRASTEVA, Petya V. e NAVARRO, Marcos Vicente de Albuquerque Salles. Isothermal titration calorimetry to determine apparent dissociation constants (Kd) and stoichiometry of interaction (n) of C-di-GMP binding proteins. c-di-GMP Signaling. Tradução . New York: Humana Press, 2017. . Disponível em: https://doi.org/10.1007/978-1-4939-7240-1_30. Acesso em: 10 ago. 2024.
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      Matsuyama, B. Y., Krasteva, P. V., & Navarro, M. V. de A. S. (2017). Isothermal titration calorimetry to determine apparent dissociation constants (Kd) and stoichiometry of interaction (n) of C-di-GMP binding proteins. In c-di-GMP Signaling. New York: Humana Press. doi:10.1007/978-1-4939-7240-1_30
    • NLM

      Matsuyama BY, Krasteva PV, Navarro MV de AS. Isothermal titration calorimetry to determine apparent dissociation constants (Kd) and stoichiometry of interaction (n) of C-di-GMP binding proteins [Internet]. In: c-di-GMP Signaling. New York: Humana Press; 2017. [citado 2024 ago. 10 ] Available from: https://doi.org/10.1007/978-1-4939-7240-1_30
    • Vancouver

      Matsuyama BY, Krasteva PV, Navarro MV de AS. Isothermal titration calorimetry to determine apparent dissociation constants (Kd) and stoichiometry of interaction (n) of C-di-GMP binding proteins [Internet]. In: c-di-GMP Signaling. New York: Humana Press; 2017. [citado 2024 ago. 10 ] Available from: https://doi.org/10.1007/978-1-4939-7240-1_30
  • Source: Biophysical Journal. Conference titles: Annual Meeting of the Biophysical Society. Unidade: IFSC

    Subjects: ESQUISTOSSOMOSE, SCHISTOSOMA MANSONI

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      ZERAIK, Ana Eliza et al. STIM-Orai interaction in Schistosoma Mansoni indicates the existence of functional store-operated calcium entry in the parasite. Biophysical Journal. Saint Louis: Cell Press. Disponível em: https://doi.org/10.1016/j.bpj.2015.11.1441. Acesso em: 10 ago. 2024. , 2016
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      Zeraik, A. E., Fontes, M. G., Lopes, J. L. S., Araújo, A. P. U. de, & De Marco, R. (2016). STIM-Orai interaction in Schistosoma Mansoni indicates the existence of functional store-operated calcium entry in the parasite. Biophysical Journal. Saint Louis: Cell Press. doi:10.1016/j.bpj.2015.11.1441
    • NLM

      Zeraik AE, Fontes MG, Lopes JLS, Araújo APU de, De Marco R. STIM-Orai interaction in Schistosoma Mansoni indicates the existence of functional store-operated calcium entry in the parasite [Internet]. Biophysical Journal. 2016 ; 110( 3): 264a.[citado 2024 ago. 10 ] Available from: https://doi.org/10.1016/j.bpj.2015.11.1441
    • Vancouver

      Zeraik AE, Fontes MG, Lopes JLS, Araújo APU de, De Marco R. STIM-Orai interaction in Schistosoma Mansoni indicates the existence of functional store-operated calcium entry in the parasite [Internet]. Biophysical Journal. 2016 ; 110( 3): 264a.[citado 2024 ago. 10 ] Available from: https://doi.org/10.1016/j.bpj.2015.11.1441
  • Source: PLOS Neglected Tropical Diseases. Unidade: IFSC

