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Artigo de periodico
Immobilization of amano lipase from pseudomonas fluorescens on silk fibroin spheres: an alternative protocol for the enantioselective synthesis of halohydrins (2017)
Ferreira , Irlon Maciel; Yoshioka, Sergio Akinobu ; Comasseto, João Valdir; Porto, Andre Luiz Meleiro
Fonte: RSC Advances. Unidades: IQSC, IQ
Assuntos: ENZIMAS, CATÁLISE
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FERREIRA , Irlon Maciel et al. Immobilization of amano lipase from pseudomonas fluorescens on silk fibroin spheres: an alternative protocol for the enantioselective synthesis of halohydrins. RSC Advances, v. 7, p. 12650-12658, 2017Tradução . . Disponível em: https://doi.org/10.1039/c7ra00083a. Acesso em: 31 jul. 2024.
APA
Ferreira , I. M., Yoshioka, S. A., Comasseto, J. V., & Porto, A. L. M. (2017). Immobilization of amano lipase from pseudomonas fluorescens on silk fibroin spheres: an alternative protocol for the enantioselective synthesis of halohydrins. RSC Advances, 7, 12650-12658. doi:10.1039/c7ra00083a
NLM
Ferreira IM, Yoshioka SA, Comasseto JV, Porto ALM. Immobilization of amano lipase from pseudomonas fluorescens on silk fibroin spheres: an alternative protocol for the enantioselective synthesis of halohydrins [Internet]. RSC Advances. 2017 ; 7 12650-12658.[citado 2024 jul. 31 ] Available from: https://doi.org/10.1039/c7ra00083a
Vancouver
Ferreira IM, Yoshioka SA, Comasseto JV, Porto ALM. Immobilization of amano lipase from pseudomonas fluorescens on silk fibroin spheres: an alternative protocol for the enantioselective synthesis of halohydrins [Internet]. RSC Advances. 2017 ; 7 12650-12658.[citado 2024 jul. 31 ] Available from: https://doi.org/10.1039/c7ra00083a
Artigo de periodico
Analysis and characterisation of bovine oocyte and embryo biomarkers by matrix-assisted desorption ionisation mass spectrometry imaging (2016)
Gonçalves, Roseli F; Ferreira, Mônica S; Oliveira, Diogo N. de; Canevarolo, Rafael; Achilles, Marcos A; D’Ercole, Daniela L; Bols, Peter E; Visintin, Jose Antonio; Killian, Gary J; Catharino, Rodrigo R
Fonte: Reproduction, Fertility and Development. Unidade: FMVZ
Assuntos: BOVINOS (EMBRIOLOGIA), EMBRIOLOGIA ANIMAL, ENZIMAS, ESPECTROFOTOMETRIA
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GONÇALVES, Roseli F et al. Analysis and characterisation of bovine oocyte and embryo biomarkers by matrix-assisted desorption ionisation mass spectrometry imaging. Reproduction, Fertility and Development, v. 28, n. 3, p. 293-301, 2016Tradução . . Disponível em: https://doi.org/10.1071/RD14047. Acesso em: 31 jul. 2024.
APA
Gonçalves, R. F., Ferreira, M. S., Oliveira, D. N. de, Canevarolo, R., Achilles, M. A., D’Ercole, D. L., et al. (2016). Analysis and characterisation of bovine oocyte and embryo biomarkers by matrix-assisted desorption ionisation mass spectrometry imaging. Reproduction, Fertility and Development, 28( 3), 293-301. doi:10.1071/RD14047
NLM
Gonçalves RF, Ferreira MS, Oliveira DN de, Canevarolo R, Achilles MA, D’Ercole DL, Bols PE, Visintin JA, Killian GJ, Catharino RR. Analysis and characterisation of bovine oocyte and embryo biomarkers by matrix-assisted desorption ionisation mass spectrometry imaging [Internet]. Reproduction, Fertility and Development. 2016 ; 28( 3): 293-301.[citado 2024 jul. 31 ] Available from: https://doi.org/10.1071/RD14047
Vancouver
Gonçalves RF, Ferreira MS, Oliveira DN de, Canevarolo R, Achilles MA, D’Ercole DL, Bols PE, Visintin JA, Killian GJ, Catharino RR. Analysis and characterisation of bovine oocyte and embryo biomarkers by matrix-assisted desorption ionisation mass spectrometry imaging [Internet]. Reproduction, Fertility and Development. 2016 ; 28( 3): 293-301.[citado 2024 jul. 31 ] Available from: https://doi.org/10.1071/RD14047
Artigo de periodico
Unique behavior of Trypanosoma cruzi mevalonate kinase: a conserved glycosomal enzyme involved in host cell invasion and signaling (2016)
Ferreira, Éden Ramalho; Horjales, Eduardo; Melo, Alexis Bonfim; Cortez, Cristian; Silva, Claudio Vieira da; De Groote, Michel; Sobreira, Tiago José Paschoal; Cruz, Mário Costa; Lima, Fabio Mitsuo; Cordero, Esteban Mauricio; Yoshida, Nobuko; Silveira, José Franco da; Mortara, Renato Arruda; Bahia, Diana
Fonte: Scientific Reports. Unidade: IFSC
Assuntos: TRYPANOSOMA CRUZI, DOENÇA DE CHAGAS, ENZIMAS
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FERREIRA, Éden Ramalho et al. Unique behavior of Trypanosoma cruzi mevalonate kinase: a conserved glycosomal enzyme involved in host cell invasion and signaling. Scientific Reports, v. 6, p. 24610-1-24610-13, 2016Tradução . . Disponível em: https://doi.org/10.1038/srep24610. Acesso em: 31 jul. 2024.
