Filtros : "PROTEÍNAS" "Financiamento NSF" Removidos: "IQ004" "iq" "223" "IFSC222" "ABDALLA, ELCIO" Limpar

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  • Source: Journal of Natural Products. Unidades: IFSC, IQSC

    Subjects: METABOLISMO, PEPTÍDEOS, PROTEÍNAS

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    • ABNT

      AMORIM, Marcelo Rodrigues de et al. Structure and biosynthesis of perochalasins A-C, open-chain merocytochalasans produced by the marine-derived fungus Peroneutypa sp. M16. Journal of Natural Products, 2024Tradução . . Disponível em: https://doi.org/10.1021/acs.jnatprod.4c00516. Acesso em: 14 set. 2024.
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      Amorim, M. R. de, Schoellhorn, S. M., Barbosa, C. de S., Mendes, G. R., Macedo, K. L. de, Ferreira, A. G., et al. (2024). Structure and biosynthesis of perochalasins A-C, open-chain merocytochalasans produced by the marine-derived fungus Peroneutypa sp. M16. Journal of Natural Products. doi:10.1021/acs.jnatprod.4c00516
    • NLM

      Amorim MR de, Schoellhorn SM, Barbosa C de S, Mendes GR, Macedo KL de, Ferreira AG, Venâncio T, Guido RVC, Batista ANL, Batista Jr. JM, Skellam E, Berlinck RG de S. Structure and biosynthesis of perochalasins A-C, open-chain merocytochalasans produced by the marine-derived fungus Peroneutypa sp. M16 [Internet]. Journal of Natural Products. 2024 ;[citado 2024 set. 14 ] Available from: https://doi.org/10.1021/acs.jnatprod.4c00516
    • Vancouver

      Amorim MR de, Schoellhorn SM, Barbosa C de S, Mendes GR, Macedo KL de, Ferreira AG, Venâncio T, Guido RVC, Batista ANL, Batista Jr. JM, Skellam E, Berlinck RG de S. Structure and biosynthesis of perochalasins A-C, open-chain merocytochalasans produced by the marine-derived fungus Peroneutypa sp. M16 [Internet]. Journal of Natural Products. 2024 ;[citado 2024 set. 14 ] Available from: https://doi.org/10.1021/acs.jnatprod.4c00516
  • Source: Science. Unidades: IFSC, FCFRP

    Subjects: COVID-19, ENZIMAS, ESPECTROSCOPIA, PROTEÍNAS, PLANEJAMENTO DE FÁRMACOS, MICROSCOPIA

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    • ABNT

      BOBY, Melissa L. et al. Open science discovery of potent noncovalent SARS-CoV-2 main protease inhibitors. Science, v. 382, n. 6671, p. eabo7201-1-eabo7201-16 + supplementary materials, 2023Tradução . . Disponível em: https://doi.org/10.1126/science.abo7201. Acesso em: 14 set. 2024.
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      Boby, M. L., Fernandes, R. S., Gawriljuk, V. O., Godoy, A. S. de, Nakamura, A. M., Noske, G. D., et al. (2023). Open science discovery of potent noncovalent SARS-CoV-2 main protease inhibitors. Science, 382( 6671), eabo7201-1-eabo7201-16 + supplementary materials. doi:10.1126/science.abo7201
    • NLM

      Boby ML, Fernandes RS, Gawriljuk VO, Godoy AS de, Nakamura AM, Noske GD, Oliva G, Rangel VL. Open science discovery of potent noncovalent SARS-CoV-2 main protease inhibitors [Internet]. Science. 2023 ; 382( 6671): eabo7201-1-eabo7201-16 + supplementary materials.[citado 2024 set. 14 ] Available from: https://doi.org/10.1126/science.abo7201
    • Vancouver

      Boby ML, Fernandes RS, Gawriljuk VO, Godoy AS de, Nakamura AM, Noske GD, Oliva G, Rangel VL. Open science discovery of potent noncovalent SARS-CoV-2 main protease inhibitors [Internet]. Science. 2023 ; 382( 6671): eabo7201-1-eabo7201-16 + supplementary materials.[citado 2024 set. 14 ] Available from: https://doi.org/10.1126/science.abo7201
  • Source: mSphere. Unidades: FMRP, FCFRP

