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Filtros : "Polikarpov, Igor" "Textor, Larissa C." Removido: "Baruselli, Pietro Sampaio" Limpar

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1 - 10 (10 records)

  • Artigo de periodico

    An alternative conformation of ERβ bound to estradiol reveals H12 in a stable antagonist position (2017)

    Souza, Paulo C. T.; Textor, Larissa C.; Melo, Denise C.; Nascimento, Alessandro Silva; Skaf, Munir S.; Polikarpov, Igor

    Source: Scientific Reports. Unidade: IFSC

    Subjects: ESTRADIOL, RECEPTORES, CRISTALOGRAFIA ESTRUTURAL

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    • ABNT

      SOUZA, Paulo C. T. et al. An alternative conformation of ERβ bound to estradiol reveals H12 in a stable antagonist position. Scientific Reports, v. 7, p. 3509-1-3509-11, 2017Tradução . . Disponível em: https://doi.org/10.1038/s41598-017-03774-x. Acesso em: 24 maio 2024.

    • APA

      Souza, P. C. T., Textor, L. C., Melo, D. C., Nascimento, A. S., Skaf, M. S., & Polikarpov, I. (2017). An alternative conformation of ERβ bound to estradiol reveals H12 in a stable antagonist position. Scientific Reports, 7, 3509-1-3509-11. doi:10.1038/s41598-017-03774-x

    • NLM

      Souza PCT, Textor LC, Melo DC, Nascimento AS, Skaf MS, Polikarpov I. An alternative conformation of ERβ bound to estradiol reveals H12 in a stable antagonist position [Internet]. Scientific Reports. 2017 ; 7 3509-1-3509-11.[citado 2024 maio 24 ] Available from: https://doi.org/10.1038/s41598-017-03774-x

    • Vancouver

      Souza PCT, Textor LC, Melo DC, Nascimento AS, Skaf MS, Polikarpov I. An alternative conformation of ERβ bound to estradiol reveals H12 in a stable antagonist position [Internet]. Scientific Reports. 2017 ; 7 3509-1-3509-11.[citado 2024 maio 24 ] Available from: https://doi.org/10.1038/s41598-017-03774-x

  • Artigo de periodico

    Crystal structure analysis of peroxidase from the palm tree Chamaerops excelsa (2015)

    Bernardes, Amanda; Textor, Larissa C.; Santos, Jademilson C.; Cuadrado, Nazaret Hidalgo; Kostetsky, Eduard Ya.; Roig, Manuel G.; Bavro, Vassiliy N.; Muniz, João Renato Carvalho; Shnyrov, Valery L.; Polikarpov, Igor

    Source: Biochimie. Unidade: IFSC

    Subjects: PEROXIDASE, PALMEIRAS, CRISTALOGRAFIA

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    • ABNT

      BERNARDES, Amanda et al. Crystal structure analysis of peroxidase from the palm tree Chamaerops excelsa. Biochimie, v. 111, p. 58-69, 2015Tradução . . Disponível em: https://doi.org/10.1016/j.biochi.2015.01.014. Acesso em: 24 maio 2024.

    • APA

      Bernardes, A., Textor, L. C., Santos, J. C., Cuadrado, N. H., Kostetsky, E. Y., Roig, M. G., et al. (2015). Crystal structure analysis of peroxidase from the palm tree Chamaerops excelsa. Biochimie, 111, 58-69. doi:10.1016/j.biochi.2015.01.014

    • NLM

      Bernardes A, Textor LC, Santos JC, Cuadrado NH, Kostetsky EY, Roig MG, Bavro VN, Muniz JRC, Shnyrov VL, Polikarpov I. Crystal structure analysis of peroxidase from the palm tree Chamaerops excelsa [Internet]. Biochimie. 2015 ; 111 58-69.[citado 2024 maio 24 ] Available from: https://doi.org/10.1016/j.biochi.2015.01.014

    • Vancouver

      Bernardes A, Textor LC, Santos JC, Cuadrado NH, Kostetsky EY, Roig MG, Bavro VN, Muniz JRC, Shnyrov VL, Polikarpov I. Crystal structure analysis of peroxidase from the palm tree Chamaerops excelsa [Internet]. Biochimie. 2015 ; 111 58-69.[citado 2024 maio 24 ] Available from: https://doi.org/10.1016/j.biochi.2015.01.014