APA
Ferreira, É. R., Horjales, E., Melo, A. B., Cortez, C., Silva, C. V. da, De Groote, M., et al. (2016). Unique behavior of Trypanosoma cruzi mevalonate kinase: a conserved glycosomal enzyme involved in host cell invasion and signaling. Scientific Reports, 6, 24610-1-24610-13. doi:10.1038/srep24610
NLM
Ferreira ÉR, Horjales E, Melo AB, Cortez C, Silva CV da, De Groote M, Sobreira TJP, Cruz MC, Lima FM, Cordero EM, Yoshida N, Silveira JF da, Mortara RA, Bahia D. Unique behavior of Trypanosoma cruzi mevalonate kinase: a conserved glycosomal enzyme involved in host cell invasion and signaling [Internet]. Scientific Reports. 2016 ; 6 24610-1-24610-13.[citado 2024 jul. 31 ] Available from: https://doi.org/10.1038/srep24610
Vancouver
Ferreira ÉR, Horjales E, Melo AB, Cortez C, Silva CV da, De Groote M, Sobreira TJP, Cruz MC, Lima FM, Cordero EM, Yoshida N, Silveira JF da, Mortara RA, Bahia D. Unique behavior of Trypanosoma cruzi mevalonate kinase: a conserved glycosomal enzyme involved in host cell invasion and signaling [Internet]. Scientific Reports. 2016 ; 6 24610-1-24610-13.[citado 2024 jul. 31 ] Available from: https://doi.org/10.1038/srep24610
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
Fonte: Enzyme and Microbial Technology. Unidade: IFSC
Assuntos: ENZIMAS, HIDRÓLISE, ENZIMAS HIDROLÍTICAS
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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: 31 jul. 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 jul. 31 ] 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 jul. 31 ] Available from: https://doi.org/10.1016/j.enzmictec.2016.02.007
Artigo de periodico
Structure of BbKI, a disulfide-free plasma kallikrein inhibitor (2015)
Zhou, Dongwen; Hansen, Daiane; Shabalin, Ivan G.; Gustchina, Alla; Vieira, Debora F.; Brito, Marlon V.; Araújo, Ana Paula Ulian de; Oliva, Maria Luiza V.; Wlodawer, Alexander
Fonte: Acta Crystallographica F. Unidade: IFSC
Assuntos: CRISTALOGRAFIA, ENZIMAS
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ZHOU, Dongwen et al. Structure of BbKI, a disulfide-free plasma kallikrein inhibitor. Acta Crystallographica F, v. 71, p. 1055-1062, 2015Tradução . . Disponível em: https://doi.org/10.1107/S2053230X15011127. Acesso em: 31 jul. 2024.
APA
Zhou, D., Hansen, D., Shabalin, I. G., Gustchina, A., Vieira, D. F., Brito, M. V., et al. (2015). Structure of BbKI, a disulfide-free plasma kallikrein inhibitor. Acta Crystallographica F, 71, 1055-1062. doi:10.1107/S2053230X15011127
NLM
Zhou D, Hansen D, Shabalin IG, Gustchina A, Vieira DF, Brito MV, Araújo APU de, Oliva MLV, Wlodawer A. Structure of BbKI, a disulfide-free plasma kallikrein inhibitor [Internet]. Acta Crystallographica F. 2015 ; 71 1055-1062.[citado 2024 jul. 31 ] Available from: https://doi.org/10.1107/S2053230X15011127
Vancouver
Zhou D, Hansen D, Shabalin IG, Gustchina A, Vieira DF, Brito MV, Araújo APU de, Oliva MLV, Wlodawer A. Structure of BbKI, a disulfide-free plasma kallikrein inhibitor [Internet]. Acta Crystallographica F. 2015 ; 71 1055-1062.[citado 2024 jul. 31 ] Available from: https://doi.org/10.1107/S2053230X15011127
Artigo de periodico
The schistosome esophagus is a 'hotspot' for microexon and lysosomal hydrolase gene expression: implications for blood processing (2015)
Wilson, R. Alan; Li, Xiao Hong; MacDonald, Sandy; Neves, Leandro Xavier; Vitoriano-Souza, Juliana; Leite, Luciana C. C.; Farias, Leonardo P.; James, Sally; Ashton, Peter D.; De Marco, Ricardo; Borges, William Castro
Fonte: PLOS Neglected Tropical Diseases. Unidade: IFSC
Assuntos: ESQUISTOSSOMOSE, SCHISTOSOMA MANSONI, EXPRESSÃO GÊNICA, ENZIMAS, SANGUE
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WILSON, R. Alan et al. The schistosome esophagus is a 'hotspot' for microexon and lysosomal hydrolase gene expression: implications for blood processing. PLOS Neglected Tropical Diseases, v. 9, n. 12, p. e0004272-1-e0004272-25, 2015Tradução . . Disponível em: https://doi.org/10.1371/journal.pntd.0004272. Acesso em: 31 jul. 2024.
