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  • Source: Journal of Molecular Modeling. Unidade: IFSC

    Subjects: XANTHOMONAS, ELASTICIDADE, CATÁLISE

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      SKAF, Munir Salomão e POLIKARPOV, Igor e STANKOVIC, Ivana M. A linker of the proline-threonine repeatingmotif sequence is bimodal. Journal of Molecular Modeling, v. 26, n. 8, p. 178-1-178-7, 2020Tradução . . Disponível em: https://doi.org/10.1007/s00894-020-04434-0. Acesso em: 15 jun. 2024.
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      Skaf, M. S., Polikarpov, I., & Stankovic, I. M. (2020). A linker of the proline-threonine repeatingmotif sequence is bimodal. Journal of Molecular Modeling, 26( 8), 178-1-178-7. doi:10.1007/s00894-020-04434-0
    • NLM

      Skaf MS, Polikarpov I, Stankovic IM. A linker of the proline-threonine repeatingmotif sequence is bimodal [Internet]. Journal of Molecular Modeling. 2020 ; 26( 8): 178-1-178-7.[citado 2024 jun. 15 ] Available from: https://doi.org/10.1007/s00894-020-04434-0
    • Vancouver

      Skaf MS, Polikarpov I, Stankovic IM. A linker of the proline-threonine repeatingmotif sequence is bimodal [Internet]. Journal of Molecular Modeling. 2020 ; 26( 8): 178-1-178-7.[citado 2024 jun. 15 ] Available from: https://doi.org/10.1007/s00894-020-04434-0
  • Source: Industrial Crops and Products. Unidades: IFSC, BIOENERGIA

    Subjects: BIOCOMBUSTÍVEIS, CATÁLISE, CAVACOS, CELULOSE DE MADEIRA, ETANOL, EUCALIPTO

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      ESPÍRITO SANTO, Melissa Cristina do et al. Physical techniques shed light on the differences in sugarcane bagasse structure subjected to steam explosion pretreatments at equivalent combined severity factors. Industrial Crops and Products, v. 158, p. 113003-1-113003-10, 2020Tradução . . Disponível em: https://doi.org/10.1016/j.indcrop.2020.113003. Acesso em: 15 jun. 2024.
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      Espírito Santo, M. C. do, Fockink, D. H., Pellegrini, V. de O. A., Guimarães, F. E. G., Azevêdo, E. R. de, Ramos, L. P., & Polikarpov, I. (2020). Physical techniques shed light on the differences in sugarcane bagasse structure subjected to steam explosion pretreatments at equivalent combined severity factors. Industrial Crops and Products, 158, 113003-1-113003-10. doi:10.1016/j.indcrop.2020.113003
    • NLM

      Espírito Santo MC do, Fockink DH, Pellegrini V de OA, Guimarães FEG, Azevêdo ER de, Ramos LP, Polikarpov I. Physical techniques shed light on the differences in sugarcane bagasse structure subjected to steam explosion pretreatments at equivalent combined severity factors [Internet]. Industrial Crops and Products. 2020 ; 158 113003-1-113003-10.[citado 2024 jun. 15 ] Available from: https://doi.org/10.1016/j.indcrop.2020.113003
    • Vancouver

      Espírito Santo MC do, Fockink DH, Pellegrini V de OA, Guimarães FEG, Azevêdo ER de, Ramos LP, Polikarpov I. Physical techniques shed light on the differences in sugarcane bagasse structure subjected to steam explosion pretreatments at equivalent combined severity factors [Internet]. Industrial Crops and Products. 2020 ; 158 113003-1-113003-10.[citado 2024 jun. 15 ] Available from: https://doi.org/10.1016/j.indcrop.2020.113003
  • Source: Proteins. Unidade: IFSC

    Subjects: PAPILLOMAVIRUS, BOVINOS, PROTEÍNAS

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      LEROY, Ludmila et al. The structure of the extended E2 DNA-binding domain of the bovine papillomavirus-1. Proteins, v. 88, n. Ja 2020, p. 106-112, 2020Tradução . . Disponível em: https://doi.org/10.1002/prot.25773. Acesso em: 15 jun. 2024.
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      Leroy, L., Barbosa, J. A. R. G., Prat-Gay, G. de, Polikarpov, I., & Pinheiro, C. B. (2020). The structure of the extended E2 DNA-binding domain of the bovine papillomavirus-1. Proteins, 88( Ja 2020), 106-112. doi:10.1002/prot.25773
    • NLM