  • Artigo de periodico

    Sets of covariant residues modulate the activity and thermal stability of GH1 β-glucosidases (2014)

    Tamaki, Fábio K.; Textor, Larissa C.; Polikarpov, Igor; Marana, Sandro Roberto

    Source: PLOS ONE. Unidades: IFSC, IQ

    Subjects: ENZIMAS (ESTUDO), PROTEÍNAS, AMINOÁCIDOS

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    • ABNT

      TAMAKI, Fábio K. et al. Sets of covariant residues modulate the activity and thermal stability of GH1 β-glucosidases. PLOS ONE, v. 9, n. 5, p. e96627-1-e96627-8, 2014Tradução . . Disponível em: https://doi.org/10.1371/journal.pone.0096627. Acesso em: 24 maio 2024.

    • APA

      Tamaki, F. K., Textor, L. C., Polikarpov, I., & Marana, S. R. (2014). Sets of covariant residues modulate the activity and thermal stability of GH1 β-glucosidases. PLOS ONE, 9( 5), e96627-1-e96627-8. doi:10.1371/journal.pone.0096627

    • NLM

      Tamaki FK, Textor LC, Polikarpov I, Marana SR. Sets of covariant residues modulate the activity and thermal stability of GH1 β-glucosidases [Internet]. PLOS ONE. 2014 ; 9( 5): e96627-1-e96627-8.[citado 2024 maio 24 ] Available from: https://doi.org/10.1371/journal.pone.0096627

    • Vancouver

      Tamaki FK, Textor LC, Polikarpov I, Marana SR. Sets of covariant residues modulate the activity and thermal stability of GH1 β-glucosidases [Internet]. PLOS ONE. 2014 ; 9( 5): e96627-1-e96627-8.[citado 2024 maio 24 ] Available from: https://doi.org/10.1371/journal.pone.0096627

  • Trabalho de evento-resumo

    Sets of co-variant positions in β-glucosidases are involved in modulating the activity and the thermal stability (2014)

    Tamaki, Fábio K.; Textor, Larissa C.; Polikarpov, Igor; Marana, Sandro Roberto

    Source: Program and Index. Conference titles: Annual Meeting of the Brazilian Biochemistry and Molecular Biology Society - SBBq. Unidades: IFSC, IQ

    Subjects: ENZIMAS, BIOTECNOLOGIA

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    • ABNT

      TAMAKI, Fábio K. et al. Sets of co-variant positions in β-glucosidases are involved in modulating the activity and the thermal stability. 2014, Anais.. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular - SBBq, 2014. Disponível em: http://www.sigeventos.com.br/sbbq/cd/2014/resumos/R03134-1.pdf. Acesso em: 24 maio 2024.

    • APA

      Tamaki, F. K., Textor, L. C., Polikarpov, I., & Marana, S. R. (2014). Sets of co-variant positions in β-glucosidases are involved in modulating the activity and the thermal stability. In Program and Index. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular - SBBq. Recuperado de http://www.sigeventos.com.br/sbbq/cd/2014/resumos/R03134-1.pdf

    • NLM

      Tamaki FK, Textor LC, Polikarpov I, Marana SR. Sets of co-variant positions in β-glucosidases are involved in modulating the activity and the thermal stability [Internet]. Program and Index. 2014 ;[citado 2024 maio 24 ] Available from: http://www.sigeventos.com.br/sbbq/cd/2014/resumos/R03134-1.pdf

    • Vancouver

      Tamaki FK, Textor LC, Polikarpov I, Marana SR. Sets of co-variant positions in β-glucosidases are involved in modulating the activity and the thermal stability [Internet]. Program and Index. 2014 ;[citado 2024 maio 24 ] Available from: http://www.sigeventos.com.br/sbbq/cd/2014/resumos/R03134-1.pdf

  • Trabalho de evento-resumo periodico

    Functional sectors involved in thermal stability and activity in beta-glucosidases (2014)