APA
Wilson, R. A., Li, X. H., MacDonald, S., Neves, L. X., Vitoriano-Souza, J., Leite, L. C. C., et al. (2015). The schistosome esophagus is a 'hotspot' for microexon and lysosomal hydrolase gene expression: implications for blood processing. PLOS Neglected Tropical Diseases, 9( 12), e0004272-1-e0004272-25. doi:10.1371/journal.pntd.0004272
NLM
Wilson RA, Li XH, MacDonald S, Neves LX, Vitoriano-Souza J, Leite LCC, Farias LP, James S, Ashton PD, De Marco R, Borges WC. The schistosome esophagus is a 'hotspot' for microexon and lysosomal hydrolase gene expression: implications for blood processing [Internet]. PLOS Neglected Tropical Diseases. 2015 ; 9( 12): e0004272-1-e0004272-25.[citado 2024 jul. 31 ] Available from: https://doi.org/10.1371/journal.pntd.0004272
Vancouver
Wilson RA, Li XH, MacDonald S, Neves LX, Vitoriano-Souza J, Leite LCC, Farias LP, James S, Ashton PD, De Marco R, Borges WC. The schistosome esophagus is a 'hotspot' for microexon and lysosomal hydrolase gene expression: implications for blood processing [Internet]. PLOS Neglected Tropical Diseases. 2015 ; 9( 12): e0004272-1-e0004272-25.[citado 2024 jul. 31 ] Available from: https://doi.org/10.1371/journal.pntd.0004272
Artigo de periodico
Tuning structural changes in glucose oxidase for enzyme fuel cell applications (2015)
Mecheri, Barbara; Porcellinis, Diana De; Campana, Patrícia Targon; Rainer, Alberto; Trombetta, Marcella; Marletta, Alexandre; Oliveira Junior, Osvaldo Novais de; Licoccia, Silvia
Fonte: ACS Applied Materials and Interfaces. Unidades: EACH, IFSC
Assuntos: ENZIMAS, CÉLULAS A COMBUSTÍVEL
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ABNT
MECHERI, Barbara et al. Tuning structural changes in glucose oxidase for enzyme fuel cell applications. ACS Applied Materials and Interfaces, v. 7, n. 51, p. 28311-28318, 2015Tradução . . Disponível em: https://doi.org/10.1021/acsami.5b08610. Acesso em: 31 jul. 2024.
APA
Mecheri, B., Porcellinis, D. D., Campana, P. T., Rainer, A., Trombetta, M., Marletta, A., et al. (2015). Tuning structural changes in glucose oxidase for enzyme fuel cell applications. ACS Applied Materials and Interfaces, 7( 51), 28311-28318. doi:10.1021/acsami.5b08610
NLM
Mecheri B, Porcellinis DD, Campana PT, Rainer A, Trombetta M, Marletta A, Oliveira Junior ON de, Licoccia S. Tuning structural changes in glucose oxidase for enzyme fuel cell applications [Internet]. ACS Applied Materials and Interfaces. 2015 ; 7( 51): 28311-28318.[citado 2024 jul. 31 ] Available from: https://doi.org/10.1021/acsami.5b08610
Vancouver
Mecheri B, Porcellinis DD, Campana PT, Rainer A, Trombetta M, Marletta A, Oliveira Junior ON de, Licoccia S. Tuning structural changes in glucose oxidase for enzyme fuel cell applications [Internet]. ACS Applied Materials and Interfaces. 2015 ; 7( 51): 28311-28318.[citado 2024 jul. 31 ] Available from: https://doi.org/10.1021/acsami.5b08610
Artigo de periodico
Interactions of bioactive molecules and nanomaterials with Langmuir monolayers as cell membrane models (2015)
Nobre, Thatyane M.; Pavinatto, Felippe José; Caseli, Luciano; Barros-Timmons, Ana; Dynarowicz-Łątka, Patrycja; Oliveira Junior, Osvaldo Novais de
Fonte: Thin Solid Films. Unidade: IFSC
Assuntos: PEPTÍDEOS, ENZIMAS, LIPÍDEOS, FILMES FINOS, NANOPARTÍCULAS
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ABNT
NOBRE, Thatyane M. et al. Interactions of bioactive molecules and nanomaterials with Langmuir monolayers as cell membrane models. Thin Solid Films, v. 593, p. 159-188, 2015Tradução . . Disponível em: https://doi.org/10.1016/j.tsf.2015.09.047. Acesso em: 31 jul. 2024.