    Subjects: ESQUISTOSSOMOSE, SCHISTOSOMA MANSONI

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      TORINI, Juliana Roberta et al. Crystal structure of Schistosoma mansoni adenosine phosphorylase/5'-methylthioadenosine phosphorylase and its importance on adenosine salvage pathway. PLOS Neglected Tropical Diseases, v. 10, n. 12, p. e0005178-1-e0005178-25, 2016Tradução . . Disponível em: https://doi.org/10.1371/journal.pntd.0005178. Acesso em: 10 ago. 2024.
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      Torini, J. R., Brandão Neto, J., De Marco, R., & Pereira, H. D. 'M. (2016). Crystal structure of Schistosoma mansoni adenosine phosphorylase/5'-methylthioadenosine phosphorylase and its importance on adenosine salvage pathway. PLOS Neglected Tropical Diseases, 10( 12), e0005178-1-e0005178-25. doi:10.1371/journal.pntd.0005178
    • NLM

      Torini JR, Brandão Neto J, De Marco R, Pereira HD'M. Crystal structure of Schistosoma mansoni adenosine phosphorylase/5'-methylthioadenosine phosphorylase and its importance on adenosine salvage pathway [Internet]. PLOS Neglected Tropical Diseases. 2016 ; 10( 12): e0005178-1-e0005178-25.[citado 2024 ago. 10 ] Available from: https://doi.org/10.1371/journal.pntd.0005178
    • Vancouver

      Torini JR, Brandão Neto J, De Marco R, Pereira HD'M. Crystal structure of Schistosoma mansoni adenosine phosphorylase/5'-methylthioadenosine phosphorylase and its importance on adenosine salvage pathway [Internet]. PLOS Neglected Tropical Diseases. 2016 ; 10( 12): e0005178-1-e0005178-25.[citado 2024 ago. 10 ] Available from: https://doi.org/10.1371/journal.pntd.0005178
  • Source: Abstracts. Conference titles: Latin American Protein Society Meeting - LAPSM. Unidade: IFSC

    Subjects: PROTEÍNAS, POLIMERIZAÇÃO, NUCLEOTÍDEOS

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      MARTINS, Carla Silva et al. Analysis of the heterotypic interaction interfaces between septin-septin. 2016, Anais.. Glendale: Latin American Protein Society - LAPS, 2016. Disponível em: http://eventoexpress.com.br/anais/laps2016/listaresumos_1.htm. Acesso em: 10 ago. 2024.
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      Martins, C. S., Macedo, J. N. A., Kumagai, P. S., Zeraik, A. E., & Araújo, A. P. U. de. (2016). Analysis of the heterotypic interaction interfaces between septin-septin. In Abstracts. Glendale: Latin American Protein Society - LAPS. Recuperado de http://eventoexpress.com.br/anais/laps2016/listaresumos_1.htm
    • NLM

      Martins CS, Macedo JNA, Kumagai PS, Zeraik AE, Araújo APU de. Analysis of the heterotypic interaction interfaces between septin-septin [Internet]. Abstracts. 2016 ;[citado 2024 ago. 10 ] Available from: http://eventoexpress.com.br/anais/laps2016/listaresumos_1.htm
    • Vancouver

      Martins CS, Macedo JNA, Kumagai PS, Zeraik AE, Araújo APU de. Analysis of the heterotypic interaction interfaces between septin-septin [Internet]. Abstracts. 2016 ;[citado 2024 ago. 10 ] Available from: http://eventoexpress.com.br/anais/laps2016/listaresumos_1.htm
  • Source: Proceedings of the National Academy of Sciences of the United States of America - PNAS. Unidade: IFSC

    Subjects: PSEUDOMONAS, BIOFILMES, PROTEÍNAS

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      MATSUYAMA, Bruno Y. et al. Mechanistic insights into c-di-GMP-dependent control of the biofilm regulator FleQ from Pseudomonas aeruginosa. Proceedings of the National Academy of Sciences of the United States of America - PNAS, v. 113, n. Ja 2016, p. E209-E218, 2016Tradução . . Disponível em: https://doi.org/10.1073/pnas.1523148113. Acesso em: 10 ago. 2024.
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      Matsuyama, B. Y., Krasteva, P. V., Baraquet, C., Harwood, C. S., Sondermann, H., & Navarro, M. V. de A. S. (2016). Mechanistic insights into c-di-GMP-dependent control of the biofilm regulator FleQ from Pseudomonas aeruginosa. Proceedings of the National Academy of Sciences of the United States of America - PNAS, 113( Ja 2016), E209-E218. doi:10.1073/pnas.1523148113
    • NLM

