ReP USP - Resultado da busca

Artigo de periodico
Structure, computational and biochemical analysis of PcCel45A endoglucanase from Phanerochaete chrysosporium and catalytic mechanisms of GH45 subfamily C members (2018)
Godoy, Andre S.; Pereira, Caroline S.; Ramia, Marina Paglione; Silveira, Rodrigo L.; Camilo, Cesar M.; Kadowaki, Marco A.; Lange, Lene; Busk, Peter K.; Nascimento, Alessandro Silva ; Skaf, Munir S.; Polikarpov, Igor
Source: Scientific Reports. Unidade: IFSC
Subjects: ENZIMAS, RECEPTORES, CRISTALOGRAFIA ESTRUTURAL
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ABNT
GODOY, Andre S. et al. Structure, computational and biochemical analysis of PcCel45A endoglucanase from Phanerochaete chrysosporium and catalytic mechanisms of GH45 subfamily C members. Scientific Reports, v. 8, p. 3678-1-3678-14, 2018Tradução . . Disponível em: https://doi.org/10.1038/s41598-018-21798-9. Acesso em: 11 nov. 2024.
APA
Godoy, A. S., Pereira, C. S., Ramia, M. P., Silveira, R. L., Camilo, C. M., Kadowaki, M. A., et al. (2018). Structure, computational and biochemical analysis of PcCel45A endoglucanase from Phanerochaete chrysosporium and catalytic mechanisms of GH45 subfamily C members. Scientific Reports, 8, 3678-1-3678-14. doi:10.1038/s41598-018-21798-9
NLM
Godoy AS, Pereira CS, Ramia MP, Silveira RL, Camilo CM, Kadowaki MA, Lange L, Busk PK, Nascimento AS, Skaf MS, Polikarpov I. Structure, computational and biochemical analysis of PcCel45A endoglucanase from Phanerochaete chrysosporium and catalytic mechanisms of GH45 subfamily C members [Internet]. Scientific Reports. 2018 ; 8 3678-1-3678-14.[citado 2024 nov. 11 ] Available from: https://doi.org/10.1038/s41598-018-21798-9
Vancouver
Godoy AS, Pereira CS, Ramia MP, Silveira RL, Camilo CM, Kadowaki MA, Lange L, Busk PK, Nascimento AS, Skaf MS, Polikarpov I. Structure, computational and biochemical analysis of PcCel45A endoglucanase from Phanerochaete chrysosporium and catalytic mechanisms of GH45 subfamily C members [Internet]. Scientific Reports. 2018 ; 8 3678-1-3678-14.[citado 2024 nov. 11 ] Available from: https://doi.org/10.1038/s41598-018-21798-9
Artigo de periodico
Structural and biochemical characterization of a GH3 b-glucosidase from the probiotic bacteria Bifidobacterium adolescentis (2018)
Florindo, Renata N.; Souza, Valquiria P.; Manzine, Livia Regina; Camilo, Cesar M.; Marana, Sandro Roberto ; Polikarpov, Igor ; Nascimento, Alessandro Silva
Source: Biochimie. Unidades: IFSC, IQ
Subjects: BACTÉRIAS, BIOQUÍMICA
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ABNT
FLORINDO, Renata N. et al. Structural and biochemical characterization of a GH3 b-glucosidase from the probiotic bacteria Bifidobacterium adolescentis. Biochimie, v. 148, p. 107-115, 2018Tradução . . Disponível em: https://doi.org/10.1016/j.biochi.2018.03.007. Acesso em: 11 nov. 2024.
