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Artigo de periodico
The structure of the extended E2 DNA-binding domain of the bovine papillomavirus-1 (2020)
Leroy, Ludmila; Barbosa, João Alexandre Ribeiro Gonçalves; Prat-Gay, Gonzalo de; Polikarpov, Igor ; Pinheiro, Carlos Basílio
Fonte: Proteins. Unidade: IFSC
Assuntos: PAPILLOMAVIRUS, BOVINOS, PROTEÍNAS
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LEROY, Ludmila et al. The structure of the extended E2 DNA-binding domain of the bovine papillomavirus-1. Proteins, v. 88, n. Ja 2020, p. 106-112, 2020Tradução . . Disponível em: https://doi.org/10.1002/prot.25773. Acesso em: 20 out. 2025.
APA
Leroy, L., Barbosa, J. A. R. G., Prat-Gay, G. de, Polikarpov, I., & Pinheiro, C. B. (2020). The structure of the extended E2 DNA-binding domain of the bovine papillomavirus-1. Proteins, 88( Ja 2020), 106-112. doi:10.1002/prot.25773
NLM
Leroy L, Barbosa JARG, Prat-Gay G de, Polikarpov I, Pinheiro CB. The structure of the extended E2 DNA-binding domain of the bovine papillomavirus-1 [Internet]. Proteins. 2020 ; 88( Ja 2020): 106-112.[citado 2025 out. 20 ] Available from: https://doi.org/10.1002/prot.25773
Vancouver
Leroy L, Barbosa JARG, Prat-Gay G de, Polikarpov I, Pinheiro CB. The structure of the extended E2 DNA-binding domain of the bovine papillomavirus-1 [Internet]. Proteins. 2020 ; 88( Ja 2020): 106-112.[citado 2025 out. 20 ] Available from: https://doi.org/10.1002/prot.25773
Artigo de periodico
Conformational variability of the stationary phase survival protein E from Xylella fastidiosa revealed by X-ray crystallography, small-angle X-ray scattering studies, and normal mode analysis (2017)
Machado, Agnes Thiane Pereira; Fonseca, Emanuella Maria Barreto; Reis, Marcelo Augusto dos; Saraiva, Antonio Marcos; Santos, Clelton Aparecido dos; Toledo, Marcelo Augusto Szymanski de; Polikarpov, Igor ; Souza, Anete Pereira de; Aparicio, Ricardo; Iulek, Jorge
Fonte: Proteins. Unidade: IFSC
Assuntos: CLOROSE VARIEGADA DOS CITROS, PROTEÍNAS, CRISTALOGRAFIA
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MACHADO, Agnes Thiane Pereira et al. Conformational variability of the stationary phase survival protein E from Xylella fastidiosa revealed by X-ray crystallography, small-angle X-ray scattering studies, and normal mode analysis. Proteins, v. 85, n. 10, p. 1931-1943, 2017Tradução . . Disponível em: https://doi.org/10.1002/prot.25347. Acesso em: 20 out. 2025.
APA
Machado, A. T. P., Fonseca, E. M. B., Reis, M. A. dos, Saraiva, A. M., Santos, C. A. dos, Toledo, M. A. S. de, et al. (2017). Conformational variability of the stationary phase survival protein E from Xylella fastidiosa revealed by X-ray crystallography, small-angle X-ray scattering studies, and normal mode analysis. Proteins, 85( 10), 1931-1943. doi:10.1002/prot.25347
NLM
Machado ATP, Fonseca EMB, Reis MA dos, Saraiva AM, Santos CA dos, Toledo MAS de, Polikarpov I, Souza AP de, Aparicio R, Iulek J. Conformational variability of the stationary phase survival protein E from Xylella fastidiosa revealed by X-ray crystallography, small-angle X-ray scattering studies, and normal mode analysis [Internet]. Proteins. 2017 ; 85( 10): 1931-1943.[citado 2025 out. 20 ] Available from: https://doi.org/10.1002/prot.25347
Vancouver
Machado ATP, Fonseca EMB, Reis MA dos, Saraiva AM, Santos CA dos, Toledo MAS de, Polikarpov I, Souza AP de, Aparicio R, Iulek J. Conformational variability of the stationary phase survival protein E from Xylella fastidiosa revealed by X-ray crystallography, small-angle X-ray scattering studies, and normal mode analysis [Internet]. Proteins. 2017 ; 85( 10): 1931-1943.[citado 2025 out. 20 ] Available from: https://doi.org/10.1002/prot.25347
Artigo de periodico
Model for the allosteric regulationof the `NA POT. +´/`CA POT. 2+' exchanger NCX (2016)
Abiko, Layara Akemi; Vitale, Phelipe M; Favaro, Denize Cristina; Hauk, Pricila; Li, Da‐Wei; Yuan, Jiaqi; Bruschweiler‐Li, Lei; Salinas, Roberto Kopke ; Brüschweiler, Rafael
Fonte: Proteins. Unidade: IQ
Assuntos: HIDRÓLISE, CELULOSE, BIOQUÍMICA
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ABIKO, Layara Akemi et al. Model for the allosteric regulationof the `NA POT. +´/`CA POT. 2+' exchanger NCX. Proteins, v. 84, n. 5, p. 580-590, 2016Tradução . . Disponível em: https://doi.org/10.1002/prot.25003. Acesso em: 20 out. 2025.