      Matsuyama BY, Krasteva PV, Baraquet C, Harwood CS, Sondermann H, Navarro MV de AS. Mechanistic insights into c-di-GMP-dependent control of the biofilm regulator FleQ from Pseudomonas aeruginosa [Internet]. Proceedings of the National Academy of Sciences of the United States of America - PNAS. 2016 ; 113( Ja 2016): E209-E218.[citado 2024 ago. 10 ] Available from: https://doi.org/10.1073/pnas.1523148113
    • Vancouver

      Matsuyama BY, Krasteva PV, Baraquet C, Harwood CS, Sondermann H, Navarro MV de AS. Mechanistic insights into c-di-GMP-dependent control of the biofilm regulator FleQ from Pseudomonas aeruginosa [Internet]. Proceedings of the National Academy of Sciences of the United States of America - PNAS. 2016 ; 113( Ja 2016): E209-E218.[citado 2024 ago. 10 ] Available from: https://doi.org/10.1073/pnas.1523148113
  • Source: PLOS ONE. Unidades: IF, IFSC

    Subjects: ENZIMAS, BIOTECNOLOGIA, BACTÉRIAS TERMÓFILAS

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      LOPES, José Luiz de Souza et al. Environmental factors modulating the stability and enzymatic activity of the Petrotoga mobilis Esterase (PmEst). PLOS ONE, v. 11, n. 6, p. e0158146-1-e0158146-16, 2016Tradução . . Disponível em: https://doi.org/10.1371/journal.pone.0158146. Acesso em: 10 ago. 2024.
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      Lopes, J. L. de S., Yoneda, J. S., Martins, J. M., De Marco, R., Jameson, D. M., Castro, A. M., et al. (2016). Environmental factors modulating the stability and enzymatic activity of the Petrotoga mobilis Esterase (PmEst). PLOS ONE, 11( 6), e0158146-1-e0158146-16. doi:10.1371/journal.pone.0158146
    • NLM

      Lopes JL de S, Yoneda JS, Martins JM, De Marco R, Jameson DM, Castro AM, Bossolan NRS, Wallace BA, Araújo APU de. Environmental factors modulating the stability and enzymatic activity of the Petrotoga mobilis Esterase (PmEst) [Internet]. PLOS ONE. 2016 ; 11( 6): e0158146-1-e0158146-16.[citado 2024 ago. 10 ] Available from: https://doi.org/10.1371/journal.pone.0158146
    • Vancouver

      Lopes JL de S, Yoneda JS, Martins JM, De Marco R, Jameson DM, Castro AM, Bossolan NRS, Wallace BA, Araújo APU de. Environmental factors modulating the stability and enzymatic activity of the Petrotoga mobilis Esterase (PmEst) [Internet]. PLOS ONE. 2016 ; 11( 6): e0158146-1-e0158146-16.[citado 2024 ago. 10 ] Available from: https://doi.org/10.1371/journal.pone.0158146
  • Source: Plant Physiology. Unidade: IFSC

    Subjects: MICROALGAS, VITAMINAS, REGULAÇÃO GÊNICA

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      HELLIWELL, Katherine E. et al. Unraveling vitamin B12-responsive gene regulation in Algae. Plant Physiology, v. 165, n. 1, p. 388-397, 2014Tradução . . Disponível em: https://doi.org/10.1104/pp.113.234369. Acesso em: 10 ago. 2024.
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      Helliwell, K. E., Scaife, M. A., Sasso, S., Araújo, A. P. U. de, Purton, S., & Smith, A. G. (2014). Unraveling vitamin B12-responsive gene regulation in Algae. Plant Physiology, 165( 1), 388-397. doi:10.1104/pp.113.234369
    • NLM

