ReP USP - Resultado da busca

Artigo de periodico
Biochemical characterization and low-resolution SAXS molecular envelope of GH1 β-Glycosidase from Saccharophagus degradans (2016)
Brognaro, Hevila; Almeida, Vitor Medeiros; Araújo, Evandro Ares de; Piyadov, Vasily; Santos, Maria Auxiliadora Morim; Marana, Sandro Roberto ; Polikarpov, Igor
Source: Molecular Biotechnology. Unidades: IFSC, IQ
Subjects: MODELAGEM MOLECULAR, GLICOSÍDEOS
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BROGNARO, Hevila et al. Biochemical characterization and low-resolution SAXS molecular envelope of GH1 β-Glycosidase from Saccharophagus degradans. Molecular Biotechnology, v. 58, n. 12, p. 777-788, 2016Tradução . . Disponível em: https://doi.org/10.1007/s12033-016-9977-3. Acesso em: 15 out. 2024.
APA
Brognaro, H., Almeida, V. M., Araújo, E. A. de, Piyadov, V., Santos, M. A. M., Marana, S. R., & Polikarpov, I. (2016). Biochemical characterization and low-resolution SAXS molecular envelope of GH1 β-Glycosidase from Saccharophagus degradans. Molecular Biotechnology, 58( 12), 777-788. doi:10.1007/s12033-016-9977-3
NLM
Brognaro H, Almeida VM, Araújo EA de, Piyadov V, Santos MAM, Marana SR, Polikarpov I. Biochemical characterization and low-resolution SAXS molecular envelope of GH1 β-Glycosidase from Saccharophagus degradans [Internet]. Molecular Biotechnology. 2016 ; 58( 12): 777-788.[citado 2024 out. 15 ] Available from: https://doi.org/10.1007/s12033-016-9977-3
Vancouver
Brognaro H, Almeida VM, Araújo EA de, Piyadov V, Santos MAM, Marana SR, Polikarpov I. Biochemical characterization and low-resolution SAXS molecular envelope of GH1 β-Glycosidase from Saccharophagus degradans [Internet]. Molecular Biotechnology. 2016 ; 58( 12): 777-788.[citado 2024 out. 15 ] Available from: https://doi.org/10.1007/s12033-016-9977-3
Artigo de periodico
Crystal structure of a putative exo-b-1,3-galactanase from Bifidobacterium bifidum S17 (2016)
Godoy, Andre S.; Lima, Mariana Z. T.; Camilo, Cesar M.; Polikarpov, Igor
Source: Acta Crystallographica F. Unidade: IFSC
Subjects: CANA-DE-AÇÚCAR, RAIOS X, BIOCOMBUSTÍVEIS
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GODOY, Andre S. et al. Crystal structure of a putative exo-b-1,3-galactanase from Bifidobacterium bifidum S17. Acta Crystallographica F, v. 72, p. 288-293, 2016Tradução . . Disponível em: https://doi.org/10.1107/S2053230X16003617. Acesso em: 15 out. 2024.
APA
Godoy, A. S., Lima, M. Z. T., Camilo, C. M., & Polikarpov, I. (2016). Crystal structure of a putative exo-b-1,3-galactanase from Bifidobacterium bifidum S17. Acta Crystallographica F, 72, 288-293. doi:10.1107/S2053230X16003617
NLM
Godoy AS, Lima MZT, Camilo CM, Polikarpov I. Crystal structure of a putative exo-b-1,3-galactanase from Bifidobacterium bifidum S17 [Internet]. Acta Crystallographica F. 2016 ; 72 288-293.[citado 2024 out. 15 ] Available from: https://doi.org/10.1107/S2053230X16003617
Vancouver
Godoy AS, Lima MZT, Camilo CM, Polikarpov I. Crystal structure of a putative exo-b-1,3-galactanase from Bifidobacterium bifidum S17 [Internet]. Acta Crystallographica F. 2016 ; 72 288-293.[citado 2024 out. 15 ] Available from: https://doi.org/10.1107/S2053230X16003617
Artigo de periodico
A novel carbohydrate-binding module from sugar cane soil metagenome featuring unique structural and carbohydrate affinity properties (2016)
Campos, Bruna Medeia; Liberato, Marcelo Vizona; Alvarez, Thabata Maria; Zanphorlin, Letícia Maria; Ematsu, Gabriela Cristina; Barud, Hernane; Polikarpov, Igor ; Ruller, Roberto; Gilbert, Harry J.; Zeri, Ana Carolina de Mattos; Squina, Fabio Marcio
Source: Journal of Biological Chemistry. Unidade: IFSC
Subjects: CANA-DE-AÇÚCAR, BIOMASSA, BAGAÇOS
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CAMPOS, Bruna Medeia et al. A novel carbohydrate-binding module from sugar cane soil metagenome featuring unique structural and carbohydrate affinity properties. Journal of Biological Chemistry, v. No 2016, n. 45, p. 23734-23743, 2016Tradução . . Disponível em: https://doi.org/10.1074/jbc.M116.744383. Acesso em: 15 out. 2024.