      Leroy L, Barbosa JARG, Prat-Gay G de, Polikarpov I, Pinheiro CB. The structure of the extended E2 DNA-binding domain of the bovine papillomavirus-1 [Internet]. Proteins. 2020 ; 88( Ja 2020): 106-112.[citado 2024 jun. 15 ] Available from: https://doi.org/10.1002/prot.25773
    • Vancouver

      Leroy L, Barbosa JARG, Prat-Gay G de, Polikarpov I, Pinheiro CB. The structure of the extended E2 DNA-binding domain of the bovine papillomavirus-1 [Internet]. Proteins. 2020 ; 88( Ja 2020): 106-112.[citado 2024 jun. 15 ] Available from: https://doi.org/10.1002/prot.25773
  • Source: Energy and Fuels. Unidades: IFSC, BIOENERGIA

    Subjects: BIOCOMBUSTÍVEIS, CATÁLISE, CAVACOS, CELULOSE DE MADEIRA, ETANOL, EUCALIPTO

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      CHIARELLO, Luana M. et al. Characterization of pretreated fractions and cellulosic ethanol production from steam-exploded Eucalyptus urograndis. Energy and Fuels, v. 34, n. Ja 2020, p. 535-545, 2020Tradução . . Disponível em: https://doi.org/10.1021/acs.energyfuels.9b03405. Acesso em: 15 jun. 2024.
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      Chiarello, L. M., Ramos, C. E. A., Santos, L. F. F., Silveira, M. H. L., Zaccaron, S., Schiehser, S., et al. (2020). Characterization of pretreated fractions and cellulosic ethanol production from steam-exploded Eucalyptus urograndis. Energy and Fuels, 34( Ja 2020), 535-545. doi:10.1021/acs.energyfuels.9b03405
    • NLM

      Chiarello LM, Ramos CEA, Santos LFF, Silveira MHL, Zaccaron S, Schiehser S, Espírito Santo MC do, Guimarães FEG, Azevêdo ER de, Polikarpov I, Potthast A, Ramos LP. Characterization of pretreated fractions and cellulosic ethanol production from steam-exploded Eucalyptus urograndis [Internet]. Energy and Fuels. 2020 ; 34( Ja 2020): 535-545.[citado 2024 jun. 15 ] Available from: https://doi.org/10.1021/acs.energyfuels.9b03405
    • Vancouver

      Chiarello LM, Ramos CEA, Santos LFF, Silveira MHL, Zaccaron S, Schiehser S, Espírito Santo MC do, Guimarães FEG, Azevêdo ER de, Polikarpov I, Potthast A, Ramos LP. Characterization of pretreated fractions and cellulosic ethanol production from steam-exploded Eucalyptus urograndis [Internet]. Energy and Fuels. 2020 ; 34( Ja 2020): 535-545.[citado 2024 jun. 15 ] Available from: https://doi.org/10.1021/acs.energyfuels.9b03405
  • Source: Biochimie. Unidade: IFSC

    Subjects: ENZIMAS, BIOTECNOLOGIA, HIDRÓLISE

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      KADOWAKI, Marco Antonio Seiki e POLIKARPOV, Igor. Structural insights into the hydrolysis pattern and molecular dynamics simulations of GH45 subfamily a endoglucanase from Neurospora crassa OR74A. Biochimie, v. 165, p. 275-284, 2019Tradução . . Disponível em: https://doi.org/10.1016/j.biochi.2019.08.016. Acesso em: 15 jun. 2024.
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      Kadowaki, M. A. S., & Polikarpov, I. (2019). Structural insights into the hydrolysis pattern and molecular dynamics simulations of GH45 subfamily a endoglucanase from Neurospora crassa OR74A. Biochimie, 165, 275-284. doi:10.1016/j.biochi.2019.08.016
    • NLM

      Kadowaki MAS, Polikarpov I. Structural insights into the hydrolysis pattern and molecular dynamics simulations of GH45 subfamily a endoglucanase from Neurospora crassa OR74A [Internet]. Biochimie. 2019 ; 165 275-284.[citado 2024 jun. 15 ] Available from: https://doi.org/10.1016/j.biochi.2019.08.016
    • Vancouver

      Kadowaki MAS, Polikarpov I. Structural insights into the hydrolysis pattern and molecular dynamics simulations of GH45 subfamily a endoglucanase from Neurospora crassa OR74A [Internet]. Biochimie. 2019 ; 165 275-284.[citado 2024 jun. 15 ] Available from: https://doi.org/10.1016/j.biochi.2019.08.016
  • Source: Protein Science. Unidades: IF, IFSC