    Subjects: ASPERGILLUS, PROTEÍNAS, EXPRESSÃO GÊNICA, GENOMAS, MUTAÇÃO, METABOLISMO

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      DROTT, M. T. et al. Diversity of secondary metabolism in Aspergillus nidulans clinical isolates. mSphere, v. 5, n. 2, p. 1-13, 2020Tradução . . Disponível em: https://doi.org/10.1128/mSphere.00156-20. Acesso em: 14 set. 2024.
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      Drott, M. T., Bastos, R. W., Rokas, A., Ries, L. N. A., Gabaldon, T., Goldman, G. H., et al. (2020). Diversity of secondary metabolism in Aspergillus nidulans clinical isolates. mSphere, 5( 2), 1-13. doi:10.1128/mSphere.00156-20
    • NLM

      Drott MT, Bastos RW, Rokas A, Ries LNA, Gabaldon T, Goldman GH, Keller NP, Greco C. Diversity of secondary metabolism in Aspergillus nidulans clinical isolates [Internet]. mSphere. 2020 ; 5( 2): 1-13.[citado 2024 set. 14 ] Available from: https://doi.org/10.1128/mSphere.00156-20
    • Vancouver

      Drott MT, Bastos RW, Rokas A, Ries LNA, Gabaldon T, Goldman GH, Keller NP, Greco C. Diversity of secondary metabolism in Aspergillus nidulans clinical isolates [Internet]. mSphere. 2020 ; 5( 2): 1-13.[citado 2024 set. 14 ] Available from: https://doi.org/10.1128/mSphere.00156-20
  • Source: Annual Review of Entomology. Unidade: ESALQ

    Subjects: BICHOS-DA-SEDA, DROSOPHILA, ENZIMAS, FEROMÔNIOS SEXUAIS, OLFATO, PROTEÍNAS, RECEPTORES SENSORIAIS

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    • ABNT

      LEAL, Walter Soares. Odorant reception in insects: roles of receptors, binding proteins, and degrading enzymes. Annual Review of Entomology, v. 58, p. 373-391, 2013Tradução . . Disponível em: https://doi.org/10.1146/annurev-ento-120811-153635. Acesso em: 14 set. 2024.
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      Leal, W. S. (2013). Odorant reception in insects: roles of receptors, binding proteins, and degrading enzymes. Annual Review of Entomology, 58, 373-391. doi:10.1146/annurev-ento-120811-153635
    • NLM

      Leal WS. Odorant reception in insects: roles of receptors, binding proteins, and degrading enzymes [Internet]. Annual Review of Entomology. 2013 ; 58 373-391.[citado 2024 set. 14 ] Available from: https://doi.org/10.1146/annurev-ento-120811-153635
    • Vancouver

      Leal WS. Odorant reception in insects: roles of receptors, binding proteins, and degrading enzymes [Internet]. Annual Review of Entomology. 2013 ; 58 373-391.[citado 2024 set. 14 ] Available from: https://doi.org/10.1146/annurev-ento-120811-153635
  • Source: PLOS ONE. Unidade: ESALQ

    Subjects: CRISTALOGRAFIA ESTRUTURAL, FEROMÔNIOS SEXUAIS, LAGARTAS, OLFATO, PROTEÍNAS, RECEPTORES SENSORIAIS

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      DI LUCCIO, Eric et al. Crystallographic observation of pH-induced conformational changes in the Amyelois transitella Pheromone-binding protein AtraPBP1. PLOS ONE, v. 8, n. 2, p. 1-7, 2013Tradução . . Disponível em: https://doi.org/10.1371/journal.pone.0053840. Acesso em: 14 set. 2024.
    • APA

      di Luccio, E., Ishida, Y., Leal, W. S., & Wilson, D. K. (2013). Crystallographic observation of pH-induced conformational changes in the Amyelois transitella Pheromone-binding protein AtraPBP1. PLOS ONE, 8( 2), 1-7. doi:10.1371/journal.pone.0053840
    • NLM

      di Luccio E, Ishida Y, Leal WS, Wilson DK. Crystallographic observation of pH-induced conformational changes in the Amyelois transitella Pheromone-binding protein AtraPBP1 [Internet]. PLOS ONE. 2013 ; 8( 2): 1-7.[citado 2024 set. 14 ] Available from: https://doi.org/10.1371/journal.pone.0053840
    • Vancouver

      di Luccio E, Ishida Y, Leal WS, Wilson DK. Crystallographic observation of pH-induced conformational changes in the Amyelois transitella Pheromone-binding protein AtraPBP1 [Internet]. PLOS ONE. 2013 ; 8( 2): 1-7.[citado 2024 set. 14 ] Available from: https://doi.org/10.1371/journal.pone.0053840
  • Source: Biochemical and Biophysical Research Communications. Unidade: ESALQ