APA
Nobre, T. M., Pavinatto, F. J., Caseli, L., Barros-Timmons, A., Dynarowicz-Łątka, P., & Oliveira Junior, O. N. de. (2015). Interactions of bioactive molecules and nanomaterials with Langmuir monolayers as cell membrane models. Thin Solid Films, 593, 159-188. doi:10.1016/j.tsf.2015.09.047
NLM
Nobre TM, Pavinatto FJ, Caseli L, Barros-Timmons A, Dynarowicz-Łątka P, Oliveira Junior ON de. Interactions of bioactive molecules and nanomaterials with Langmuir monolayers as cell membrane models [Internet]. Thin Solid Films. 2015 ; 593 159-188.[citado 2024 jul. 31 ] Available from: https://doi.org/10.1016/j.tsf.2015.09.047
Vancouver
Nobre TM, Pavinatto FJ, Caseli L, Barros-Timmons A, Dynarowicz-Łątka P, Oliveira Junior ON de. Interactions of bioactive molecules and nanomaterials with Langmuir monolayers as cell membrane models [Internet]. Thin Solid Films. 2015 ; 593 159-188.[citado 2024 jul. 31 ] Available from: https://doi.org/10.1016/j.tsf.2015.09.047
Artigo de periodico
N-terminal microdomain peptide from human dihydroorotate dehydrogenase: structure and model membrane interactions (2015)
Vicente, Eduardo F.; Nobre-Pavinatto, T. M.; Pavinatto, Felippe José; Oliveira Junior, Osvaldo Novais de; Costa Filho, Antônio José da; Cilli, Eduardo M.
Fonte: Protein and Peptide Letters. Unidades: IFSC, FFCLRP
Assuntos: PEPTÍDEOS, ENZIMAS, LIPÍDEOS
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ABNT
VICENTE, Eduardo F. et al. N-terminal microdomain peptide from human dihydroorotate dehydrogenase: structure and model membrane interactions. Protein and Peptide Letters, v. 22, n. 2, p. 119-129 + supplementary materials: i-iii, 2015Tradução . . Disponível em: https://doi.org/10.2174/0929866521666140508125215. Acesso em: 31 jul. 2024.
APA
Vicente, E. F., Nobre-Pavinatto, T. M., Pavinatto, F. J., Oliveira Junior, O. N. de, Costa Filho, A. J. da, & Cilli, E. M. (2015). N-terminal microdomain peptide from human dihydroorotate dehydrogenase: structure and model membrane interactions. Protein and Peptide Letters, 22( 2), 119-129 + supplementary materials: i-iii. doi:10.2174/0929866521666140508125215
NLM
Vicente EF, Nobre-Pavinatto TM, Pavinatto FJ, Oliveira Junior ON de, Costa Filho AJ da, Cilli EM. N-terminal microdomain peptide from human dihydroorotate dehydrogenase: structure and model membrane interactions [Internet]. Protein and Peptide Letters. 2015 ; 22( 2): 119-129 + supplementary materials: i-iii.[citado 2024 jul. 31 ] Available from: https://doi.org/10.2174/0929866521666140508125215
Vancouver
Vicente EF, Nobre-Pavinatto TM, Pavinatto FJ, Oliveira Junior ON de, Costa Filho AJ da, Cilli EM. N-terminal microdomain peptide from human dihydroorotate dehydrogenase: structure and model membrane interactions [Internet]. Protein and Peptide Letters. 2015 ; 22( 2): 119-129 + supplementary materials: i-iii.[citado 2024 jul. 31 ] Available from: https://doi.org/10.2174/0929866521666140508125215
Artigo de periodico
Fragment-based QSAR and structural analysis of a series of hydroxyethylamine derivatives as HIV-1 protease inhibitors (2015)
Ferreira, Leonardo Luiz Gomes; Andricopulo, Adriano Defini
Fonte: Combinatorial Chemistry and High Troughput Screening. Unidade: IFSC
Assuntos: HIV, SÍNDROME DE IMUNODEFICIÊNCIA ADQUIRIDA, HOLOGRAMAS, MODELAGEM MOLECULAR, ENZIMAS
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ABNT
FERREIRA, Leonardo Luiz Gomes e ANDRICOPULO, Adriano Defini. Fragment-based QSAR and structural analysis of a series of hydroxyethylamine derivatives as HIV-1 protease inhibitors. Combinatorial Chemistry and High Troughput Screening, v. 18, n. 5, p. 464-475, 2015Tradução . . Disponível em: https://doi.org/10.2174/1386207318666150508095331. Acesso em: 31 jul. 2024.