    Subjects: PESO MOLECULAR, PROTEÍNAS, ESPALHAMENTO DE RAIOS X A BAIXOS ÂNGULOS

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      PIIADOV, Vassili et al. SAXSMoW 2.0: online calculator of the molecular weight of proteins in dilute solution from experimental SAXS data measured on a relative scale. Protein Science, v. 28, n. 2, p. 454-463, 2019Tradução . . Disponível em: https://doi.org/10.1002/pro.3528. Acesso em: 15 jun. 2024.
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      Piiadov, V., Araújo, E. A. de, Oliveira Neto, M., Craievich, A. F., & Polikarpov, I. (2019). SAXSMoW 2.0: online calculator of the molecular weight of proteins in dilute solution from experimental SAXS data measured on a relative scale. Protein Science, 28( 2), 454-463. doi:10.1002/pro.3528
    • NLM

      Piiadov V, Araújo EA de, Oliveira Neto M, Craievich AF, Polikarpov I. SAXSMoW 2.0: online calculator of the molecular weight of proteins in dilute solution from experimental SAXS data measured on a relative scale [Internet]. Protein Science. 2019 ; 28( 2): 454-463.[citado 2024 jun. 15 ] Available from: https://doi.org/10.1002/pro.3528
    • Vancouver

      Piiadov V, Araújo EA de, Oliveira Neto M, Craievich AF, Polikarpov I. SAXSMoW 2.0: online calculator of the molecular weight of proteins in dilute solution from experimental SAXS data measured on a relative scale [Internet]. Protein Science. 2019 ; 28( 2): 454-463.[citado 2024 jun. 15 ] Available from: https://doi.org/10.1002/pro.3528
  • Source: Enzyme and Microbial Technology. Unidades: IFSC, EEL

    Subjects: CANA-DE-AÇÚCAR, BAGAÇOS, HIDRÓLISE

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      BERTO, Gabriela Leila et al. Functional characterization and comparative analysis of two heterologous endoglucanases from diverging subfamilies of glycosyl hydrolase family 45. Enzyme and Microbial Technology, v. 120, n. Ja 2019, p. 23-35, 2019Tradução . . Disponível em: https://doi.org/10.1016/j.enzmictec.2018.09.005. Acesso em: 15 jun. 2024.
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      Berto, G. L., Velasco, J., Ribeiro, C. T. C., Zanphorlin, L. M., Domingues, M. N., Murakami, M. T., et al. (2019). Functional characterization and comparative analysis of two heterologous endoglucanases from diverging subfamilies of glycosyl hydrolase family 45. Enzyme and Microbial Technology, 120( Ja 2019), 23-35. doi:10.1016/j.enzmictec.2018.09.005
    • NLM

      Berto GL, Velasco J, Ribeiro CTC, Zanphorlin LM, Domingues MN, Murakami MT, Polikarpov I, Oliveira LC de, Ferraz A, Segato F. Functional characterization and comparative analysis of two heterologous endoglucanases from diverging subfamilies of glycosyl hydrolase family 45 [Internet]. Enzyme and Microbial Technology. 2019 ; 120( Ja 2019): 23-35.[citado 2024 jun. 15 ] Available from: https://doi.org/10.1016/j.enzmictec.2018.09.005
    • Vancouver

      Berto GL, Velasco J, Ribeiro CTC, Zanphorlin LM, Domingues MN, Murakami MT, Polikarpov I, Oliveira LC de, Ferraz A, Segato F. Functional characterization and comparative analysis of two heterologous endoglucanases from diverging subfamilies of glycosyl hydrolase family 45 [Internet]. Enzyme and Microbial Technology. 2019 ; 120( Ja 2019): 23-35.[citado 2024 jun. 15 ] Available from: https://doi.org/10.1016/j.enzmictec.2018.09.005
  • Source: Process Biochemistry. Unidade: IFSC

    Subjects: ENZIMAS, BIOCOMBUSTÍVEIS, ETANOL

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      HANS, Meenu et al. A review on bioprocessing of paddy straw to ethanol using simultaneous saccharification and fermentation. Process Biochemistry, v. 85, p. 125-134, 2019Tradução . . Disponível em: https://doi.org/10.1016/j.procbio.2019.06.019. Acesso em: 15 jun. 2024.
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      Hans, M., Kumar, S., Chandel, A. K., & Polikarpov, I. (2019). A review on bioprocessing of paddy straw to ethanol using simultaneous saccharification and fermentation. Process Biochemistry, 85, 125-134. doi:10.1016/j.procbio.2019.06.019
    • NLM

