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Artigo de periodico
Unravelling biochemical and structural features of bacillus licheniformis GH5 mannanase using site-directed mutagenesis and high-resolution protein crystallography studies (2024)
Briganti, Lorenzo; Manzine, Livia Regina ; Capetti, Caio Cesar de Mello ; Araújo, Evandro Ares de ; Pellegrini, Vanessa de Oliveira Arnoldi ; Guimarães, Francisco Eduardo Gontijo ; Oliveira Neto, Mario de; Polikarpov, Igor
Source: International Journal of Biological Macromolecules. Unidade: IFSC
Subjects: AÇUCARES, ENZIMAS, BIOTECNOLOGIA, CRISTALOGRAFIA ESTRUTURAL
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ABNT
BRIGANTI, Lorenzo et al. Unravelling biochemical and structural features of bacillus licheniformis GH5 mannanase using site-directed mutagenesis and high-resolution protein crystallography studies. International Journal of Biological Macromolecules, v. 274, p. 133182-1-133182-16 + supplementary data, 2024Tradução . . Disponível em: https://doi.org/10.1016/j.ijbiomac.2024.133182. Acesso em: 13 set. 2024.
APA
Briganti, L., Manzine, L. R., Capetti, C. C. de M., Araújo, E. A. de, Pellegrini, V. de O. A., Guimarães, F. E. G., et al. (2024). Unravelling biochemical and structural features of bacillus licheniformis GH5 mannanase using site-directed mutagenesis and high-resolution protein crystallography studies. International Journal of Biological Macromolecules, 274, 133182-1-133182-16 + supplementary data. doi:10.1016/j.ijbiomac.2024.133182
NLM
Briganti L, Manzine LR, Capetti CC de M, Araújo EA de, Pellegrini V de OA, Guimarães FEG, Oliveira Neto M de, Polikarpov I. Unravelling biochemical and structural features of bacillus licheniformis GH5 mannanase using site-directed mutagenesis and high-resolution protein crystallography studies [Internet]. International Journal of Biological Macromolecules. 2024 ; 274 133182-1-133182-16 + supplementary data.[citado 2024 set. 13 ] Available from: https://doi.org/10.1016/j.ijbiomac.2024.133182
Vancouver
Briganti L, Manzine LR, Capetti CC de M, Araújo EA de, Pellegrini V de OA, Guimarães FEG, Oliveira Neto M de, Polikarpov I. Unravelling biochemical and structural features of bacillus licheniformis GH5 mannanase using site-directed mutagenesis and high-resolution protein crystallography studies [Internet]. International Journal of Biological Macromolecules. 2024 ; 274 133182-1-133182-16 + supplementary data.[citado 2024 set. 13 ] Available from: https://doi.org/10.1016/j.ijbiomac.2024.133182
Artigo de periodico
SAXSMoW 3.0: new advances in the determination of the molecular weight of proteins in dilute solutions from SAXS intensity data on a relative scale (2022)
Oliveira Neto, Mario de; Fernandes, Adriano de Freitas; Piiadov, Vassili; Craievich, Aldo Felix ; Araújo, Evandro Ares de; Polikarpov, Igor
Source: Protein Science. Unidades: IF, IFSC
Subjects: ESPALHAMENTO DE RAIOS X A BAIXOS ÂNGULOS, PESO MOLECULAR, PROTEÍNAS
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ABNT
OLIVEIRA NETO, Mario de et al. SAXSMoW 3.0: new advances in the determination of the molecular weight of proteins in dilute solutions from SAXS intensity data on a relative scale. Protein Science, v. 31, n. Ja 2022, p. 251-258 + supporting information: 1-3, 2022Tradução . . Disponível em: https://doi.org/10.1002/pro.4227. Acesso em: 13 set. 2024.
APA
Oliveira Neto, M. de, Fernandes, A. de F., Piiadov, V., Craievich, A. F., Araújo, E. A. de, & Polikarpov, I. (2022). SAXSMoW 3.0: new advances in the determination of the molecular weight of proteins in dilute solutions from SAXS intensity data on a relative scale. Protein Science, 31( Ja 2022), 251-258 + supporting information: 1-3. doi:10.1002/pro.4227
NLM
Oliveira Neto M de, Fernandes A de F, Piiadov V, Craievich AF, Araújo EA de, Polikarpov I. SAXSMoW 3.0: new advances in the determination of the molecular weight of proteins in dilute solutions from SAXS intensity data on a relative scale [Internet]. Protein Science. 2022 ; 31( Ja 2022): 251-258 + supporting information: 1-3.[citado 2024 set. 13 ] Available from: https://doi.org/10.1002/pro.4227
Vancouver
Oliveira Neto M de, Fernandes A de F, Piiadov V, Craievich AF, Araújo EA de, Polikarpov I. SAXSMoW 3.0: new advances in the determination of the molecular weight of proteins in dilute solutions from SAXS intensity data on a relative scale [Internet]. Protein Science. 2022 ; 31( Ja 2022): 251-258 + supporting information: 1-3.[citado 2024 set. 13 ] Available from: https://doi.org/10.1002/pro.4227
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: 13 set. 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 set. 13 ] 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 set. 13 ] 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
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
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: 13 set. 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 set. 13 ] 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 set. 13 ] Available from: https://doi.org/10.1016/j.enzmictec.2016.02.007

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