APA
Ferreira, L. L. G., & Andricopulo, A. D. (2015). Fragment-based QSAR and structural analysis of a series of hydroxyethylamine derivatives as HIV-1 protease inhibitors. Combinatorial Chemistry and High Troughput Screening, 18( 5), 464-475. doi:10.2174/1386207318666150508095331
NLM
Ferreira LLG, Andricopulo AD. Fragment-based QSAR and structural analysis of a series of hydroxyethylamine derivatives as HIV-1 protease inhibitors [Internet]. Combinatorial Chemistry and High Troughput Screening. 2015 ; 18( 5): 464-475.[citado 2024 jul. 31 ] Available from: https://doi.org/10.2174/1386207318666150508095331
Vancouver
Ferreira LLG, Andricopulo AD. Fragment-based QSAR and structural analysis of a series of hydroxyethylamine derivatives as HIV-1 protease inhibitors [Internet]. Combinatorial Chemistry and High Troughput Screening. 2015 ; 18( 5): 464-475.[citado 2024 jul. 31 ] Available from: https://doi.org/10.2174/1386207318666150508095331
Artigo de periodico
Isolation and characterization of a β-galactosidase from a new Amazon forest strain of Aspergillus niger as a potential accessory enzyme for biomass conversion (2014)
Tonelotto, Mariana; Pirota, Rosangela Donizete Perpetua Buzon; Delabona, Priscila da Silva; Barros, Georgia de Oliveira Figueiredo; Golubev, Alexander M.; Polikarpov, Igor; Farinas, Cristiane Sanchez
Fonte: Biocatalysis and Biotransformation. Unidade: IFSC
Assuntos: ENZIMAS, DIFRAÇÃO POR RAIOS X, BIOMASSA, ASPERGILLUS (ESTUDO)
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ABNT
TONELOTTO, Mariana et al. Isolation and characterization of a β-galactosidase from a new Amazon forest strain of Aspergillus niger as a potential accessory enzyme for biomass conversion. Biocatalysis and Biotransformation, v. 32, n. 1, p. 13-22, 2014Tradução . . Disponível em: https://doi.org/10.3109/10242422.2013.801018. Acesso em: 31 jul. 2024.
APA
Tonelotto, M., Pirota, R. D. P. B., Delabona, P. da S., Barros, G. de O. F., Golubev, A. M., Polikarpov, I., & Farinas, C. S. (2014). Isolation and characterization of a β-galactosidase from a new Amazon forest strain of Aspergillus niger as a potential accessory enzyme for biomass conversion. Biocatalysis and Biotransformation, 32( 1), 13-22. doi:10.3109/10242422.2013.801018
NLM
Tonelotto M, Pirota RDPB, Delabona P da S, Barros G de OF, Golubev AM, Polikarpov I, Farinas CS. Isolation and characterization of a β-galactosidase from a new Amazon forest strain of Aspergillus niger as a potential accessory enzyme for biomass conversion [Internet]. Biocatalysis and Biotransformation. 2014 ; 32( 1): 13-22.[citado 2024 jul. 31 ] Available from: https://doi.org/10.3109/10242422.2013.801018
Vancouver
Tonelotto M, Pirota RDPB, Delabona P da S, Barros G de OF, Golubev AM, Polikarpov I, Farinas CS. Isolation and characterization of a β-galactosidase from a new Amazon forest strain of Aspergillus niger as a potential accessory enzyme for biomass conversion [Internet]. Biocatalysis and Biotransformation. 2014 ; 32( 1): 13-22.[citado 2024 jul. 31 ] Available from: https://doi.org/10.3109/10242422.2013.801018
Artigo de periodico
Control of KirBac3.1 potassium channel gating at the interface between cytoplasmic domains (2014)
Zubcevic, Lejla; Bavro, Vassiliy N.; Muniz, João Renato Carvalho; Schmidt, Matthias R.; Wang, Shizhen; De Zorzi, Rita; Venien-Bryan, Catherine; Sansom, Mark S. P.; Nichols, Colin G.; Tucker, Stephen J.
Fonte: Journal of Biological Chemistry. Unidade: IFSC
Assuntos: ENZIMAS, BIOQUÍMICA
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ABNT
ZUBCEVIC, Lejla et al. Control of KirBac3.1 potassium channel gating at the interface between cytoplasmic domains. Journal of Biological Chemistry, v. 289, n. Ja 2014, p. 143-151, 2014Tradução . . Disponível em: https://doi.org/10.1074/jbc.M113.501833. Acesso em: 31 jul. 2024.
