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Artigo de periodico
Two-domain GH30 xylanase from human gut microbiota as a tool for enzymatic production of xylooligosaccharides: crystallographic structure and a synergy with GH11 xylosidase (2024)
Vacilotto, Milena Moreira ; Montalvão, Lucas de Araujo; Pellegrini, Vanessa de Oliveira Arnoldi ; Liberato, Marcelo Vizona; Araújo, Evandro Ares de ; Polikarpov, Igor
Source: Carbohydrate Polymers. Unidade: IFSC
Subjects: ENZIMAS, POLISSACARÍDEOS, BIOTECNOLOGIA
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ABNT
VACILOTTO, Milena Moreira et al. Two-domain GH30 xylanase from human gut microbiota as a tool for enzymatic production of xylooligosaccharides: crystallographic structure and a synergy with GH11 xylosidase. Carbohydrate Polymers, v. 337, p. 122141-1-122141-14 + supplementary data, 2024Tradução . . Disponível em: https://doi.org/10.1016/j.carbpol.2024.122141. Acesso em: 01 jul. 2024.
APA
Vacilotto, M. M., Montalvão, L. de A., Pellegrini, V. de O. A., Liberato, M. V., Araújo, E. A. de, & Polikarpov, I. (2024). Two-domain GH30 xylanase from human gut microbiota as a tool for enzymatic production of xylooligosaccharides: crystallographic structure and a synergy with GH11 xylosidase. Carbohydrate Polymers, 337, 122141-1-122141-14 + supplementary data. doi:10.1016/j.carbpol.2024.122141
NLM
Vacilotto MM, Montalvão L de A, Pellegrini V de OA, Liberato MV, Araújo EA de, Polikarpov I. Two-domain GH30 xylanase from human gut microbiota as a tool for enzymatic production of xylooligosaccharides: crystallographic structure and a synergy with GH11 xylosidase [Internet]. Carbohydrate Polymers. 2024 ; 337 122141-1-122141-14 + supplementary data.[citado 2024 jul. 01 ] Available from: https://doi.org/10.1016/j.carbpol.2024.122141
Vancouver
Vacilotto MM, Montalvão L de A, Pellegrini V de OA, Liberato MV, Araújo EA de, Polikarpov I. Two-domain GH30 xylanase from human gut microbiota as a tool for enzymatic production of xylooligosaccharides: crystallographic structure and a synergy with GH11 xylosidase [Internet]. Carbohydrate Polymers. 2024 ; 337 122141-1-122141-14 + supplementary data.[citado 2024 jul. 01 ] Available from: https://doi.org/10.1016/j.carbpol.2024.122141
Artigo de periodico
Insights into the dual cleavage activity of the GH16 laminarinase enzyme class on β-1,3 and β-1,4 glycosidic bonds (2021)
Liberato, Marcelo Vizona; Prates, Erica Teixeira; Gonçalves, Thiago Augusto; Bernardes, Amanda; Vilela, Nathalia ; Fattori, Juliana; Ematsu, Gabriela Cristina; Chinaglia, Mariana; Gomes, Emerson Rodrigo Machi; Figueira, Ana Carolina Migliorini; Damasio, André; Polikarpov, Igor ; Skaf, Munir S.; Squina, Fabio Marcio
Source: Journal of Biological Chemistry. Unidade: IFSC
Subjects: BIOTECNOLOGIA, ENZIMAS HIDROLÍTICAS, POLISSACARÍDEOS
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ABNT
LIBERATO, Marcelo Vizona et al. Insights into the dual cleavage activity of the GH16 laminarinase enzyme class on β-1,3 and β-1,4 glycosidic bonds. Journal of Biological Chemistry, v. 296, n. ja-ju 2021, p. 100385-1-100385-13 + supporting information: S1-S15, 2021Tradução . . Disponível em: https://doi.org/10.1016/j.jbc.2021.100385. Acesso em: 01 jul. 2024.