      Hans M, Kumar S, Chandel AK, Polikarpov I. A review on bioprocessing of paddy straw to ethanol using simultaneous saccharification and fermentation [Internet]. Process Biochemistry. 2019 ; 85 125-134.[citado 2024 jun. 15 ] Available from: https://doi.org/10.1016/j.procbio.2019.06.019
    • Vancouver

      Hans M, Kumar S, Chandel AK, Polikarpov I. A review on bioprocessing of paddy straw to ethanol using simultaneous saccharification and fermentation [Internet]. Process Biochemistry. 2019 ; 85 125-134.[citado 2024 jun. 15 ] Available from: https://doi.org/10.1016/j.procbio.2019.06.019
  • Source: Applied Microbiology and Biotechnology. Unidade: IFSC

    Subjects: CANA-DE-AÇÚCAR, BAGAÇOS, HIDRÓLISE

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      ARAÚJO, Evandro Ares de e OLIVEIRA NETO, Mário de e POLIKARPOV, Igor. Biochemical characterization and low-resolution SAXS structure of two-domain endoglucanase BlCel9 from Bacillus licheniformis. Applied Microbiology and Biotechnology, v. 103, n. 3, p. 1275-1285, 2019Tradução . . Disponível em: https://doi.org/10.1007/s00253-018-9508-1. Acesso em: 15 jun. 2024.
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      Araújo, E. A. de, Oliveira Neto, M. de, & Polikarpov, I. (2019). Biochemical characterization and low-resolution SAXS structure of two-domain endoglucanase BlCel9 from Bacillus licheniformis. Applied Microbiology and Biotechnology, 103( 3), 1275-1285. doi:10.1007/s00253-018-9508-1
    • NLM

      Araújo EA de, Oliveira Neto M de, Polikarpov I. Biochemical characterization and low-resolution SAXS structure of two-domain endoglucanase BlCel9 from Bacillus licheniformis [Internet]. Applied Microbiology and Biotechnology. 2019 ; 103( 3): 1275-1285.[citado 2024 jun. 15 ] Available from: https://doi.org/10.1007/s00253-018-9508-1
    • Vancouver

      Araújo EA de, Oliveira Neto M de, Polikarpov I. Biochemical characterization and low-resolution SAXS structure of two-domain endoglucanase BlCel9 from Bacillus licheniformis [Internet]. Applied Microbiology and Biotechnology. 2019 ; 103( 3): 1275-1285.[citado 2024 jun. 15 ] Available from: https://doi.org/10.1007/s00253-018-9508-1
  • Source: Journal of Applied Microbiology. Unidade: IFSC

    Subjects: POLÍMEROS (MATERIAIS), BIOCOMBUSTÍVEIS

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      VIEIRA, F. R. et al. Exploring oyster mushroom (Pleurotus ostreatus) substrate preparation by varying phase I composting time: changes in bacterial communities and physicochemical composition of biomass impacting mushroom yields. Journal of Applied Microbiology, v. 126, n. 3, p. 931-944, 2019Tradução . . Disponível em: https://doi.org/10.1111/jam.14168. Acesso em: 15 jun. 2024.
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      Vieira, F. R., Pecchia, J. A., Segato, F., & Polikarpov, I. (2019). Exploring oyster mushroom (Pleurotus ostreatus) substrate preparation by varying phase I composting time: changes in bacterial communities and physicochemical composition of biomass impacting mushroom yields. Journal of Applied Microbiology, 126( 3), 931-944. doi:10.1111/jam.14168
    • NLM

      Vieira FR, Pecchia JA, Segato F, Polikarpov I. Exploring oyster mushroom (Pleurotus ostreatus) substrate preparation by varying phase I composting time: changes in bacterial communities and physicochemical composition of biomass impacting mushroom yields [Internet]. Journal of Applied Microbiology. 2019 ; 126( 3): 931-944.[citado 2024 jun. 15 ] Available from: https://doi.org/10.1111/jam.14168
    • Vancouver