    Tamaki, Fabio K.; Textor, Larissa C.; Polikarpov, Igor; Marana, Sandro Roberto

    Source: Protein Science. Conference titles: Annual Symposium of the Protein Society. Unidades: IFSC, IQ

    Subjects: ENZIMAS, TEMPERATURA

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    • ABNT

      TAMAKI, Fabio K. et al. Functional sectors involved in thermal stability and activity in beta-glucosidases. Protein Science. Hoboken: Wiley-Blackwell. Disponível em: https://doi.org/10.1002/pro.2504. Acesso em: 24 maio 2024. , 2014

    • APA

      Tamaki, F. K., Textor, L. C., Polikarpov, I., & Marana, S. R. (2014). Functional sectors involved in thermal stability and activity in beta-glucosidases. Protein Science. Hoboken: Wiley-Blackwell. doi:10.1002/pro.2504

    • NLM

      Tamaki FK, Textor LC, Polikarpov I, Marana SR. Functional sectors involved in thermal stability and activity in beta-glucosidases [Internet]. Protein Science. 2014 ; 23( S1): 190-191.[citado 2024 maio 24 ] Available from: https://doi.org/10.1002/pro.2504

    • Vancouver

      Tamaki FK, Textor LC, Polikarpov I, Marana SR. Functional sectors involved in thermal stability and activity in beta-glucosidases [Internet]. Protein Science. 2014 ; 23( S1): 190-191.[citado 2024 maio 24 ] Available from: https://doi.org/10.1002/pro.2504

  • Artigo de periodico

    Joint X-ray crystallographic and molecular dynamics study of cellobiohydrolase I from Trichoderma harzianum: deciphering the structural features of cellobiohydrolase catalytic activity (2013)

    Textor, Larissa C.; Colussi, Francieli; Silveira, Rodrigo L.; Serpa, Viviane; Mello, Bruno L.; Muniz, João Renato C.; Squina, Fabio M.; Pereira Júnior, Nei; Skaf, Munir S.; Polikarpov, Igor

    Source: FEBS Journal. Unidade: IFSC

    Subjects: TRICHODERMA (ESTUDO), BIOMASSA, HIDRÓLISE

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    • ABNT

      TEXTOR, Larissa C. et al. Joint X-ray crystallographic and molecular dynamics study of cellobiohydrolase I from Trichoderma harzianum: deciphering the structural features of cellobiohydrolase catalytic activity. FEBS Journal, v. 280, n. Ja 2013, p. 56-69, 2013Tradução . . Disponível em: https://doi.org/10.1111/febs.12049. Acesso em: 24 maio 2024.

    • APA

      Textor, L. C., Colussi, F., Silveira, R. L., Serpa, V., Mello, B. L., Muniz, J. R. C., et al. (2013). Joint X-ray crystallographic and molecular dynamics study of cellobiohydrolase I from Trichoderma harzianum: deciphering the structural features of cellobiohydrolase catalytic activity. FEBS Journal, 280( Ja 2013), 56-69. doi:10.1111/febs.12049

    • NLM

      Textor LC, Colussi F, Silveira RL, Serpa V, Mello BL, Muniz JRC, Squina FM, Pereira Júnior N, Skaf MS, Polikarpov I. Joint X-ray crystallographic and molecular dynamics study of cellobiohydrolase I from Trichoderma harzianum: deciphering the structural features of cellobiohydrolase catalytic activity [Internet]. FEBS Journal. 2013 ; 280( Ja 2013): 56-69.[citado 2024 maio 24 ] Available from: https://doi.org/10.1111/febs.12049

    • Vancouver

      Textor LC, Colussi F, Silveira RL, Serpa V, Mello BL, Muniz JRC, Squina FM, Pereira Júnior N, Skaf MS, Polikarpov I. Joint X-ray crystallographic and molecular dynamics study of cellobiohydrolase I from Trichoderma harzianum: deciphering the structural features of cellobiohydrolase catalytic activity [Internet]. FEBS Journal. 2013 ; 280( Ja 2013): 56-69.[citado 2024 maio 24 ] Available from: https://doi.org/10.1111/febs.12049