      Helliwell KE, Scaife MA, Sasso S, Araújo APU de, Purton S, Smith AG. Unraveling vitamin B12-responsive gene regulation in Algae [Internet]. Plant Physiology. 2014 ; 165( 1): 388-397.[citado 2024 ago. 10 ] Available from: https://doi.org/10.1104/pp.113.234369
    • Vancouver

      Helliwell KE, Scaife MA, Sasso S, Araújo APU de, Purton S, Smith AG. Unraveling vitamin B12-responsive gene regulation in Algae [Internet]. Plant Physiology. 2014 ; 165( 1): 388-397.[citado 2024 ago. 10 ] Available from: https://doi.org/10.1104/pp.113.234369
  • Source: Biophysical Journal. Conference titles: Annual Meeting of the Biophysical Society. Unidades: FFCLRP, IFSC

    Subjects: PROTEÍNAS (ESTUDO), LIPOSSOMOS, LIPÍDEOS

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      LOPES, Jose Luiz S. et al. Probing S100A12 interactions with model membranes. Biophysical Journal. Saint Louis: Cell Press. Disponível em: https://doi.org/10.1016/j.bpj.2013.11.2883. Acesso em: 10 ago. 2024. , 2014
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      Lopes, J. L. S., Garcia, A. F., Costa Filho, A. J. da, Wallace, B. A., & Araújo, A. P. U. de. (2014). Probing S100A12 interactions with model membranes. Biophysical Journal. Saint Louis: Cell Press. doi:10.1016/j.bpj.2013.11.2883
    • NLM

      Lopes JLS, Garcia AF, Costa Filho AJ da, Wallace BA, Araújo APU de. Probing S100A12 interactions with model membranes [Internet]. Biophysical Journal. 2014 ; 106( Ja 2014): 516a.[citado 2024 ago. 10 ] Available from: https://doi.org/10.1016/j.bpj.2013.11.2883
    • Vancouver

      Lopes JLS, Garcia AF, Costa Filho AJ da, Wallace BA, Araújo APU de. Probing S100A12 interactions with model membranes [Internet]. Biophysical Journal. 2014 ; 106( Ja 2014): 516a.[citado 2024 ago. 10 ] Available from: https://doi.org/10.1016/j.bpj.2013.11.2883
  • Source: PLOS Neglected Tropical Diseases. Unidade: IFSC

    Subjects: ESQUISTOSSOMOSE, PROTEÍNAS (ESTUDO), SCHISTOSOMA MANSONI

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      ZERAIK, Ana E. et al. Septins of platyhelminths: identification, phylogeny, expression and localization among developmental stages of Schistosoma mansoni. PLOS Neglected Tropical Diseases, v. 7, n. 12, p. e2602-1-e2602-14, 2013Tradução . . Disponível em: https://doi.org/10.1371/journal.pntd.0002602. Acesso em: 10 ago. 2024.
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      Zeraik, A. E., Rinaldi, G., Mann, V. H., Popratiloff, A., Araújo, A. P. U. de, De Marco, R., & Brindley, P. J. (2013). Septins of platyhelminths: identification, phylogeny, expression and localization among developmental stages of Schistosoma mansoni. PLOS Neglected Tropical Diseases, 7( 12), e2602-1-e2602-14. doi:10.1371/journal.pntd.0002602
    • NLM

      Zeraik AE, Rinaldi G, Mann VH, Popratiloff A, Araújo APU de, De Marco R, Brindley PJ. Septins of platyhelminths: identification, phylogeny, expression and localization among developmental stages of Schistosoma mansoni [Internet]. PLOS Neglected Tropical Diseases. 2013 ; 7( 12): e2602-1-e2602-14.[citado 2024 ago. 10 ] Available from: https://doi.org/10.1371/journal.pntd.0002602
    • Vancouver