      Vieira FR, Pecchia JA, Segato F, Polikarpov I. Exploring oyster mushroom (Pleurotus ostreatus) substrate preparation by varying phase I composting time: changes in bacterial communities and physicochemical composition of biomass impacting mushroom yields [Internet]. Journal of Applied Microbiology. 2019 ; 126( 3): 931-944.[citado 2024 jun. 15 ] Available from: https://doi.org/10.1111/jam.14168
  • Source: Livro de resumos. Conference titles: Reunião da Associação Brasileira de Cristalografia - ABCr. Unidade: IFSC

    Subjects: ESPALHAMENTO DE RAIOS X A BAIXOS ÂNGULOS, ENZIMAS HIDROLÍTICAS, MACROMOLÉCULA

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      OLIVEIRA NETO, M. et al. Glycoside hydrolases molecular characterization: a SAXS approach. 2019, Anais.. Campinas: Associação Brasileira de Cristalografia - ABCr, 2019. Disponível em: http://www.abcristalografia.org.br/evento.php?cod=24ABCr&tab=files. Acesso em: 15 jun. 2024.
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      Oliveira Neto, M., Gandin, C. A., Garcia, W., Polikarpov, I., & Squina, F. M. (2019). Glycoside hydrolases molecular characterization: a SAXS approach. In Livro de resumos. Campinas: Associação Brasileira de Cristalografia - ABCr. Recuperado de http://www.abcristalografia.org.br/evento.php?cod=24ABCr&tab=files
    • NLM

      Oliveira Neto M, Gandin CA, Garcia W, Polikarpov I, Squina FM. Glycoside hydrolases molecular characterization: a SAXS approach [Internet]. Livro de resumos. 2019 ;[citado 2024 jun. 15 ] Available from: http://www.abcristalografia.org.br/evento.php?cod=24ABCr&tab=files
    • Vancouver

      Oliveira Neto M, Gandin CA, Garcia W, Polikarpov I, Squina FM. Glycoside hydrolases molecular characterization: a SAXS approach [Internet]. Livro de resumos. 2019 ;[citado 2024 jun. 15 ] Available from: http://www.abcristalografia.org.br/evento.php?cod=24ABCr&tab=files
  • Source: International Journal of Biological Macromolecules. Unidades: IQSC, IFSC

    Assunto: PROTEÍNAS

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      MINARI, Karine et al. Thermodynamic analysis of interactions of the Hsp90 with adenosine nucleotides: a comparative perspective. International Journal of Biological Macromolecules, v. 130, p. 125-138, 2019Tradução . . Disponível em: https://doi.org/10.1016/j.ijbiomac.2019.02.116. Acesso em: 15 jun. 2024.
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      Minari, K., Azevedo, É. C. de, Kiraly, V. T. R., Batista, F. A. H., Moraes, F. R., Melo, F. A. de, et al. (2019). Thermodynamic analysis of interactions of the Hsp90 with adenosine nucleotides: a comparative perspective. International Journal of Biological Macromolecules, 130, 125-138. doi:10.1016/j.ijbiomac.2019.02.116
    • NLM

      Minari K, Azevedo ÉC de, Kiraly VTR, Batista FAH, Moraes FR, Melo FA de, Nascimento AS, Gava LM, Ramos CHI, Borges JC. Thermodynamic analysis of interactions of the Hsp90 with adenosine nucleotides: a comparative perspective [Internet]. International Journal of Biological Macromolecules. 2019 ;130 125-138.[citado 2024 jun. 15 ] Available from: https://doi.org/10.1016/j.ijbiomac.2019.02.116
    • Vancouver

      Minari K, Azevedo ÉC de, Kiraly VTR, Batista FAH, Moraes FR, Melo FA de, Nascimento AS, Gava LM, Ramos CHI, Borges JC. Thermodynamic analysis of interactions of the Hsp90 with adenosine nucleotides: a comparative perspective [Internet]. International Journal of Biological Macromolecules. 2019 ;130 125-138.[citado 2024 jun. 15 ] Available from: https://doi.org/10.1016/j.ijbiomac.2019.02.116
  • Source: PLOS ONE. Unidades: FFCLRP, IFSC

    Subjects: ENZIMAS, RECEPTORES, CRISTALOGRAFIA ESTRUTURAL

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      KADOWAKI, Marco A. et al. Functional characterization of a lytic polysaccharide monooxygenase from the thermophilic fungus Myceliophthora thermophila. PLOS ONE, v. 13, n. 8, p. e0202148-1- e0202148-16, 2018Tradução . . Disponível em: https://doi.org/10.1371/journal.pone.0202148. Acesso em: 15 jun. 2024.
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      Kadowaki, M. A., Várnai, A., Jameson, J. -K., Leite, A. E. T., Costa Filho, A. J. da, Kumagai, P. S., et al. (2018). Functional characterization of a lytic polysaccharide monooxygenase from the thermophilic fungus Myceliophthora thermophila. PLOS ONE, 13( 8), e0202148-1- e0202148-16. doi:10.1371/journal.pone.0202148
    • NLM

