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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: 08 jul. 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 jul. 08 ] 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 jul. 08 ] Available from: https://doi.org/10.1002/pro.4227
Artigo de periodico
SAXSMoW 2.0: online calculator of the molecular weight of proteins in dilute solution from experimental SAXS data measured on a relative scale (2019)
Piiadov, Vassili; Araújo, Evandro Ares de; Oliveira Neto, Mario; Craievich, Aldo Felix; Polikarpov, Igor
Source: Protein Science. Unidades: IF, IFSC
Subjects: PESO MOLECULAR, PROTEÍNAS, ESPALHAMENTO DE RAIOS X A BAIXOS ÂNGULOS
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ABNT
PIIADOV, Vassili et al. SAXSMoW 2.0: online calculator of the molecular weight of proteins in dilute solution from experimental SAXS data measured on a relative scale. Protein Science, v. 28, n. 2, p. 454-463, 2019Tradução . . Disponível em: https://doi.org/10.1002/pro.3528. Acesso em: 08 jul. 2024.
APA
Piiadov, V., Araújo, E. A. de, Oliveira Neto, M., Craievich, A. F., & Polikarpov, I. (2019). SAXSMoW 2.0: online calculator of the molecular weight of proteins in dilute solution from experimental SAXS data measured on a relative scale. Protein Science, 28( 2), 454-463. doi:10.1002/pro.3528
NLM
Piiadov V, Araújo EA de, Oliveira Neto M, Craievich AF, Polikarpov I. SAXSMoW 2.0: online calculator of the molecular weight of proteins in dilute solution from experimental SAXS data measured on a relative scale [Internet]. Protein Science. 2019 ; 28( 2): 454-463.[citado 2024 jul. 08 ] Available from: https://doi.org/10.1002/pro.3528
Vancouver
Piiadov V, Araújo EA de, Oliveira Neto M, Craievich AF, Polikarpov I. SAXSMoW 2.0: online calculator of the molecular weight of proteins in dilute solution from experimental SAXS data measured on a relative scale [Internet]. Protein Science. 2019 ; 28( 2): 454-463.[citado 2024 jul. 08 ] Available from: https://doi.org/10.1002/pro.3528
Trabalho de evento-resumo periodico
Functional sectors involved in thermal stability and activity in beta-glucosidases (2014)
Tamaki, Fabio K.; Textor, Larissa C.; Polikarpov, Igor; Marana, Sandro Roberto
Source: Protein Science. Conference titles: Annual Symposium of the Protein Society. Unidades: IFSC, IQ
Subjects: ENZIMAS, TEMPERATURA
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ABNT
TAMAKI, Fabio K. et al. Functional sectors involved in thermal stability and activity in beta-glucosidases. Protein Science. Hoboken: Wiley-Blackwell. Disponível em: https://doi.org/10.1002/pro.2504. Acesso em: 08 jul. 2024. , 2014
APA
Tamaki, F. K., Textor, L. C., Polikarpov, I., & Marana, S. R. (2014). Functional sectors involved in thermal stability and activity in beta-glucosidases. Protein Science. Hoboken: Wiley-Blackwell. doi:10.1002/pro.2504
NLM
Tamaki FK, Textor LC, Polikarpov I, Marana SR. Functional sectors involved in thermal stability and activity in beta-glucosidases [Internet]. Protein Science. 2014 ; 23( S1): 190-191.[citado 2024 jul. 08 ] Available from: https://doi.org/10.1002/pro.2504
Vancouver
Tamaki FK, Textor LC, Polikarpov I, Marana SR. Functional sectors involved in thermal stability and activity in beta-glucosidases [Internet]. Protein Science. 2014 ; 23( S1): 190-191.[citado 2024 jul. 08 ] Available from: https://doi.org/10.1002/pro.2504
Artigo de periodico
Orphan nuclear receptor NGFI-B forms dimers with nonclassical interface (2007)
Calgaro, Marcos R.; Oliveira Neto, Mario de; Figueira, Ana Carolina Migliorini; Santos, Maria A. M.; Portugal, Rodrigo Villares; Guzzi, Carolina Aparecida de; Saidemberg, Daniel Menezes; Bleicher, Lucas; Vernal, Javier; Fernandez, Pablo; Terenzi, Hernán; Palma, Mario Sergio; Polikarpov, Igor
Source: Protein Science. Unidade: IFSC
Subjects: CRISTALOGRAFIA, RAIOS X, DNA
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ABNT
CALGARO, Marcos R. et al. Orphan nuclear receptor NGFI-B forms dimers with nonclassical interface. Protein Science, v. 16, n. 8, p. 1762-1772, 2007Tradução . . Disponível em: https://doi.org/10.1110/ps.062692207. Acesso em: 08 jul. 2024.
APA
Calgaro, M. R., Oliveira Neto, M. de, Figueira, A. C. M., Santos, M. A. M., Portugal, R. V., Guzzi, C. A. de, et al. (2007). Orphan nuclear receptor NGFI-B forms dimers with nonclassical interface. Protein Science, 16( 8), 1762-1772. doi:10.1110/ps.062692207
NLM
Calgaro MR, Oliveira Neto M de, Figueira ACM, Santos MAM, Portugal RV, Guzzi CA de, Saidemberg DM, Bleicher L, Vernal J, Fernandez P, Terenzi H, Palma MS, Polikarpov I. Orphan nuclear receptor NGFI-B forms dimers with nonclassical interface [Internet]. Protein Science. 2007 ; 16( 8): 1762-1772.[citado 2024 jul. 08 ] Available from: https://doi.org/10.1110/ps.062692207
Vancouver
Calgaro MR, Oliveira Neto M de, Figueira ACM, Santos MAM, Portugal RV, Guzzi CA de, Saidemberg DM, Bleicher L, Vernal J, Fernandez P, Terenzi H, Palma MS, Polikarpov I. Orphan nuclear receptor NGFI-B forms dimers with nonclassical interface [Internet]. Protein Science. 2007 ; 16( 8): 1762-1772.[citado 2024 jul. 08 ] Available from: https://doi.org/10.1110/ps.062692207
Artigo de periodico
Average protein density is a molecular-weight-dependent function (2004)
Fischer, Hannes; Polikarpov, Igor; Craievich, Aldo Felix
Source: Protein Science. Unidades: IF, IFSC
Subjects: CRISTALOGRAFIA FÍSICA, BIOQUÍMICA, BIOLOGIA MOLECULAR
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
ABNT
FISCHER, Hannes e POLIKARPOV, Igor e CRAIEVICH, Aldo Felix. Average protein density is a molecular-weight-dependent function. Protein Science, 2004Tradução . . Disponível em: https://doi.org/10.1110/ps.04688204. Acesso em: 08 jul. 2024.
APA
Fischer, H., Polikarpov, I., & Craievich, A. F. (2004). Average protein density is a molecular-weight-dependent function. Protein Science. doi:10.1110/ps.04688204
NLM
Fischer H, Polikarpov I, Craievich AF. Average protein density is a molecular-weight-dependent function [Internet]. Protein Science. 2004 ;[citado 2024 jul. 08 ] Available from: https://doi.org/10.1110/ps.04688204
Vancouver
Fischer H, Polikarpov I, Craievich AF. Average protein density is a molecular-weight-dependent function [Internet]. Protein Science. 2004 ;[citado 2024 jul. 08 ] Available from: https://doi.org/10.1110/ps.04688204

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