  • Trabalho de evento-resumo

    Effects on the thermal stability and enzymatic activity caused by substitutions of co-variant amino acids of the 'beta'-glucosidase from Spodoptera frugiperda (2012)

    Tamaki, Fabio K.; Textor, Larissa C.; Polikarpov, Igor; Marana, Sandro Roberto

    Source: Program. Conference titles: Congress of the International Union of Biochemistry and Molecular Biology - IUBMB. Unidades: IFSC, IQ

    Subjects: ENZIMAS (ESTUDO), PROTEÍNAS, AMINOÁCIDOS

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    • ABNT

      TAMAKI, Fabio K. et al. Effects on the thermal stability and enzymatic activity caused by substitutions of co-variant amino acids of the 'beta'-glucosidase from Spodoptera frugiperda. 2012, Anais.. Madri: Sociedad Española de Bioquímica y Biología Molecular - SEBBM, 2012. . Acesso em: 24 maio 2024.

    • APA

      Tamaki, F. K., Textor, L. C., Polikarpov, I., & Marana, S. R. (2012). Effects on the thermal stability and enzymatic activity caused by substitutions of co-variant amino acids of the 'beta'-glucosidase from Spodoptera frugiperda. In Program. Madri: Sociedad Española de Bioquímica y Biología Molecular - SEBBM.

    • NLM

      Tamaki FK, Textor LC, Polikarpov I, Marana SR. Effects on the thermal stability and enzymatic activity caused by substitutions of co-variant amino acids of the 'beta'-glucosidase from Spodoptera frugiperda. Program. 2012 ;[citado 2024 maio 24 ]

    • Vancouver

      Tamaki FK, Textor LC, Polikarpov I, Marana SR. Effects on the thermal stability and enzymatic activity caused by substitutions of co-variant amino acids of the 'beta'-glucosidase from Spodoptera frugiperda. Program. 2012 ;[citado 2024 maio 24 ]

  • Artigo de periodico

    Purification, crystallization and preliminary crystallographic analysis of peroxidase from the palm tree Chamaerops excelsa (2011)

    Textor, Larissa C.; Santos, Jademilson C.; Cuadrado, Nazaret Hidalgo; Roig, Manuel G.; Zhadan, Galina G.; Shnyrov, Valery L.; Polikarpov, Igor

    Source: Acta Crystallographica F. Unidade: IFSC

    Subjects: PRODUTOS NATURAIS (ESTUDO), ENZIMAS, BIOTECNOLOGIA, PALMEIRAS

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    • ABNT

      TEXTOR, Larissa C. et al. Purification, crystallization and preliminary crystallographic analysis of peroxidase from the palm tree Chamaerops excelsa. Acta Crystallographica F, v. 67, p. 1641-1644, 2011Tradução . . Disponível em: https://doi.org/10.1107/S1744309111039030. Acesso em: 24 maio 2024.

    • APA

      Textor, L. C., Santos, J. C., Cuadrado, N. H., Roig, M. G., Zhadan, G. G., Shnyrov, V. L., & Polikarpov, I. (2011). Purification, crystallization and preliminary crystallographic analysis of peroxidase from the palm tree Chamaerops excelsa. Acta Crystallographica F, 67, 1641-1644. doi:10.1107/S1744309111039030

    • NLM

      Textor LC, Santos JC, Cuadrado NH, Roig MG, Zhadan GG, Shnyrov VL, Polikarpov I. Purification, crystallization and preliminary crystallographic analysis of peroxidase from the palm tree Chamaerops excelsa [Internet]. Acta Crystallographica F. 2011 ; 67 1641-1644.[citado 2024 maio 24 ] Available from: https://doi.org/10.1107/S1744309111039030

    • Vancouver

      Textor LC, Santos JC, Cuadrado NH, Roig MG, Zhadan GG, Shnyrov VL, Polikarpov I. Purification, crystallization and preliminary crystallographic analysis of peroxidase from the palm tree Chamaerops excelsa [Internet]. Acta Crystallographica F. 2011 ; 67 1641-1644.[citado 2024 maio 24 ] Available from: https://doi.org/10.1107/S1744309111039030

  • Artigo de periodico

    Palm peroxidases: the most robust enzymes (2011)

    Cuadrado, Nazaret Hidalgo; Arellano, Juan B.; Calvete, Juan J.; Sanz, Libia; Zhadan, Galina G.; Textor, Larissa C.; Polikarpov, Igor; Bursakov, Sergey; Roig, Manuel G.; Shnyrov, Valery L.