APA
Zubcevic, L., Bavro, V. N., Muniz, J. R. C., Schmidt, M. R., Wang, S., De Zorzi, R., et al. (2014). Control of KirBac3.1 potassium channel gating at the interface between cytoplasmic domains. Journal of Biological Chemistry, 289( Ja 2014), 143-151. doi:10.1074/jbc.M113.501833
NLM
Zubcevic L, Bavro VN, Muniz JRC, Schmidt MR, Wang S, De Zorzi R, Venien-Bryan C, Sansom MSP, Nichols CG, Tucker SJ. Control of KirBac3.1 potassium channel gating at the interface between cytoplasmic domains [Internet]. Journal of Biological Chemistry. 2014 ; 289( Ja 2014): 143-151.[citado 2024 jul. 31 ] Available from: https://doi.org/10.1074/jbc.M113.501833
Vancouver
Zubcevic L, Bavro VN, Muniz JRC, Schmidt MR, Wang S, De Zorzi R, Venien-Bryan C, Sansom MSP, Nichols CG, Tucker SJ. Control of KirBac3.1 potassium channel gating at the interface between cytoplasmic domains [Internet]. Journal of Biological Chemistry. 2014 ; 289( Ja 2014): 143-151.[citado 2024 jul. 31 ] Available from: https://doi.org/10.1074/jbc.M113.501833
Artigo de periodico
Nanobiosensors exploiting specific interactions between an enzyme and herbicides in atomic force spectroscopy (2014)
Silva, Aline C. N.; Deda, Daiana K.; Bueno, Carolina C.; Moraes, Ariana S.; Da Roz, Alessandra L.; Yamaji, Fabio M.; Prado, Rogilene A.; Viviani, Vadim; Oliveira Junior, Osvaldo Novais de; Leite, Fábio L.
Fonte: Journal of Nanoscience and Nanotechnology. Unidade: IFSC
Assuntos: SENSOR, NANOTECNOLOGIA, ENZIMAS, HERBICIDAS
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ABNT
SILVA, Aline C. N. et al. Nanobiosensors exploiting specific interactions between an enzyme and herbicides in atomic force spectroscopy. Journal of Nanoscience and Nanotechnology, v. 14, n. 9, p. 6678-6684, 2014Tradução . . Disponível em: https://doi.org/10.1166/jnn.2014.9360. Acesso em: 31 jul. 2024.
APA
Silva, A. C. N., Deda, D. K., Bueno, C. C., Moraes, A. S., Da Roz, A. L., Yamaji, F. M., et al. (2014). Nanobiosensors exploiting specific interactions between an enzyme and herbicides in atomic force spectroscopy. Journal of Nanoscience and Nanotechnology, 14( 9), 6678-6684. doi:10.1166/jnn.2014.9360
NLM
Silva ACN, Deda DK, Bueno CC, Moraes AS, Da Roz AL, Yamaji FM, Prado RA, Viviani V, Oliveira Junior ON de, Leite FL. Nanobiosensors exploiting specific interactions between an enzyme and herbicides in atomic force spectroscopy [Internet]. Journal of Nanoscience and Nanotechnology. 2014 ; 14( 9): 6678-6684.[citado 2024 jul. 31 ] Available from: https://doi.org/10.1166/jnn.2014.9360
Vancouver
Silva ACN, Deda DK, Bueno CC, Moraes AS, Da Roz AL, Yamaji FM, Prado RA, Viviani V, Oliveira Junior ON de, Leite FL. Nanobiosensors exploiting specific interactions between an enzyme and herbicides in atomic force spectroscopy [Internet]. Journal of Nanoscience and Nanotechnology. 2014 ; 14( 9): 6678-6684.[citado 2024 jul. 31 ] Available from: https://doi.org/10.1166/jnn.2014.9360
Artigo de periodico
Insights into the structure and function of fungal β-mannosidases from glycoside hydrolase family 2 based on multiple crystal structures of the Trichoderma harzianum enzyme (2014)
Nascimento, Alessandro Silva; Muniz, João Renato Carvalho; Aparício, Ricardo; Golubev, Alexander M.; Polikarpov, Igor
Fonte: FEBS Journal. Unidade: IFSC
Assuntos: TRICHODERMA (ESTUDO), ENZIMAS, HIDRÓLISE
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ABNT
NASCIMENTO, Alessandro Silva et al. Insights into the structure and function of fungal β-mannosidases from glycoside hydrolase family 2 based on multiple crystal structures of the Trichoderma harzianum enzyme. FEBS Journal, v. 281, n. 18, p. 4165-4178, 2014Tradução . . Disponível em: https://doi.org/10.1111/febs.12894. Acesso em: 31 jul. 2024.