APA
Campos, B. M., Liberato, M. V., Alvarez, T. M., Zanphorlin, L. M., Ematsu, G. C., Barud, H., et al. (2016). A novel carbohydrate-binding module from sugar cane soil metagenome featuring unique structural and carbohydrate affinity properties. Journal of Biological Chemistry, No 2016( 45), 23734-23743. doi:10.1074/jbc.M116.744383
NLM
Campos BM, Liberato MV, Alvarez TM, Zanphorlin LM, Ematsu GC, Barud H, Polikarpov I, Ruller R, Gilbert HJ, Zeri AC de M, Squina FM. A novel carbohydrate-binding module from sugar cane soil metagenome featuring unique structural and carbohydrate affinity properties [Internet]. Journal of Biological Chemistry. 2016 ; No 2016( 45): 23734-23743.[citado 2024 out. 15 ] Available from: https://doi.org/10.1074/jbc.M116.744383
Vancouver
Campos BM, Liberato MV, Alvarez TM, Zanphorlin LM, Ematsu GC, Barud H, Polikarpov I, Ruller R, Gilbert HJ, Zeri AC de M, Squina FM. A novel carbohydrate-binding module from sugar cane soil metagenome featuring unique structural and carbohydrate affinity properties [Internet]. Journal of Biological Chemistry. 2016 ; No 2016( 45): 23734-23743.[citado 2024 out. 15 ] Available from: https://doi.org/10.1074/jbc.M116.744383
Artigo de periodico
Biophysical and biochemical studies of a major endoglucanase secreted by Xanthomonas campestris pv. campestris (2016)
Rosseto, Flávio Rodolfo; Manzine, Livia Regina; Oliveira Neto, Mario de; Polikarpov, Igor
Source: Enzyme and Microbial Technology. Unidade: IFSC
Subjects: ENZIMAS, HIDRÓLISE, XANTHOMONAS
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ABNT
ROSSETO, Flávio Rodolfo et al. Biophysical and biochemical studies of a major endoglucanase secreted by Xanthomonas campestris pv. campestris. Enzyme and Microbial Technology, v. 91, p. 1-7, 2016Tradução . . Disponível em: https://doi.org/10.1016/j.enzmictec.2016.05.007. Acesso em: 15 out. 2024.
APA
Rosseto, F. R., Manzine, L. R., Oliveira Neto, M. de, & Polikarpov, I. (2016). Biophysical and biochemical studies of a major endoglucanase secreted by Xanthomonas campestris pv. campestris. Enzyme and Microbial Technology, 91, 1-7. doi:10.1016/j.enzmictec.2016.05.007
NLM
Rosseto FR, Manzine LR, Oliveira Neto M de, Polikarpov I. Biophysical and biochemical studies of a major endoglucanase secreted by Xanthomonas campestris pv. campestris [Internet]. Enzyme and Microbial Technology. 2016 ; 91 1-7.[citado 2024 out. 15 ] Available from: https://doi.org/10.1016/j.enzmictec.2016.05.007
Vancouver
Rosseto FR, Manzine LR, Oliveira Neto M de, Polikarpov I. Biophysical and biochemical studies of a major endoglucanase secreted by Xanthomonas campestris pv. campestris [Internet]. Enzyme and Microbial Technology. 2016 ; 91 1-7.[citado 2024 out. 15 ] Available from: https://doi.org/10.1016/j.enzmictec.2016.05.007
Artigo de periodico
Non-productive adsorption of bacterial β-glucosidases on lignins is electrostatically modulated and depends on the presence offibronection type III-like domain (2016)
Silva, Viviam M.; Souza, Anderson S.; Negrão, Djanira R.; Polikarpov, Igor ; Squina, Fabio M.; Oliveira Neto, Mario de; Muniz, João Renato Carvalho ; Garcia, Wanius
Source: Enzyme and Microbial Technology. Unidade: IFSC
Subjects: ENZIMAS, HIDRÓLISE, ENZIMAS HIDROLÍTICAS
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ABNT
SILVA, Viviam M. et al. Non-productive adsorption of bacterial β-glucosidases on lignins is electrostatically modulated and depends on the presence offibronection type III-like domain. Enzyme and Microbial Technology, v. 87-88, p. 1-8, 2016Tradução . . Disponível em: https://doi.org/10.1016/j.enzmictec.2016.02.007. Acesso em: 15 out. 2024.