APA
Florindo, R. N., Souza, V. P., Manzine, L. R., Camilo, C. M., Marana, S. R., Polikarpov, I., & Nascimento, A. S. (2018). Structural and biochemical characterization of a GH3 b-glucosidase from the probiotic bacteria Bifidobacterium adolescentis. Biochimie, 148, 107-115. doi:10.1016/j.biochi.2018.03.007
NLM
Florindo RN, Souza VP, Manzine LR, Camilo CM, Marana SR, Polikarpov I, Nascimento AS. Structural and biochemical characterization of a GH3 b-glucosidase from the probiotic bacteria Bifidobacterium adolescentis [Internet]. Biochimie. 2018 ; 148 107-115.[citado 2024 nov. 11 ] Available from: https://doi.org/10.1016/j.biochi.2018.03.007
Vancouver
Florindo RN, Souza VP, Manzine LR, Camilo CM, Marana SR, Polikarpov I, Nascimento AS. Structural and biochemical characterization of a GH3 b-glucosidase from the probiotic bacteria Bifidobacterium adolescentis [Internet]. Biochimie. 2018 ; 148 107-115.[citado 2024 nov. 11 ] Available from: https://doi.org/10.1016/j.biochi.2018.03.007
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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ABNT
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: 11 nov. 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 nov. 11 ] 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 nov. 11 ] Available from: https://doi.org/10.1107/S2053230X16003617
Artigo de periodico
Molecular characterization of a family 5 glycoside hydrolase suggests an induced-fit enzymatic mechanism (2016)
Liberato, Marcelo V.; Silveira, Rodrigo L.; Prates, Érica T.; Araujo, Evandro A.; Pellegrini, Vanessa O. A.; Camilo, Cesar M.; Kadowaki, Marco A.; Neto, Mario de O.; Popov, Alexander; Skaf, Munir S.; Polikarpov, Igor
Source: Scientific Reports. Unidade: IFSC
Subjects: BIOTECNOLOGIA, MICROBIOLOGIA
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ABNT
LIBERATO, Marcelo V. et al. Molecular characterization of a family 5 glycoside hydrolase suggests an induced-fit enzymatic mechanism. Scientific Reports, v. 6, p. 23473-1-23473-15 + supplementary information, 2016Tradução . . Disponível em: https://doi.org/10.1038/srep23473. Acesso em: 11 nov. 2024.
APA
Liberato, M. V., Silveira, R. L., Prates, É. T., Araujo, E. A., Pellegrini, V. O. A., Camilo, C. M., et al. (2016). Molecular characterization of a family 5 glycoside hydrolase suggests an induced-fit enzymatic mechanism. Scientific Reports, 6, 23473-1-23473-15 + supplementary information. doi:10.1038/srep23473
NLM
Liberato MV, Silveira RL, Prates ÉT, Araujo EA, Pellegrini VOA, Camilo CM, Kadowaki MA, Neto M de O, Popov A, Skaf MS, Polikarpov I. Molecular characterization of a family 5 glycoside hydrolase suggests an induced-fit enzymatic mechanism [Internet]. Scientific Reports. 2016 ; 6 23473-1-23473-15 + supplementary information.[citado 2024 nov. 11 ] Available from: https://doi.org/10.1038/srep23473
Vancouver
Liberato MV, Silveira RL, Prates ÉT, Araujo EA, Pellegrini VOA, Camilo CM, Kadowaki MA, Neto M de O, Popov A, Skaf MS, Polikarpov I. Molecular characterization of a family 5 glycoside hydrolase suggests an induced-fit enzymatic mechanism [Internet]. Scientific Reports. 2016 ; 6 23473-1-23473-15 + supplementary information.[citado 2024 nov. 11 ] Available from: https://doi.org/10.1038/srep23473
Artigo de periodico
Recombinant Trichoderma harzianum endoglucanase I (Cel7B) is a highly acidic and promiscuous carbohydrate-active enzyme (2015)
Pellegrini, Vanessa O. A.; Serpa, Viviane Isabel; Godoy, Andre S.; Camilo, Cesar M.; Bernardes, Amanda; Rezende, Camila A.; Pereira Junior, Nei; Cairo, João Paulo L. Franco; Squina, Fabio M.; Polikarpov, Igor
Source: Applied Microbiology and Biotechnology. Unidade: IFSC
Subjects: CELULOSE, TRICHODERMA, BIOCOMBUSTÍVEIS
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ABNT
PELLEGRINI, Vanessa O. A. et al. Recombinant Trichoderma harzianum endoglucanase I (Cel7B) is a highly acidic and promiscuous carbohydrate-active enzyme. Applied Microbiology and Biotechnology, v. No 2015, n. 22, p. 9591-9604, 2015Tradução . . Disponível em: https://doi.org/10.1007/s00253-015-6772-1. Acesso em: 11 nov. 2024.