APA
Nascimento, A. S., Muniz, J. R. C., Aparício, R., Golubev, A. M., & Polikarpov, I. (2014). Insights into the structure and function of fungal β-mannosidases from glycoside hydrolase family 2 based on multiple crystal structures of the Trichoderma harzianum enzyme. FEBS Journal, 281( 18), 4165-4178. doi:10.1111/febs.12894
NLM
Nascimento AS, Muniz JRC, Aparício R, Golubev AM, Polikarpov I. Insights into the structure and function of fungal β-mannosidases from glycoside hydrolase family 2 based on multiple crystal structures of the Trichoderma harzianum enzyme [Internet]. FEBS Journal. 2014 ; 281( 18): 4165-4178.[citado 2024 jul. 31 ] Available from: https://doi.org/10.1111/febs.12894
Vancouver
Nascimento AS, Muniz JRC, Aparício R, Golubev AM, Polikarpov I. Insights into the structure and function of fungal β-mannosidases from glycoside hydrolase family 2 based on multiple crystal structures of the Trichoderma harzianum enzyme [Internet]. FEBS Journal. 2014 ; 281( 18): 4165-4178.[citado 2024 jul. 31 ] Available from: https://doi.org/10.1111/febs.12894
Artigo de periodico
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 (2014)
Miotto, Lis S.; Reis, Caio V.; Oliveira Neto, Mario de; Polikarpov, Igor
Fonte: Materials. Unidade: IFSC
Assuntos: BIOFÍSICA, FUNGOS, ENZIMAS
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
ABNT
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: 31 jul. 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 jul. 31 ] 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 jul. 31 ] Available from: https://doi.org/10.3390/ma7075202
Artigo de periodico
Expression, purification, crystallization and preliminary X-ray diffraction analysis of the pectin methylesterase from the sugar cane weevil Sphenophorus levis (2014)
Evangelista, Danilo Elton; Godoy, Andre Schutzer de; Paula, Fernando Fonseca Pereira de; Silva, Flavio Henrique; Polikarpov, Igor
Fonte: Acta Crystallographica F. Unidade: IFSC
Assuntos: ENZIMAS, DIFRAÇÃO POR RAIOS X
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ABNT
EVANGELISTA, Danilo Elton et al. Expression, purification, crystallization and preliminary X-ray diffraction analysis of the pectin methylesterase from the sugar cane weevil Sphenophorus levis. Acta Crystallographica F, v. 70, p. 331-334, 2014Tradução . . Disponível em: https://doi.org/10.1107/S2053230X14001630. Acesso em: 31 jul. 2024.
APA
Evangelista, D. E., Godoy, A. S. de, Paula, F. F. P. de, Silva, F. H., & Polikarpov, I. (2014). Expression, purification, crystallization and preliminary X-ray diffraction analysis of the pectin methylesterase from the sugar cane weevil Sphenophorus levis. Acta Crystallographica F, 70, 331-334. doi:10.1107/S2053230X14001630
NLM
Evangelista DE, Godoy AS de, Paula FFP de, Silva FH, Polikarpov I. Expression, purification, crystallization and preliminary X-ray diffraction analysis of the pectin methylesterase from the sugar cane weevil Sphenophorus levis [Internet]. Acta Crystallographica F. 2014 ; 70 331-334.[citado 2024 jul. 31 ] Available from: https://doi.org/10.1107/S2053230X14001630
Vancouver
Evangelista DE, Godoy AS de, Paula FFP de, Silva FH, Polikarpov I. Expression, purification, crystallization and preliminary X-ray diffraction analysis of the pectin methylesterase from the sugar cane weevil Sphenophorus levis [Internet]. Acta Crystallographica F. 2014 ; 70 331-334.[citado 2024 jul. 31 ] Available from: https://doi.org/10.1107/S2053230X14001630
Artigo de periodico
High-throughput cloning, expression and purification of glycoside hydrolases using Ligation-Independent Cloning (LIC) (2014)
Camilo, Cesar M.; Polikarpov, Igor
Fonte: Protein Expression and Purification. Unidade: IFSC
Assuntos: CLONAGEM, ENZIMAS, PROTEÍNAS (CARACTERÍSTICAS)
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
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: 31 jul. 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 jul. 31 ] 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 jul. 31 ] Available from: https://doi.org/10.1016/j.pep.2014.03.008
Artigo de periodico
Transcriptome profile of Trichoderma harzianum IOC- 3844 induced by sugarcane bagasse (2014)
Horta, Maria Augusta Crivelente; Vicentini, Renato; Delabona, Priscila da Silva; Laborda, Prianda; Crucello, Aline; Freitas, Sindélia; Kuroshu, Reginaldo Massanobu; Polikarpov, Igor; Pradella, José Geraldo da Cruz; Souza, Anete Pereira
Fonte: PLOS ONE. Unidade: IFSC
Assuntos: ENZIMAS, FUNGOS, GENES, CANA-DE-AÇÚCAR, BAGAÇOS, BIOMASSA
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
ABNT
HORTA, Maria Augusta Crivelente et al. Transcriptome profile of Trichoderma harzianum IOC- 3844 induced by sugarcane bagasse. PLOS ONE, v. 9, n. 2, p. e88689-1-ee88689-17, 2014Tradução . . Disponível em: https://doi.org/10.1371/journal.pone.0088689. Acesso em: 31 jul. 2024.