APA
Liberato, M. V., Prates, E. T., Gonçalves, T. A., Bernardes, A., Vilela, N., Fattori, J., et al. (2021). Insights into the dual cleavage activity of the GH16 laminarinase enzyme class on β-1,3 and β-1,4 glycosidic bonds. Journal of Biological Chemistry, 296( ja-ju 2021), 100385-1-100385-13 + supporting information: S1-S15. doi:10.1016/j.jbc.2021.100385
NLM
Liberato MV, Prates ET, Gonçalves TA, Bernardes A, Vilela N, Fattori J, Ematsu GC, Chinaglia M, Gomes ERM, Figueira ACM, Damasio A, Polikarpov I, Skaf MS, Squina FM. Insights into the dual cleavage activity of the GH16 laminarinase enzyme class on β-1,3 and β-1,4 glycosidic bonds [Internet]. Journal of Biological Chemistry. 2021 ; 296( ja-ju 2021): 100385-1-100385-13 + supporting information: S1-S15.[citado 2024 jul. 01 ] Available from: https://doi.org/10.1016/j.jbc.2021.100385
Vancouver
Liberato MV, Prates ET, Gonçalves TA, Bernardes A, Vilela N, Fattori J, Ematsu GC, Chinaglia M, Gomes ERM, Figueira ACM, Damasio A, Polikarpov I, Skaf MS, Squina FM. Insights into the dual cleavage activity of the GH16 laminarinase enzyme class on β-1,3 and β-1,4 glycosidic bonds [Internet]. Journal of Biological Chemistry. 2021 ; 296( ja-ju 2021): 100385-1-100385-13 + supporting information: S1-S15.[citado 2024 jul. 01 ] Available from: https://doi.org/10.1016/j.jbc.2021.100385
Trabalho de evento-resumo
How alkaline deacetylation can enhance the building blocks obtention from sugarcane bagasse? (2019)
Andrade, Liliane Pires; Lima, Cleilton S. ; Roberto, Inês Conceição; Murakami, Mario T. ; Rocha, George Jackson de Moraes
Source: Anais do Simpósio Nacional de Bioprocessos. Unidade: EEL
Assunto: BIOTECNOLOGIA
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ABNT
ANDRADE, Liliane Pires et al. How alkaline deacetylation can enhance the building blocks obtention from sugarcane bagasse? 2019, Anais.. Uberlândia-MG: Escola de Engenharia de Lorena, Universidade de São Paulo, 2019. p. 1-1. Disponível em: https://proceedings.science/p/104419. Acesso em: 01 jul. 2024.
APA
Andrade, L. P., Lima, C. S., Roberto, I. C., Murakami, M. T., & Rocha, G. J. de M. (2019). How alkaline deacetylation can enhance the building blocks obtention from sugarcane bagasse? In Anais do Simpósio Nacional de Bioprocessos (p. 1-1). Uberlândia-MG: Escola de Engenharia de Lorena, Universidade de São Paulo. Recuperado de https://proceedings.science/p/104419
NLM
Andrade LP, Lima CS, Roberto IC, Murakami MT, Rocha GJ de M. How alkaline deacetylation can enhance the building blocks obtention from sugarcane bagasse? [Internet]. Anais do Simpósio Nacional de Bioprocessos. 2019 ;1-1.[citado 2024 jul. 01 ] Available from: https://proceedings.science/p/104419
Vancouver
Andrade LP, Lima CS, Roberto IC, Murakami MT, Rocha GJ de M. How alkaline deacetylation can enhance the building blocks obtention from sugarcane bagasse? [Internet]. Anais do Simpósio Nacional de Bioprocessos. 2019 ;1-1.[citado 2024 jul. 01 ] Available from: https://proceedings.science/p/104419
Artigo de periodico
Understanding the role of the master regulator XYR1 in Trichoderma reesei by global transcriptional analysis (2016)
Castro, Lilian dos Santos; Paula, Renato Graciano de; Antoniêto, Amanda Cristina Campos; Persinoti, Gabriela Felix; Silva-Rocha, Rafael; Silva, Roberto do Nascimento
Source: Frontiers in Microbiology. Unidade: FMRP
Subjects: TRICHODERMA, FUNGOS, BIOTECNOLOGIA, CELULOSE, EXPRESSÃO GÊNICA
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ABNT
CASTRO, Lilian dos Santos et al. Understanding the role of the master regulator XYR1 in Trichoderma reesei by global transcriptional analysis. Frontiers in Microbiology, v. 7, 2016Tradução . . Disponível em: https://doi.org/10.3389/fmicb.2016.00175. Acesso em: 01 jul. 2024.