APA
Silva, V. M., Souza, A. S., Negrão, D. R., Polikarpov, I., Squina, F. M., Oliveira Neto, M. de, et al. (2016). Non-productive adsorption of bacterial β-glucosidases on lignins is electrostatically modulated and depends on the presence offibronection type III-like domain. Enzyme and Microbial Technology, 87-88, 1-8. doi:10.1016/j.enzmictec.2016.02.007
NLM
Silva VM, Souza AS, Negrão DR, Polikarpov I, Squina FM, Oliveira Neto M de, Muniz JRC, Garcia W. Non-productive adsorption of bacterial β-glucosidases on lignins is electrostatically modulated and depends on the presence offibronection type III-like domain [Internet]. Enzyme and Microbial Technology. 2016 ; 87-88 1-8.[citado 2024 out. 15 ] Available from: https://doi.org/10.1016/j.enzmictec.2016.02.007
Vancouver
Silva VM, Souza AS, Negrão DR, Polikarpov I, Squina FM, Oliveira Neto M de, Muniz JRC, Garcia W. Non-productive adsorption of bacterial β-glucosidases on lignins is electrostatically modulated and depends on the presence offibronection type III-like domain [Internet]. Enzyme and Microbial Technology. 2016 ; 87-88 1-8.[citado 2024 out. 15 ] Available from: https://doi.org/10.1016/j.enzmictec.2016.02.007
Artigo de periodico
Design of an enzyme cocktail consisting of different fungal platforms for efficient hydrolysis of sugarcane bagasse: optimization and synergism studies (2016)
Arias, Johanna Méndez; Modesto, Luiz Felipe Amarante; Polikarpov, Igor ; Pereira Junior, Nei
Source: Biotechnology Progress. Unidade: IFSC
Subjects: BAGAÇOS, CANA-DE-AÇÚCAR, CELULOSE, HIDRÓLISE, ENZIMAS
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ABNT
ARIAS, Johanna Méndez et al. Design of an enzyme cocktail consisting of different fungal platforms for efficient hydrolysis of sugarcane bagasse: optimization and synergism studies. Biotechnology Progress, v. 32, n. 5, p. 1222-1229, 2016Tradução . . Disponível em: https://doi.org/10.1002/btpr.2306. Acesso em: 15 out. 2024.
APA
Arias, J. M., Modesto, L. F. A., Polikarpov, I., & Pereira Junior, N. (2016). Design of an enzyme cocktail consisting of different fungal platforms for efficient hydrolysis of sugarcane bagasse: optimization and synergism studies. Biotechnology Progress, 32( 5), 1222-1229. doi:10.1002/btpr.2306
NLM
Arias JM, Modesto LFA, Polikarpov I, Pereira Junior N. Design of an enzyme cocktail consisting of different fungal platforms for efficient hydrolysis of sugarcane bagasse: optimization and synergism studies [Internet]. Biotechnology Progress. 2016 ; 32( 5): 1222-1229.[citado 2024 out. 15 ] Available from: https://doi.org/10.1002/btpr.2306
Vancouver
Arias JM, Modesto LFA, Polikarpov I, Pereira Junior N. Design of an enzyme cocktail consisting of different fungal platforms for efficient hydrolysis of sugarcane bagasse: optimization and synergism studies [Internet]. Biotechnology Progress. 2016 ; 32( 5): 1222-1229.[citado 2024 out. 15 ] Available from: https://doi.org/10.1002/btpr.2306
Trabalho de evento-resumo
The synergic strategies employed by Aspergillus niveus and Myceliophthora thermophila to degrade sugarcane bagasse (2016)
Segato, Fernando; Couger, B.; Prade, R. A.; Correr, F. H.; Corrêa, F. E.; Margarido, Gabriel Rodrigues Alves; Polikarpov, Igor
Source: Abstracts. Conference titles: Symposium on Biotechnology for Fuels and Chemicals - SBFC. Unidades: EEL, ESALQ, IFSC
Subjects: ENZIMAS, BIOMASSA, BIOCOMBUSTÍVEIS
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SEGATO, Fernando et al. The synergic strategies employed by Aspergillus niveus and Myceliophthora thermophila to degrade sugarcane bagasse. 2016, Anais.. Fairfax: Society for Industrial Microbiology - SIMB, 2016. Disponível em: https://sim.confex.com/sim/38th/webprogram/Paper31988.html. Acesso em: 15 out. 2024.