    Source: Current Topics in Biochemical Research. Unidade: IFSC

    Subjects: ENZIMAS (APLICAÇÕES;ESTUDO), PROTEÍNAS, BIOTECNOLOGIA

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      CUADRADO, Nazaret Hidalgo et al. Palm peroxidases: the most robust enzymes. Current Topics in Biochemical Research, v. 13, n. 2, p. 67-79, 2011Tradução . . Disponível em: https://doi.org/10.1021/jp200330z. Acesso em: 24 maio 2024.

    • APA

      Cuadrado, N. H., Arellano, J. B., Calvete, J. J., Sanz, L., Zhadan, G. G., Textor, L. C., et al. (2011). Palm peroxidases: the most robust enzymes. Current Topics in Biochemical Research, 13( 2), 67-79. doi:10.1021/jp200330z

    • NLM

      Cuadrado NH, Arellano JB, Calvete JJ, Sanz L, Zhadan GG, Textor LC, Polikarpov I, Bursakov S, Roig MG, Shnyrov VL. Palm peroxidases: the most robust enzymes [Internet]. Current Topics in Biochemical Research. 2011 ; 13( 2): 67-79.[citado 2024 maio 24 ] Available from: https://doi.org/10.1021/jp200330z

    • Vancouver

      Cuadrado NH, Arellano JB, Calvete JJ, Sanz L, Zhadan GG, Textor LC, Polikarpov I, Bursakov S, Roig MG, Shnyrov VL. Palm peroxidases: the most robust enzymes [Internet]. Current Topics in Biochemical Research. 2011 ; 13( 2): 67-79.[citado 2024 maio 24 ] Available from: https://doi.org/10.1021/jp200330z

  • Artigo de periodico

    Purification, crystallization and preliminary crystallographic analysis of the catalytic domain of the extracellular cellulase CBHI from Trichoderma harzianum (2010)

    Colussi, Francieli; Textor, Larissa C.; Serpa, Viviane; Maeda, Roberto Nobuyuki; Pereira Júnior, Nei; Polikarpov, Igor

    Source: Acta Crystallographica F. Unidade: IFSC

    Subjects: MICROBIOLOGIA (ANÁLISE), BIOTECNOLOGIA, FUNGOS, CELULOSE

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      COLUSSI, Francieli et al. Purification, crystallization and preliminary crystallographic analysis of the catalytic domain of the extracellular cellulase CBHI from Trichoderma harzianum. Acta Crystallographica F, v. 66, p. 1041-1044, 2010Tradução . . Disponível em: https://doi.org/10.1107/S1744309110026886. Acesso em: 24 maio 2024.

    • APA

      Colussi, F., Textor, L. C., Serpa, V., Maeda, R. N., Pereira Júnior, N., & Polikarpov, I. (2010). Purification, crystallization and preliminary crystallographic analysis of the catalytic domain of the extracellular cellulase CBHI from Trichoderma harzianum. Acta Crystallographica F, 66, 1041-1044. doi:10.1107/S1744309110026886

    • NLM

      Colussi F, Textor LC, Serpa V, Maeda RN, Pereira Júnior N, Polikarpov I. Purification, crystallization and preliminary crystallographic analysis of the catalytic domain of the extracellular cellulase CBHI from Trichoderma harzianum [Internet]. Acta Crystallographica F. 2010 ; 66 1041-1044.[citado 2024 maio 24 ] Available from: https://doi.org/10.1107/S1744309110026886

    • Vancouver

      Colussi F, Textor LC, Serpa V, Maeda RN, Pereira Júnior N, Polikarpov I. Purification, crystallization and preliminary crystallographic analysis of the catalytic domain of the extracellular cellulase CBHI from Trichoderma harzianum [Internet]. Acta Crystallographica F. 2010 ; 66 1041-1044.[citado 2024 maio 24 ] Available from: https://doi.org/10.1107/S1744309110026886
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