    Subjects: FEROMÔNIOS SEXUAIS, LAGARTAS, LARANJA, PROTEÍNAS

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      XU, Wei et al. Extrusion of the C-terminal helix in navel orangeworm moth pheromone-binding protein (AtraPBP1) controls pheromone binding. Biochemical and Biophysical Research Communications, v. 404, n. 1, p. 335–338, 2011Tradução . . Disponível em: https://doi.org/10.1016/j.bbrc.2010.11.119. Acesso em: 14 set. 2024.
    • APA

      Xu, W., Xu, X., Leal, W. S., & Ames, J. B. (2011). Extrusion of the C-terminal helix in navel orangeworm moth pheromone-binding protein (AtraPBP1) controls pheromone binding. Biochemical and Biophysical Research Communications, 404( 1), 335–338. doi:10.1016/j.bbrc.2010.11.119
    • NLM

      Xu W, Xu X, Leal WS, Ames JB. Extrusion of the C-terminal helix in navel orangeworm moth pheromone-binding protein (AtraPBP1) controls pheromone binding [Internet]. Biochemical and Biophysical Research Communications. 2011 ; 404( 1): 335–338.[citado 2024 set. 14 ] Available from: https://doi.org/10.1016/j.bbrc.2010.11.119
    • Vancouver

      Xu W, Xu X, Leal WS, Ames JB. Extrusion of the C-terminal helix in navel orangeworm moth pheromone-binding protein (AtraPBP1) controls pheromone binding [Internet]. Biochemical and Biophysical Research Communications. 2011 ; 404( 1): 335–338.[citado 2024 set. 14 ] Available from: https://doi.org/10.1016/j.bbrc.2010.11.119
  • Source: PLOS ONE. Unidade: ESALQ

    Subjects: FEROMÔNIOS DE ALARME, FLUORESCÊNCIA, INSETOS PREDADORES, OLFATO, PROTEÍNAS, PULGÃO, REAÇÃO EM CADEIA POR POLIMERASE

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      VANDERMOTEN, Sophie et al. Conserved odorant-binding proteins from Aphids and Eavesdropping predators. PLOS ONE, v. 6, n. 8, p. 1-6, 2011Tradução . . Disponível em: https://doi.org/10.1371/journal.pone.0023608. Acesso em: 14 set. 2024.
    • APA

      Vandermoten, S., Francis, F., Haubruge, E., & Leal, W. S. (2011). Conserved odorant-binding proteins from Aphids and Eavesdropping predators. PLOS ONE, 6( 8), 1-6. doi:10.1371/journal.pone.0023608
    • NLM

      Vandermoten S, Francis F, Haubruge E, Leal WS. Conserved odorant-binding proteins from Aphids and Eavesdropping predators [Internet]. PLOS ONE. 2011 ; 6( 8): 1-6.[citado 2024 set. 14 ] Available from: https://doi.org/10.1371/journal.pone.0023608
    • Vancouver

      Vandermoten S, Francis F, Haubruge E, Leal WS. Conserved odorant-binding proteins from Aphids and Eavesdropping predators [Internet]. PLOS ONE. 2011 ; 6( 8): 1-6.[citado 2024 set. 14 ] Available from: https://doi.org/10.1371/journal.pone.0023608
  • Source: Proceedings of the National Academy of Sciences. Unidade: ESALQ