      Kadowaki MA, Várnai A, Jameson J-K, Leite AET, Costa Filho AJ da, Kumagai PS, Prade RA, Polikarpov I, Vincent GHE. Functional characterization of a lytic polysaccharide monooxygenase from the thermophilic fungus Myceliophthora thermophila [Internet]. PLOS ONE. 2018 ; 13( 8): e0202148-1- e0202148-16.[citado 2024 jun. 15 ] Available from: https://doi.org/10.1371/journal.pone.0202148
    • Vancouver

      Kadowaki MA, Várnai A, Jameson J-K, Leite AET, Costa Filho AJ da, Kumagai PS, Prade RA, Polikarpov I, Vincent GHE. Functional characterization of a lytic polysaccharide monooxygenase from the thermophilic fungus Myceliophthora thermophila [Internet]. PLOS ONE. 2018 ; 13( 8): e0202148-1- e0202148-16.[citado 2024 jun. 15 ] Available from: https://doi.org/10.1371/journal.pone.0202148
  • Source: Abstract book. Conference titles: Annual Meeting of the Brazilian Society for Biochemistry and Molecular Biology - SBBq. Unidade: IFSC

    Subjects: MACROMOLÉCULA, SIMULAÇÃO DE SISTEMAS

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      SOUSA, Stheffany e NASCIMENTO, Alessandro Silva. Comparative study between Gaussian-accelerated molecular dynamics (GaMD) and adaptively biased molecular dynamics (ABMD) for enhanced sampling and free energy evaluation. 2018, Anais.. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular - SBBq, 2018. Disponível em: http://www.sbbq.org.br/reuniao/2018/livro_resumos_2018.pdf. Acesso em: 15 jun. 2024.
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      Sousa, S., & Nascimento, A. S. (2018). Comparative study between Gaussian-accelerated molecular dynamics (GaMD) and adaptively biased molecular dynamics (ABMD) for enhanced sampling and free energy evaluation. In Abstract book. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular - SBBq. Recuperado de http://www.sbbq.org.br/reuniao/2018/livro_resumos_2018.pdf
    • NLM

      Sousa S, Nascimento AS. Comparative study between Gaussian-accelerated molecular dynamics (GaMD) and adaptively biased molecular dynamics (ABMD) for enhanced sampling and free energy evaluation [Internet]. Abstract book. 2018 ;[citado 2024 jun. 15 ] Available from: http://www.sbbq.org.br/reuniao/2018/livro_resumos_2018.pdf
    • Vancouver

      Sousa S, Nascimento AS. Comparative study between Gaussian-accelerated molecular dynamics (GaMD) and adaptively biased molecular dynamics (ABMD) for enhanced sampling and free energy evaluation [Internet]. Abstract book. 2018 ;[citado 2024 jun. 15 ] Available from: http://www.sbbq.org.br/reuniao/2018/livro_resumos_2018.pdf
  • Source: Abstract book. Conference titles: Annual Meeting of the Brazilian Society for Biochemistry and Molecular Biology - SBBq. Unidade: IFSC

    Subjects: MÉTODO DE MONTE CARLO, TRANSCRIÇÃO GÊNICA, MOLÉCULA (INTERAÇÃO)

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      NOGUEIRA, Victor Henrique Rabesquine e NASCIMENTO, Alessandro Silva. Monte Carlo simulations for calculating binding free energy in biological systems. 2018, Anais.. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular - SBBq, 2018. Disponível em: http://www.sbbq.org.br/reuniao/2018/livro_resumos_2018.pdf. Acesso em: 15 jun. 2024.
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      Nogueira, V. H. R., & Nascimento, A. S. (2018). Monte Carlo simulations for calculating binding free energy in biological systems. In Abstract book. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular - SBBq. Recuperado de http://www.sbbq.org.br/reuniao/2018/livro_resumos_2018.pdf
    • NLM

      Nogueira VHR, Nascimento AS. Monte Carlo simulations for calculating binding free energy in biological systems [Internet]. Abstract book. 2018 ;[citado 2024 jun. 15 ] Available from: http://www.sbbq.org.br/reuniao/2018/livro_resumos_2018.pdf
    • Vancouver