APA
Pellegrini, V. O. A., Serpa, V. I., Godoy, A. S., Camilo, C. M., Bernardes, A., Rezende, C. A., et al. (2015). Recombinant Trichoderma harzianum endoglucanase I (Cel7B) is a highly acidic and promiscuous carbohydrate-active enzyme. Applied Microbiology and Biotechnology, No 2015( 22), 9591-9604. doi:10.1007/s00253-015-6772-1
NLM
Pellegrini VOA, Serpa VI, Godoy AS, Camilo CM, Bernardes A, Rezende CA, Pereira Junior N, Cairo JPLF, Squina FM, Polikarpov I. Recombinant Trichoderma harzianum endoglucanase I (Cel7B) is a highly acidic and promiscuous carbohydrate-active enzyme [Internet]. Applied Microbiology and Biotechnology. 2015 ; No 2015( 22): 9591-9604.[citado 2024 nov. 11 ] Available from: https://doi.org/10.1007/s00253-015-6772-1
Vancouver
Pellegrini VOA, Serpa VI, Godoy AS, Camilo CM, Bernardes A, Rezende CA, Pereira Junior N, Cairo JPLF, Squina FM, Polikarpov I. Recombinant Trichoderma harzianum endoglucanase I (Cel7B) is a highly acidic and promiscuous carbohydrate-active enzyme [Internet]. Applied Microbiology and Biotechnology. 2015 ; No 2015( 22): 9591-9604.[citado 2024 nov. 11 ] Available from: https://doi.org/10.1007/s00253-015-6772-1
Artigo de periodico
HTP-oligodesigner: an online primer design tool for high-throughput gene cloning and site-directed mutagenesis (2015)
Camilo, Cesar M.; Lima, Gustavo, M. A.; Maluf, Fernando V.; Guido, Rafael Victorio Carvalho ; Polikarpov, Igor
Source: Journal of Computational Biology. Unidade: IFSC
Subjects: GENÔMICA, PRIMERS DO DNA
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ABNT
CAMILO, Cesar M. et al. HTP-oligodesigner: an online primer design tool for high-throughput gene cloning and site-directed mutagenesis. Journal of Computational Biology, v. 23, n. 1, p. 27-29, 2015Tradução . . Disponível em: https://doi.org/10.1089/cmb.2015.0148. Acesso em: 11 nov. 2024.
APA
Camilo, C. M., Lima, G., Maluf, F. V., Guido, R. V. C., & Polikarpov, I. (2015). HTP-oligodesigner: an online primer design tool for high-throughput gene cloning and site-directed mutagenesis. Journal of Computational Biology, 23( 1), 27-29. doi:10.1089/cmb.2015.0148
NLM
Camilo CM, Lima G, Maluf FV, Guido RVC, Polikarpov I. HTP-oligodesigner: an online primer design tool for high-throughput gene cloning and site-directed mutagenesis [Internet]. Journal of Computational Biology. 2015 ; 23( 1): 27-29.[citado 2024 nov. 11 ] Available from: https://doi.org/10.1089/cmb.2015.0148
Vancouver
Camilo CM, Lima G, Maluf FV, Guido RVC, Polikarpov I. HTP-oligodesigner: an online primer design tool for high-throughput gene cloning and site-directed mutagenesis [Internet]. Journal of Computational Biology. 2015 ; 23( 1): 27-29.[citado 2024 nov. 11 ] Available from: https://doi.org/10.1089/cmb.2015.0148
Artigo de periodico
Draft genome sequence of the thermophile Thermus filiformis ATCC 43280, producer of carotenoid-(di)glucoside-branched fatty acid (di)esters and source of hyperthermostable enzymes of biotechnological interest (2015)
Mandelli, Fernanda; Ramires, Brenda Oliveira; Couger, Matthew Brian; Paixão, Douglas A. A.; Camilo, Cesar M.; Polikarpov, Igor ; Prade, Rolf; Riaño-Pachón, Diego Mauricio; Squina, Fabio M.