    Subjects: CRISTALOGRAFIA DE RAIOS X, CULEX, FEROMÔNIOS, MOSQUITOS, OLFATO, OVIPOSIÇÃO, PROTEÍNAS, RECEPTORES SENSORIAIS

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      MAO, Y et al. Crystal and solution structures of an odorant-binding protein from the southern house mosquito complexed with an oviposition pheromone. Proceedings of the National Academy of Sciences, v. 107 | n. 44, p. 19102-1910, 2010Tradução . . Disponível em: https://doi.org/10.1073/pnas.1012274107. Acesso em: 14 set. 2024.
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      Mao, Y., Xu, X., Xu, W., Ishida, Y., Leal, W. S., Ames, J. B., & Clardy, J. (2010). Crystal and solution structures of an odorant-binding protein from the southern house mosquito complexed with an oviposition pheromone. Proceedings of the National Academy of Sciences, 107 | n. 44, 19102-1910. doi:10.1073/pnas.1012274107
    • NLM

      Mao Y, Xu X, Xu W, Ishida Y, Leal WS, Ames JB, Clardy J. Crystal and solution structures of an odorant-binding protein from the southern house mosquito complexed with an oviposition pheromone [Internet]. Proceedings of the National Academy of Sciences. 2010 ; 107 | n. 44 19102-1910.[citado 2024 set. 14 ] Available from: https://doi.org/10.1073/pnas.1012274107
    • Vancouver

      Mao Y, Xu X, Xu W, Ishida Y, Leal WS, Ames JB, Clardy J. Crystal and solution structures of an odorant-binding protein from the southern house mosquito complexed with an oviposition pheromone [Internet]. Proceedings of the National Academy of Sciences. 2010 ; 107 | n. 44 19102-1910.[citado 2024 set. 14 ] Available from: https://doi.org/10.1073/pnas.1012274107
  • Source: Biochemistry. Unidade: ESALQ

    Subjects: ACASALAMENTO, FEROMÔNIOS SEXUAIS, LAGARTAS, PROTEÍNAS, RESSONÂNCIA MAGNÉTICA NUCLEAR

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      XU, Xianzhong et al. NMR structure of navel orangeworm moth pheromone-binding protein (AtraPBP1): implications for pH-sensitive pheromone detection. Biochemistry, v. 49, n. 7, p. 1469-1476, 2010Tradução . . Disponível em: https://doi.org/10.1021/bi9020132. Acesso em: 14 set. 2024.
    • APA

      Xu, X., Xu, W., Rayo, J., Ishida, Y., Leal, W. S., & Ames, J. B. (2010). NMR structure of navel orangeworm moth pheromone-binding protein (AtraPBP1): implications for pH-sensitive pheromone detection. Biochemistry, 49( 7), 1469-1476. doi:10.1021/bi9020132
    • NLM

      Xu X, Xu W, Rayo J, Ishida Y, Leal WS, Ames JB. NMR structure of navel orangeworm moth pheromone-binding protein (AtraPBP1): implications for pH-sensitive pheromone detection [Internet]. Biochemistry. 2010 ; 49( 7): 1469-1476.[citado 2024 set. 14 ] Available from: https://doi.org/10.1021/bi9020132
    • Vancouver

      Xu X, Xu W, Rayo J, Ishida Y, Leal WS, Ames JB. NMR structure of navel orangeworm moth pheromone-binding protein (AtraPBP1): implications for pH-sensitive pheromone detection [Internet]. Biochemistry. 2010 ; 49( 7): 1469-1476.[citado 2024 set. 14 ] Available from: https://doi.org/10.1021/bi9020132
  • Source: PLOS ONE. Unidades: ESALQ, IFSC

    Subjects: AEDES, PROTEÍNAS, DENGUE

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      LEITE, Ney Ribeiro et al. Structure of an odorant-binding protein from the mosquito Aedes aegypti suggests a binding pocket covered by a pH-sensitive "lid". PLOS ONE, v. 4, n. 11, p. 1-7, 2009Tradução . . Disponível em: https://doi.org/10.1371/journal.pone.0008006.t001. Acesso em: 14 set. 2024.
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      Leite, N. R., Krogh, R., Xu, W., Ishida, Y., Iulek, J., Leal, W. S., & Oliva, G. (2009). Structure of an odorant-binding protein from the mosquito Aedes aegypti suggests a binding pocket covered by a pH-sensitive "lid". PLOS ONE, 4( 11), 1-7. doi:10.1371/journal.pone.0008006.t001
    • NLM