APA
Segato, F., Couger, B., Prade, R. A., Correr, F. H., Corrêa, F. E., Margarido, G. R. A., & Polikarpov, I. (2016). The synergic strategies employed by Aspergillus niveus and Myceliophthora thermophila to degrade sugarcane bagasse. In Abstracts. Fairfax: Society for Industrial Microbiology - SIMB. Recuperado de https://sim.confex.com/sim/38th/webprogram/Paper31988.html
NLM
Segato F, Couger B, Prade RA, Correr FH, Corrêa FE, Margarido GRA, Polikarpov I. The synergic strategies employed by Aspergillus niveus and Myceliophthora thermophila to degrade sugarcane bagasse [Internet]. Abstracts. 2016 ;[citado 2024 out. 15 ] Available from: https://sim.confex.com/sim/38th/webprogram/Paper31988.html
Vancouver
Segato F, Couger B, Prade RA, Correr FH, Corrêa FE, Margarido GRA, Polikarpov I. The synergic strategies employed by Aspergillus niveus and Myceliophthora thermophila to degrade sugarcane bagasse [Internet]. Abstracts. 2016 ;[citado 2024 out. 15 ] Available from: https://sim.confex.com/sim/38th/webprogram/Paper31988.html
Editor de periodico
Enzyme Engineering (2016)
Vilanova, Eugenio (Editor); Polikarpov, Igor (Editor)
Unidade: IFSC
Assunto: ENGENHARIA QUÍMICA
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ABNT
Enzyme Engineering. . Los Angeles: OMICS International. . Acesso em: 15 out. 2024. , 2016
APA
Enzyme Engineering. (2016). Enzyme Engineering. Los Angeles: OMICS International.
NLM
Enzyme Engineering. 2016 ;[citado 2024 out. 15 ]
Vancouver
Enzyme Engineering. 2016 ;[citado 2024 out. 15 ]
Artigo de periodico
Crystal structure of β1→6-galactosidase from Bifidobacterium bifidum S17: trimeric architecture, molecular determinants of the enzymatic activity and its inhibition by a-galactose (2016)
Godoy, Andre Schutzer; Camilo, Cesar Moises; Kadowaki, Marco Antonio; Muniz, Heloisa dos S.; Espirito Santo, Melissa; Murakami, Mario Tyago; Nascimento, Alessandro Silva ; Polikarpov, Igor
Source: FEBS Journal. Unidade: IFSC
Subjects: ENZIMAS, BAGAÇOS, BIOMASSA, CANA-DE-AÇÚCAR
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ABNT
GODOY, Andre Schutzer et al. Crystal structure of β1→6-galactosidase from Bifidobacterium bifidum S17: trimeric architecture, molecular determinants of the enzymatic activity and its inhibition by a-galactose. FEBS Journal, v. No 2016, n. 22, p. 4097-4112, 2016Tradução . . Disponível em: https://doi.org/10.1111/febs.13908. Acesso em: 15 out. 2024.
APA
Godoy, A. S., Camilo, C. M., Kadowaki, M. A., Muniz, H. dos S., Espirito Santo, M., Murakami, M. T., et al. (2016). Crystal structure of β1→6-galactosidase from Bifidobacterium bifidum S17: trimeric architecture, molecular determinants of the enzymatic activity and its inhibition by a-galactose. FEBS Journal, No 2016( 22), 4097-4112. doi:10.1111/febs.13908
NLM
Godoy AS, Camilo CM, Kadowaki MA, Muniz H dos S, Espirito Santo M, Murakami MT, Nascimento AS, Polikarpov I. Crystal structure of β1→6-galactosidase from Bifidobacterium bifidum S17: trimeric architecture, molecular determinants of the enzymatic activity and its inhibition by a-galactose [Internet]. FEBS Journal. 2016 ; No 2016( 22): 4097-4112.[citado 2024 out. 15 ] Available from: https://doi.org/10.1111/febs.13908
Vancouver
Godoy AS, Camilo CM, Kadowaki MA, Muniz H dos S, Espirito Santo M, Murakami MT, Nascimento AS, Polikarpov I. Crystal structure of β1→6-galactosidase from Bifidobacterium bifidum S17: trimeric architecture, molecular determinants of the enzymatic activity and its inhibition by a-galactose [Internet]. FEBS Journal. 2016 ; No 2016( 22): 4097-4112.[citado 2024 out. 15 ] Available from: https://doi.org/10.1111/febs.13908

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