APA
Castro, L. dos S., Paula, R. G. de, Antoniêto, A. C. C., Persinoti, G. F., Silva-Rocha, R., & Silva, R. do N. (2016). Understanding the role of the master regulator XYR1 in Trichoderma reesei by global transcriptional analysis. Frontiers in Microbiology, 7. doi:10.3389/fmicb.2016.00175
NLM
Castro L dos S, Paula RG de, Antoniêto ACC, Persinoti GF, Silva-Rocha R, Silva R do N. Understanding the role of the master regulator XYR1 in Trichoderma reesei by global transcriptional analysis [Internet]. Frontiers in Microbiology. 2016 ; 7[citado 2024 jul. 01 ] Available from: https://doi.org/10.3389/fmicb.2016.00175
Vancouver
Castro L dos S, Paula RG de, Antoniêto ACC, Persinoti GF, Silva-Rocha R, Silva R do N. Understanding the role of the master regulator XYR1 in Trichoderma reesei by global transcriptional analysis [Internet]. Frontiers in Microbiology. 2016 ; 7[citado 2024 jul. 01 ] Available from: https://doi.org/10.3389/fmicb.2016.00175
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: 01 jul. 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 jul. 01 ] 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 jul. 01 ] Available from: https://doi.org/10.1128/genomeA.00466-15
Artigo de periodico
RXR agonist modulates TR: corepressor dissociation upon 9-cis retinoic acid treatment (2015)
Fattori, Juliana; Campos, Jéssica L. O.; Doratioto, Tábata R.; Assis, Lucas M.; Vitorino, Mariela T.; Polikarpov, Igor; Xavier-Neto, José
Source: Molecular Endocrinology. Unidade: IFSC
Subjects: BIOTECNOLOGIA, DOENÇAS (TRATAMENTO)
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ABNT
FATTORI, Juliana et al. RXR agonist modulates TR: corepressor dissociation upon 9-cis retinoic acid treatment. Molecular Endocrinology, v. 29, n. 2, p. 258-273, 2015Tradução . . Disponível em: https://doi.org/10.1210/me.2014-125. Acesso em: 01 jul. 2024.
APA
Fattori, J., Campos, J. L. O., Doratioto, T. R., Assis, L. M., Vitorino, M. T., Polikarpov, I., & Xavier-Neto, J. (2015). RXR agonist modulates TR: corepressor dissociation upon 9-cis retinoic acid treatment. Molecular Endocrinology, 29( 2), 258-273. doi:10.1210/me.2014-125
NLM
Fattori J, Campos JLO, Doratioto TR, Assis LM, Vitorino MT, Polikarpov I, Xavier-Neto J. RXR agonist modulates TR: corepressor dissociation upon 9-cis retinoic acid treatment [Internet]. Molecular Endocrinology. 2015 ; 29( 2): 258-273.[citado 2024 jul. 01 ] Available from: https://doi.org/10.1210/me.2014-125
Vancouver
Fattori J, Campos JLO, Doratioto TR, Assis LM, Vitorino MT, Polikarpov I, Xavier-Neto J. RXR agonist modulates TR: corepressor dissociation upon 9-cis retinoic acid treatment [Internet]. Molecular Endocrinology. 2015 ; 29( 2): 258-273.[citado 2024 jul. 01 ] Available from: https://doi.org/10.1210/me.2014-125
Artigo de periodico
Low-resolution molecular models reveal the oligomeric state of the PPAR and the conformational organization of its domains in solution (2012)
Bernardes, Amanda; Batista, Fernanda A. H.; Oliveira Neto, Mario de; Figueira, Ana Carolina M.; Webb, Paul; Saidemberg, Daniel Menezes; Palma, Mario S.; Polikarpov, Igor
Source: PLOS ONE. Unidade: IFSC
Subjects: RECEPTORES, CRISTALOGRAFIA, BIOTECNOLOGIA
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ABNT
BERNARDES, Amanda et al. Low-resolution molecular models reveal the oligomeric state of the PPAR and the conformational organization of its domains in solution. PLOS ONE, v. 7, n. 2, p. e31852-1-e31852-15, 2012Tradução . . Disponível em: https://doi.org/10.1371/journal.pone.0031852. Acesso em: 01 jul. 2024.
APA
Bernardes, A., Batista, F. A. H., Oliveira Neto, M. de, Figueira, A. C. M., Webb, P., Saidemberg, D. M., et al. (2012). Low-resolution molecular models reveal the oligomeric state of the PPAR and the conformational organization of its domains in solution. PLOS ONE, 7( 2), e31852-1-e31852-15. doi:10.1371/journal.pone.0031852
NLM
Bernardes A, Batista FAH, Oliveira Neto M de, Figueira ACM, Webb P, Saidemberg DM, Palma MS, Polikarpov I. Low-resolution molecular models reveal the oligomeric state of the PPAR and the conformational organization of its domains in solution [Internet]. PLOS ONE. 2012 ; 7( 2): e31852-1-e31852-15.[citado 2024 jul. 01 ] Available from: https://doi.org/10.1371/journal.pone.0031852
Vancouver
Bernardes A, Batista FAH, Oliveira Neto M de, Figueira ACM, Webb P, Saidemberg DM, Palma MS, Polikarpov I. Low-resolution molecular models reveal the oligomeric state of the PPAR and the conformational organization of its domains in solution [Internet]. PLOS ONE. 2012 ; 7( 2): e31852-1-e31852-15.[citado 2024 jul. 01 ] Available from: https://doi.org/10.1371/journal.pone.0031852

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