      Zeraik AE, Rinaldi G, Mann VH, Popratiloff A, Araújo APU de, De Marco R, Brindley PJ. Septins of platyhelminths: identification, phylogeny, expression and localization among developmental stages of Schistosoma mansoni [Internet]. PLOS Neglected Tropical Diseases. 2013 ; 7( 12): e2602-1-e2602-14.[citado 2024 ago. 10 ] Available from: https://doi.org/10.1371/journal.pntd.0002602
  • Source: PLOS Neglected Tropical Diseases. Unidade: IFSC

    Subjects: ESQUISTOSSOMOSE, PROTEÍNAS (ESTUDO)

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      XIAO-HONG, Li et al. The schistosome oesophageal gland: initiator of blood processing. PLOS Neglected Tropical Diseases, v. 7, n. 7, p. e2337-1-e2337-15, 2013Tradução . . Disponível em: https://doi.org/10.1371/journal.pntd.0002337. Acesso em: 10 ago. 2024.
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      Xiao-Hong, L., Borges, W. de C., Parker-Manuel, S., Vance, G. M., De Marco, R., Neves, L. X., et al. (2013). The schistosome oesophageal gland: initiator of blood processing. PLOS Neglected Tropical Diseases, 7( 7), e2337-1-e2337-15. doi:10.1371/journal.pntd.0002337
    • NLM

      Xiao-Hong L, Borges W de C, Parker-Manuel S, Vance GM, De Marco R, Neves LX, Evans GJO, Wilson RA. The schistosome oesophageal gland: initiator of blood processing [Internet]. PLOS Neglected Tropical Diseases. 2013 ; 7( 7): e2337-1-e2337-15.[citado 2024 ago. 10 ] Available from: https://doi.org/10.1371/journal.pntd.0002337
    • Vancouver

      Xiao-Hong L, Borges W de C, Parker-Manuel S, Vance GM, De Marco R, Neves LX, Evans GJO, Wilson RA. The schistosome oesophageal gland: initiator of blood processing [Internet]. PLOS Neglected Tropical Diseases. 2013 ; 7( 7): e2337-1-e2337-15.[citado 2024 ago. 10 ] Available from: https://doi.org/10.1371/journal.pntd.0002337
  • Source: Biophysical Journal. Conference titles: Annual Meeting of the Biophysical Society. Unidade: IFSC

    Subjects: PROTEÍNAS (ESTUDO), ESPECTROSCOPIA, SCHISTOSOMA MANSONI

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      LOPES, Jose Luiz S. et al. Synchrotron radiation circular dichroism spectroscopy of MEG14, an intrinsically disordered protein. Biophysical Journal. Saint Louis: Cell Press. Disponível em: https://doi.org/10.1016/j.bpj.2012.11.1319. Acesso em: 10 ago. 2024. , 2013
    • APA

      Lopes, J. L. S., Orcia, D., De Marco, R., & Araújo, A. P. U. de. (2013). Synchrotron radiation circular dichroism spectroscopy of MEG14, an intrinsically disordered protein. Biophysical Journal. Saint Louis: Cell Press. doi:10.1016/j.bpj.2012.11.1319
    • NLM

      Lopes JLS, Orcia D, De Marco R, Araújo APU de. Synchrotron radiation circular dichroism spectroscopy of MEG14, an intrinsically disordered protein [Internet]. Biophysical Journal. 2013 ; 104( Ja 2013): 234a.[citado 2024 ago. 10 ] Available from: https://doi.org/10.1016/j.bpj.2012.11.1319
    • Vancouver

      Lopes JLS, Orcia D, De Marco R, Araújo APU de. Synchrotron radiation circular dichroism spectroscopy of MEG14, an intrinsically disordered protein [Internet]. Biophysical Journal. 2013 ; 104( Ja 2013): 234a.[citado 2024 ago. 10 ] Available from: https://doi.org/10.1016/j.bpj.2012.11.1319

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