      Nogueira VHR, Nascimento AS. Monte Carlo simulations for calculating binding free energy in biological systems [Internet]. Abstract book. 2018 ;[citado 2024 jun. 15 ] Available from: http://www.sbbq.org.br/reuniao/2018/livro_resumos_2018.pdf
  • Source: Abstract book. Conference titles: Annual Meeting of the Brazilian Society for Biochemistry and Molecular Biology - SBBq. Unidade: IFSC

    Subjects: CELULOSE, ENZIMAS

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      KADOWAKI, Marco Antonio Seiki et al. Biochemical and structural insights into the catalytic mechanism and molecular dynamics of a thermostable cellobiohydrolase from Myceliophthora thermophila: an increase in cellulolytic degradation by accellerase. 2018, Anais.. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular - SBBq, 2018. Disponível em: http://www.sbbq.org.br/reuniao/2018/livro_resumos_2018.pdf. Acesso em: 15 jun. 2024.
    • APA

      Kadowaki, M. A. S., Higasi, P., Godoy, M. O. de, & Polikarpov, I. (2018). Biochemical and structural insights into the catalytic mechanism and molecular dynamics of a thermostable cellobiohydrolase from Myceliophthora thermophila: an increase in cellulolytic degradation by accellerase. In Abstract book. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular - SBBq. Recuperado de http://www.sbbq.org.br/reuniao/2018/livro_resumos_2018.pdf
    • NLM

      Kadowaki MAS, Higasi P, Godoy MO de, Polikarpov I. Biochemical and structural insights into the catalytic mechanism and molecular dynamics of a thermostable cellobiohydrolase from Myceliophthora thermophila: an increase in cellulolytic degradation by accellerase [Internet]. Abstract book. 2018 ;[citado 2024 jun. 15 ] Available from: http://www.sbbq.org.br/reuniao/2018/livro_resumos_2018.pdf
    • Vancouver

      Kadowaki MAS, Higasi P, Godoy MO de, Polikarpov I. Biochemical and structural insights into the catalytic mechanism and molecular dynamics of a thermostable cellobiohydrolase from Myceliophthora thermophila: an increase in cellulolytic degradation by accellerase [Internet]. Abstract book. 2018 ;[citado 2024 jun. 15 ] Available from: http://www.sbbq.org.br/reuniao/2018/livro_resumos_2018.pdf
  • Source: International Journal of Biological Macromolecules. Unidade: IFSC

    Subjects: ENZIMAS, BIOTECNOLOGIA, HIDRÓLISE

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      NAKAMURA, Aline M. et al. Low-resolution envelope, biophysical analysis and biochemical characterization of a short-chain specific and halotolerant carboxylesterase from Bacillus licheniformis. International Journal of Biological Macromolecules, v. 120, p. 1893-1905, 2018Tradução . . Disponível em: https://doi.org/10.1016/j.ijbiomac.2018.10.003. Acesso em: 15 jun. 2024.
    • APA

      Nakamura, A. M., Kadowaki, M. A. S., Godoy, A., Nascimento, A. S., & Polikarpov, I. (2018). Low-resolution envelope, biophysical analysis and biochemical characterization of a short-chain specific and halotolerant carboxylesterase from Bacillus licheniformis. International Journal of Biological Macromolecules, 120, 1893-1905. doi:10.1016/j.ijbiomac.2018.10.003
    • NLM

      Nakamura AM, Kadowaki MAS, Godoy A, Nascimento AS, Polikarpov I. Low-resolution envelope, biophysical analysis and biochemical characterization of a short-chain specific and halotolerant carboxylesterase from Bacillus licheniformis [Internet]. International Journal of Biological Macromolecules. 2018 ; 120 1893-1905.[citado 2024 jun. 15 ] Available from: https://doi.org/10.1016/j.ijbiomac.2018.10.003
    • Vancouver

      Nakamura AM, Kadowaki MAS, Godoy A, Nascimento AS, Polikarpov I. Low-resolution envelope, biophysical analysis and biochemical characterization of a short-chain specific and halotolerant carboxylesterase from Bacillus licheniformis [Internet]. International Journal of Biological Macromolecules. 2018 ; 120 1893-1905.[citado 2024 jun. 15 ] Available from: https://doi.org/10.1016/j.ijbiomac.2018.10.003
  • Source: Catalysts. Unidades: FFCLRP, IFSC