APA
Horta, M. A. C., Vicentini, R., Delabona, P. da S., Laborda, P., Crucello, A., Freitas, S., et al. (2014). Transcriptome profile of Trichoderma harzianum IOC- 3844 induced by sugarcane bagasse. PLOS ONE, 9( 2), e88689-1-ee88689-17. doi:10.1371/journal.pone.0088689
NLM
Horta MAC, Vicentini R, Delabona P da S, Laborda P, Crucello A, Freitas S, Kuroshu RM, Polikarpov I, Pradella JG da C, Souza AP. Transcriptome profile of Trichoderma harzianum IOC- 3844 induced by sugarcane bagasse [Internet]. PLOS ONE. 2014 ; 9( 2): e88689-1-ee88689-17.[citado 2024 jul. 31 ] Available from: https://doi.org/10.1371/journal.pone.0088689
Vancouver
Horta MAC, Vicentini R, Delabona P da S, Laborda P, Crucello A, Freitas S, Kuroshu RM, Polikarpov I, Pradella JG da C, Souza AP. Transcriptome profile of Trichoderma harzianum IOC- 3844 induced by sugarcane bagasse [Internet]. PLOS ONE. 2014 ; 9( 2): e88689-1-ee88689-17.[citado 2024 jul. 31 ] Available from: https://doi.org/10.1371/journal.pone.0088689
Artigo de periodico
Deconstructing the DGAT1 enzyme: binding sites and substrate interactions (2014)
Lopes, José L. S.; Nobre, Thatyane M.; Cilli, Eduardo M.; Beltramini, Leila Maria; Araújo, Ana Paula Ulian de; Wallace, B. A.
Fonte: Biochimica et Biophysica Acta : Proteins and Proteomics. Unidade: IFSC
Assuntos: ENZIMAS, FILMES FINOS, ESPECTROSCOPIA
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
ABNT
LOPES, José L. S. et al. Deconstructing the DGAT1 enzyme: binding sites and substrate interactions. Biochimica et Biophysica Acta : Proteins and Proteomics, v. 1838, n. 12, p. 3145-3152, 2014Tradução . . Disponível em: https://doi.org/10.1016/j.bbamem.2014.08.017. Acesso em: 31 jul. 2024.
APA
Lopes, J. L. S., Nobre, T. M., Cilli, E. M., Beltramini, L. M., Araújo, A. P. U. de, & Wallace, B. A. (2014). Deconstructing the DGAT1 enzyme: binding sites and substrate interactions. Biochimica et Biophysica Acta : Proteins and Proteomics, 1838( 12), 3145-3152. doi:10.1016/j.bbamem.2014.08.017
NLM
Lopes JLS, Nobre TM, Cilli EM, Beltramini LM, Araújo APU de, Wallace BA. Deconstructing the DGAT1 enzyme: binding sites and substrate interactions [Internet]. Biochimica et Biophysica Acta : Proteins and Proteomics. 2014 ; 1838( 12): 3145-3152.[citado 2024 jul. 31 ] Available from: https://doi.org/10.1016/j.bbamem.2014.08.017
Vancouver
Lopes JLS, Nobre TM, Cilli EM, Beltramini LM, Araújo APU de, Wallace BA. Deconstructing the DGAT1 enzyme: binding sites and substrate interactions [Internet]. Biochimica et Biophysica Acta : Proteins and Proteomics. 2014 ; 1838( 12): 3145-3152.[citado 2024 jul. 31 ] Available from: https://doi.org/10.1016/j.bbamem.2014.08.017
Artigo de periodico
Enzymatic and structural characterization of rTSγ provides insights into the function of rTSβ (2014)
Wichelecki, Daniel J.; Froese, D. Sean; Kopec, Jolanta; Muniz, João Renato Carvalho; Yue, Wyatt W.; Gerlt, John A.
Fonte: Biochemistry. Unidade: IFSC
Assuntos: ENZIMAS, BIOQUÍMICA
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
ABNT
WICHELECKI, Daniel J. et al. Enzymatic and structural characterization of rTSγ provides insights into the function of rTSβ. Biochemistry, v. 53, n. 16, p. 2732-2738, 2014Tradução . . Disponível em: https://doi.org/10.1021/bi500349e. Acesso em: 31 jul. 2024.
APA
Wichelecki, D. J., Froese, D. S., Kopec, J., Muniz, J. R. C., Yue, W. W., & Gerlt, J. A. (2014). Enzymatic and structural characterization of rTSγ provides insights into the function of rTSβ. Biochemistry, 53( 16), 2732-2738. doi:10.1021/bi500349e
NLM
Wichelecki DJ, Froese DS, Kopec J, Muniz JRC, Yue WW, Gerlt JA. Enzymatic and structural characterization of rTSγ provides insights into the function of rTSβ [Internet]. Biochemistry. 2014 ; 53( 16): 2732-2738.[citado 2024 jul. 31 ] Available from: https://doi.org/10.1021/bi500349e
Vancouver
Wichelecki DJ, Froese DS, Kopec J, Muniz JRC, Yue WW, Gerlt JA. Enzymatic and structural characterization of rTSγ provides insights into the function of rTSβ [Internet]. Biochemistry. 2014 ; 53( 16): 2732-2738.[citado 2024 jul. 31 ] Available from: https://doi.org/10.1021/bi500349e

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