Source: Genome Announcements. Unidade: IFSC
Subjects: BIOTECNOLOGIA, TUBERCULOSE
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ABNT
MANDELLI, Fernanda et al. Draft genome sequence of the thermophile Thermus filiformis ATCC 43280, producer of carotenoid-(di)glucoside-branched fatty acid (di)esters and source of hyperthermostable enzymes of biotechnological interest. Genome Announcements, v. 3, n. 3, p. e00475-15-1-e00475-15-2, 2015Tradução . . Disponível em: https://doi.org/10.1128/genomeA.00466-15. Acesso em: 11 nov. 2024.
APA
Mandelli, F., Ramires, B. O., Couger, M. B., Paixão, D. A. A., Camilo, C. M., Polikarpov, I., et al. (2015). Draft genome sequence of the thermophile Thermus filiformis ATCC 43280, producer of carotenoid-(di)glucoside-branched fatty acid (di)esters and source of hyperthermostable enzymes of biotechnological interest. Genome Announcements, 3( 3), e00475-15-1-e00475-15-2. doi:10.1128/genomeA.00466-15
NLM
Mandelli F, Ramires BO, Couger MB, Paixão DAA, Camilo CM, Polikarpov I, Prade R, Riaño-Pachón DM, Squina FM. Draft genome sequence of the thermophile Thermus filiformis ATCC 43280, producer of carotenoid-(di)glucoside-branched fatty acid (di)esters and source of hyperthermostable enzymes of biotechnological interest [Internet]. Genome Announcements. 2015 ; 3( 3): e00475-15-1-e00475-15-2.[citado 2024 nov. 11 ] Available from: https://doi.org/10.1128/genomeA.00466-15
Vancouver
Mandelli F, Ramires BO, Couger MB, Paixão DAA, Camilo CM, Polikarpov I, Prade R, Riaño-Pachón DM, Squina FM. Draft genome sequence of the thermophile Thermus filiformis ATCC 43280, producer of carotenoid-(di)glucoside-branched fatty acid (di)esters and source of hyperthermostable enzymes of biotechnological interest [Internet]. Genome Announcements. 2015 ; 3( 3): e00475-15-1-e00475-15-2.[citado 2024 nov. 11 ] Available from: https://doi.org/10.1128/genomeA.00466-15
Artigo de periodico
High-throughput cloning, expression and purification of glycoside hydrolases using Ligation-Independent Cloning (LIC) (2014)
Camilo, Cesar M.; Polikarpov, Igor
Source: Protein Expression and Purification. Unidade: IFSC
Subjects: CLONAGEM, ENZIMAS, PROTEÍNAS (CARACTERÍSTICAS)
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ABNT
CAMILO, Cesar M. e POLIKARPOV, Igor. High-throughput cloning, expression and purification of glycoside hydrolases using Ligation-Independent Cloning (LIC). Protein Expression and Purification, v. 99, p. 35-42, 2014Tradução . . Disponível em: https://doi.org/10.1016/j.pep.2014.03.008. Acesso em: 11 nov. 2024.
APA
Camilo, C. M., & Polikarpov, I. (2014). High-throughput cloning, expression and purification of glycoside hydrolases using Ligation-Independent Cloning (LIC). Protein Expression and Purification, 99, 35-42. doi:10.1016/j.pep.2014.03.008
NLM
Camilo CM, Polikarpov I. High-throughput cloning, expression and purification of glycoside hydrolases using Ligation-Independent Cloning (LIC) [Internet]. Protein Expression and Purification. 2014 ; 99 35-42.[citado 2024 nov. 11 ] Available from: https://doi.org/10.1016/j.pep.2014.03.008
Vancouver
Camilo CM, Polikarpov I. High-throughput cloning, expression and purification of glycoside hydrolases using Ligation-Independent Cloning (LIC) [Internet]. Protein Expression and Purification. 2014 ; 99 35-42.[citado 2024 nov. 11 ] Available from: https://doi.org/10.1016/j.pep.2014.03.008

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