    Subjects: ENZIMAS, FUNGOS TERMÓFILOS, RESSONÂNCIA PARAMAGNÉTICA ELETRÔNICA

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      KADOWAKI, Marco Antonio Seiki et al. Characterization of a new glyoxal oxidase from the thermophilic fungus Myceliophthora thermophila M77: hydrogen peroxide production retained in 5-hydroxymethylfurfural oxidation. Catalysts, v. 8, n. 10, p. 476-1-476-15, 2018Tradução . . Disponível em: https://doi.org/10.3390/catal8100476. Acesso em: 15 jun. 2024.
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      Kadowaki, M. A. S., Godoy, M. O. de, Kumagai, P. S., Costa Filho, A. J. da, Mort, A., Prade, R. A., & Polikarpov, I. (2018). Characterization of a new glyoxal oxidase from the thermophilic fungus Myceliophthora thermophila M77: hydrogen peroxide production retained in 5-hydroxymethylfurfural oxidation. Catalysts, 8( 10), 476-1-476-15. doi:10.3390/catal8100476
    • NLM

      Kadowaki MAS, Godoy MO de, Kumagai PS, Costa Filho AJ da, Mort A, Prade RA, Polikarpov I. Characterization of a new glyoxal oxidase from the thermophilic fungus Myceliophthora thermophila M77: hydrogen peroxide production retained in 5-hydroxymethylfurfural oxidation [Internet]. Catalysts. 2018 ; 8( 10): 476-1-476-15.[citado 2024 jun. 15 ] Available from: https://doi.org/10.3390/catal8100476
    • Vancouver

      Kadowaki MAS, Godoy MO de, Kumagai PS, Costa Filho AJ da, Mort A, Prade RA, Polikarpov I. Characterization of a new glyoxal oxidase from the thermophilic fungus Myceliophthora thermophila M77: hydrogen peroxide production retained in 5-hydroxymethylfurfural oxidation [Internet]. Catalysts. 2018 ; 8( 10): 476-1-476-15.[citado 2024 jun. 15 ] Available from: https://doi.org/10.3390/catal8100476
  • Source: Biochimie. Unidade: IFSC

    Subjects: PEROXIDASE, PALMEIRAS, CRISTALOGRAFIA

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      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: 15 jun. 2024.
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      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 jun. 15 ] 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 jun. 15 ] Available from: https://doi.org/10.1016/j.biochi.2015.01.014
  • Source: Molecular Biotechnology. Unidade: IFSC

    Subjects: BIOMASSA, ENZIMAS HIDROLÍTICAS

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      KADOWAKI, Marco Antonio Seiki et al. Functional characterization and low-resolution structure of an endoglucanase Cel45A from the filamentous fungus Neurospora crassa OR74A: thermostable enzyme with high activity toward lichenan and b-glucan. Molecular Biotechnology, v. 57, n. 6, p. 574-588, 2015Tradução . . Disponível em: https://doi.org/10.1007/s12033-015-9851-8. Acesso em: 15 jun. 2024.
    • APA

      Kadowaki, M. A. S., Camilo, C. M., Muniz, A. B., & Polikarpov, I. (2015). Functional characterization and low-resolution structure of an endoglucanase Cel45A from the filamentous fungus Neurospora crassa OR74A: thermostable enzyme with high activity toward lichenan and b-glucan. Molecular Biotechnology, 57( 6), 574-588. doi:10.1007/s12033-015-9851-8
    • NLM

      Kadowaki MAS, Camilo CM, Muniz AB, Polikarpov I. Functional characterization and low-resolution structure of an endoglucanase Cel45A from the filamentous fungus Neurospora crassa OR74A: thermostable enzyme with high activity toward lichenan and b-glucan [Internet]. Molecular Biotechnology. 2015 ; 57( 6): 574-588.[citado 2024 jun. 15 ] Available from: https://doi.org/10.1007/s12033-015-9851-8
    • Vancouver

      Kadowaki MAS, Camilo CM, Muniz AB, Polikarpov I. Functional characterization and low-resolution structure of an endoglucanase Cel45A from the filamentous fungus Neurospora crassa OR74A: thermostable enzyme with high activity toward lichenan and b-glucan [Internet]. Molecular Biotechnology. 2015 ; 57( 6): 574-588.[citado 2024 jun. 15 ] Available from: https://doi.org/10.1007/s12033-015-9851-8

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