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PEIXOTO, Guilherme et al. Acidogenesis of pentose liquor to produce biohydrogen and organic acids integrated with 1G-2G ethanol production in sugarcane biorefineries. Waste, v. 1, n. 3, p. 672-688, 2023Tradução . . Disponível em: https://doi.org/10.3390/waste1030040. Acesso em: 10 nov. 2024.
APA
Peixoto, G., Mockaitis, G., Moreira, W. K., Lima, D. M. F., Coral, M. A. de L., Ferreira, F. V., et al. (2023). Acidogenesis of pentose liquor to produce biohydrogen and organic acids integrated with 1G-2G ethanol production in sugarcane biorefineries. Waste, 1( 3), 672-688. doi:10.3390/waste1030040
NLM
Peixoto G, Mockaitis G, Moreira WK, Lima DMF, Coral MA de L, Ferreira FV, Fuess LT, Polikarpov I, Zaiat M. Acidogenesis of pentose liquor to produce biohydrogen and organic acids integrated with 1G-2G ethanol production in sugarcane biorefineries [Internet]. Waste. 2023 ; 1( 3): 672-688.[citado 2024 nov. 10 ] Available from: https://doi.org/10.3390/waste1030040
Vancouver
Peixoto G, Mockaitis G, Moreira WK, Lima DMF, Coral MA de L, Ferreira FV, Fuess LT, Polikarpov I, Zaiat M. Acidogenesis of pentose liquor to produce biohydrogen and organic acids integrated with 1G-2G ethanol production in sugarcane biorefineries [Internet]. Waste. 2023 ; 1( 3): 672-688.[citado 2024 nov. 10 ] Available from: https://doi.org/10.3390/waste1030040
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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: 10 nov. 2024.
APA
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 nov. 10 ] 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 nov. 10 ] Available from: https://doi.org/10.3390/catal8100476
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MIOTTO, Lis S. et al. SAXS studies of the endoglucanase cel12A from Gloeophyllum trabeum show its monomeric structure and reveal the influence of temperature on the structural stability of the enzyme. Materials, v. 7, n. 7, p. 5202-5211, 2014Tradução . . Disponível em: https://doi.org/10.3390/ma7075202. Acesso em: 10 nov. 2024.
APA
Miotto, L. S., Reis, C. V., Oliveira Neto, M. de, & Polikarpov, I. (2014). SAXS studies of the endoglucanase cel12A from Gloeophyllum trabeum show its monomeric structure and reveal the influence of temperature on the structural stability of the enzyme. Materials, 7( 7), 5202-5211. doi:10.3390/ma7075202
NLM
Miotto LS, Reis CV, Oliveira Neto M de, Polikarpov I. SAXS studies of the endoglucanase cel12A from Gloeophyllum trabeum show its monomeric structure and reveal the influence of temperature on the structural stability of the enzyme [Internet]. Materials. 2014 ; 7( 7): 5202-5211.[citado 2024 nov. 10 ] Available from: https://doi.org/10.3390/ma7075202
Vancouver
Miotto LS, Reis CV, Oliveira Neto M de, Polikarpov I. SAXS studies of the endoglucanase cel12A from Gloeophyllum trabeum show its monomeric structure and reveal the influence of temperature on the structural stability of the enzyme [Internet]. Materials. 2014 ; 7( 7): 5202-5211.[citado 2024 nov. 10 ] Available from: https://doi.org/10.3390/ma7075202
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SANT'ANNA, Ricardo O. et al. Inhibition of human transthyretin aggregation by non-steroidal anti-inflammatory compounds: a structural and thermodynamic analysis. International Journal of Molecular Sciences, v. 14, n. 3, p. 5284-5311, 2013Tradução . . Disponível em: https://doi.org/10.3390/ijms14035284. Acesso em: 10 nov. 2024.