      Leite NR, Krogh R, Xu W, Ishida Y, Iulek J, Leal WS, Oliva G. Structure of an odorant-binding protein from the mosquito Aedes aegypti suggests a binding pocket covered by a pH-sensitive "lid" [Internet]. PLOS ONE. 2009 ; 4( 11): 1-7.[citado 2024 set. 14 ] Available from: https://doi.org/10.1371/journal.pone.0008006.t001
    • Vancouver

      Leite NR, Krogh R, Xu W, Ishida Y, Iulek J, Leal WS, Oliva G. Structure of an odorant-binding protein from the mosquito Aedes aegypti suggests a binding pocket covered by a pH-sensitive "lid" [Internet]. PLOS ONE. 2009 ; 4( 11): 1-7.[citado 2024 set. 14 ] Available from: https://doi.org/10.1371/journal.pone.0008006.t001
  • Source: Biomolecular NMR Assignments. Unidade: ESALQ

    Subjects: FEROMÔNIOS, LAGARTAS, OLFATO, PROTEÍNAS, RECEPTORES SENSORIAIS

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      XU, Xianzhong et al. 1H, 15N, and 13C Chemical shift assignments of the navel orange worm pheromone-binding protein-1 (Atra-PBP1). Biomolecular NMR Assignments, v. 2, n. 2 , p. 105-106, 2008Tradução . . Disponível em: https://doi.org/10.1007/s12104-008-9096-6. Acesso em: 14 set. 2024.
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      Xu, X., Li, Y., Rayo, J., Ishida, Y., Leal, W. S., & Ames, J. B. (2008). 1H, 15N, and 13C Chemical shift assignments of the navel orange worm pheromone-binding protein-1 (Atra-PBP1). Biomolecular NMR Assignments, 2( 2 ), 105-106. doi:10.1007/s12104-008-9096-6
    • NLM

      Xu X, Li Y, Rayo J, Ishida Y, Leal WS, Ames JB. 1H, 15N, and 13C Chemical shift assignments of the navel orange worm pheromone-binding protein-1 (Atra-PBP1) [Internet]. Biomolecular NMR Assignments. 2008 ;2( 2 ): 105-106.[citado 2024 set. 14 ] Available from: https://doi.org/10.1007/s12104-008-9096-6
    • Vancouver

      Xu X, Li Y, Rayo J, Ishida Y, Leal WS, Ames JB. 1H, 15N, and 13C Chemical shift assignments of the navel orange worm pheromone-binding protein-1 (Atra-PBP1) [Internet]. Biomolecular NMR Assignments. 2008 ;2( 2 ): 105-106.[citado 2024 set. 14 ] Available from: https://doi.org/10.1007/s12104-008-9096-6
  • Source: Structure. Unidade: ESALQ

    Subjects: BICHOS-DA-SEDA, FEROMÔNIOS SEXUAIS, OLFATO, PROTEÍNAS, RECEPTORES SENSORIAIS

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      LAUTENSCHLAGER, Catherine e LEAL, Walter Soares e CLARDY, Jon. Bombyx mori pheromone-binding protein binding nonpheromone ligands: implications for pheromone recognition. Structure, v. 15, n. 9 , p. 1148-115, 2007Tradução . . Disponível em: https://doi.org/10.1016/j.str.2007.07.013. Acesso em: 14 set. 2024.
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      Lautenschlager, C., Leal, W. S., & Clardy, J. (2007). Bombyx mori pheromone-binding protein binding nonpheromone ligands: implications for pheromone recognition. Structure, 15( 9 ), 1148-115. doi:10.1016/j.str.2007.07.013
    • NLM

      Lautenschlager C, Leal WS, Clardy J. Bombyx mori pheromone-binding protein binding nonpheromone ligands: implications for pheromone recognition [Internet]. Structure. 2007 ; 15( 9 ): 1148-115.[citado 2024 set. 14 ] Available from: https://doi.org/10.1016/j.str.2007.07.013
    • Vancouver

      Lautenschlager C, Leal WS, Clardy J. Bombyx mori pheromone-binding protein binding nonpheromone ligands: implications for pheromone recognition [Internet]. Structure. 2007 ; 15( 9 ): 1148-115.[citado 2024 set. 14 ] Available from: https://doi.org/10.1016/j.str.2007.07.013

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