APA
Sant'Anna, R. O., Braga, C. A., Polikarpov, I., Ventura, S., Lima, L. M. T. R., & Foguel, D. (2013). Inhibition of human transthyretin aggregation by non-steroidal anti-inflammatory compounds: a structural and thermodynamic analysis. International Journal of Molecular Sciences, 14( 3), 5284-5311. doi:10.3390/ijms14035284
NLM
Sant'Anna RO, Braga CA, Polikarpov I, Ventura S, Lima LMTR, Foguel D. Inhibition of human transthyretin aggregation by non-steroidal anti-inflammatory compounds: a structural and thermodynamic analysis [Internet]. International Journal of Molecular Sciences. 2013 ; 14( 3): 5284-5311.[citado 2024 nov. 10 ] Available from: https://doi.org/10.3390/ijms14035284
Vancouver
Sant'Anna RO, Braga CA, Polikarpov I, Ventura S, Lima LMTR, Foguel D. Inhibition of human transthyretin aggregation by non-steroidal anti-inflammatory compounds: a structural and thermodynamic analysis [Internet]. International Journal of Molecular Sciences. 2013 ; 14( 3): 5284-5311.[citado 2024 nov. 10 ] Available from: https://doi.org/10.3390/ijms14035284
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LEITE, Fabio L. et al. Theoretical models for surface forces and adhesion and their measurement using atomic force microscopy. International Journal of Molecular Sciences, v. 13, n. 10, p. 12773-12856, 2012Tradução . . Disponível em: https://doi.org/10.3390/ijms131012773. Acesso em: 10 nov. 2024.
APA
Leite, F. L., Bueno, C. C., Da Róz, A. L., Ziemath, E. C., & Oliveira Junior, O. N. de. (2012). Theoretical models for surface forces and adhesion and their measurement using atomic force microscopy. International Journal of Molecular Sciences, 13( 10), 12773-12856. doi:10.3390/ijms131012773
NLM
Leite FL, Bueno CC, Da Róz AL, Ziemath EC, Oliveira Junior ON de. Theoretical models for surface forces and adhesion and their measurement using atomic force microscopy [Internet]. International Journal of Molecular Sciences. 2012 ; 13( 10): 12773-12856.[citado 2024 nov. 10 ] Available from: https://doi.org/10.3390/ijms131012773
Vancouver
Leite FL, Bueno CC, Da Róz AL, Ziemath EC, Oliveira Junior ON de. Theoretical models for surface forces and adhesion and their measurement using atomic force microscopy [Internet]. International Journal of Molecular Sciences. 2012 ; 13( 10): 12773-12856.[citado 2024 nov. 10 ] Available from: https://doi.org/10.3390/ijms131012773
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LAINE, Élodie et al. Molecular motions as a drug target: mechanistic simulations of anthrax toxin edema factor function led to the discovery of novel allosteric inhibitors. Toxins, v. 4, n. 8, p. 580-604, 2012Tradução . . Disponível em: https://doi.org/10.3390/toxins4080580. Acesso em: 10 nov. 2024.
APA
Laine, É., Martínez, L., Ladant, D., Malliavin, T., & Blondel, A. (2012). Molecular motions as a drug target: mechanistic simulations of anthrax toxin edema factor function led to the discovery of novel allosteric inhibitors. Toxins, 4( 8), 580-604. doi:10.3390/toxins4080580
NLM
Laine É, Martínez L, Ladant D, Malliavin T, Blondel A. Molecular motions as a drug target: mechanistic simulations of anthrax toxin edema factor function led to the discovery of novel allosteric inhibitors [Internet]. Toxins. 2012 ; 4( 8): 580-604.[citado 2024 nov. 10 ] Available from: https://doi.org/10.3390/toxins4080580
Vancouver
Laine É, Martínez L, Ladant D, Malliavin T, Blondel A. Molecular motions as a drug target: mechanistic simulations of anthrax toxin edema factor function led to the discovery of novel allosteric inhibitors [Internet]. Toxins. 2012 ; 4( 8): 580-604.[citado 2024 nov. 10 ] Available from: https://doi.org/10.3390/toxins4080580