APA
Abiko, L. A., Vitale, P. M., Favaro, D. C., Hauk, P., Li, D. ‐W., Yuan, J., et al. (2016). Model for the allosteric regulationof the `NA POT. +´/`CA POT. 2+' exchanger NCX. Proteins, 84( 5), 580-590. doi:10.1002/prot.25003
NLM
Abiko LA, Vitale PM, Favaro DC, Hauk P, Li D‐W, Yuan J, Bruschweiler‐Li L, Salinas RK, Brüschweiler R. Model for the allosteric regulationof the `NA POT. +´/`CA POT. 2+' exchanger NCX [Internet]. Proteins. 2016 ; 84( 5): 580-590.[citado 2025 out. 20 ] Available from: https://doi.org/10.1002/prot.25003
Vancouver
Abiko LA, Vitale PM, Favaro DC, Hauk P, Li D‐W, Yuan J, Bruschweiler‐Li L, Salinas RK, Brüschweiler R. Model for the allosteric regulationof the `NA POT. +´/`CA POT. 2+' exchanger NCX [Internet]. Proteins. 2016 ; 84( 5): 580-590.[citado 2025 out. 20 ] Available from: https://doi.org/10.1002/prot.25003
Artigo de periodico
Conformational flexibility of the complete catalytic domain of Cdc25B phosphatases (2016)
Sayegh, Raphael Santa Rosa; Tamaki, Fabio Kendi; Marana, Sandro Roberto ; Salinas, Roberto Kopke ; Arantes, Guilherme Menegon
Fonte: Proteins. Unidade: IQ
Assuntos: ESPECTROSCOPIA DE RESSONÂNCIA MAGNÉTICA NUCLEAR, PROTEÍNAS
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SAYEGH, Raphael Santa Rosa et al. Conformational flexibility of the complete catalytic domain of Cdc25B phosphatases. Proteins, v. 84, n. 11, p. 1567–1575, 2016Tradução . . Disponível em: https://doi.org/10.1002/prot.25100. Acesso em: 20 out. 2025.
APA
Sayegh, R. S. R., Tamaki, F. K., Marana, S. R., Salinas, R. K., & Arantes, G. M. (2016). Conformational flexibility of the complete catalytic domain of Cdc25B phosphatases. Proteins, 84( 11), 1567–1575. doi:10.1002/prot.25100
NLM
Sayegh RSR, Tamaki FK, Marana SR, Salinas RK, Arantes GM. Conformational flexibility of the complete catalytic domain of Cdc25B phosphatases [Internet]. Proteins. 2016 ; 84( 11): 1567–1575.[citado 2025 out. 20 ] Available from: https://doi.org/10.1002/prot.25100
Vancouver
Sayegh RSR, Tamaki FK, Marana SR, Salinas RK, Arantes GM. Conformational flexibility of the complete catalytic domain of Cdc25B phosphatases [Internet]. Proteins. 2016 ; 84( 11): 1567–1575.[citado 2025 out. 20 ] Available from: https://doi.org/10.1002/prot.25100
Artigo de periodico
Wefold: a coopetition for protein structure prediction (2014)
Khoury, George A; Liwo, Adam; Khatib, Firas; Zhou, Hongyi; Chopra, Gaurav; Bacardit, Jaume; Bortot, Leandro O; Faccioli, Rodrigo A; Deng, Xin; He, Yi; Krupa, Pawel; Li, Jilong; Mozolewska, Magdalena A; Sieradzan, Adam K; Smadbeck, James; Wirecki, Tomasz; Cooper, Seth; Flatten, Jeff; Xu, Kefan; Baker, David; Cheng, Jianlin; Delbem, Alexandre Cláudio Botazzo ; Floudas, Christodoulos A; Keasar, Chen; Levitt, Michael; Popovic, Zoran; Scheraga, Harold A; Zhou, Hongyi; Crivelli, Silvia N
Fonte: Proteins. Unidade: ICMC
Assunto: SISTEMAS EMBUTIDOS
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KHOURY, George A et al. Wefold: a coopetition for protein structure prediction. Proteins, v. 82, n. 9, p. 1850-1868, 2014Tradução . . Disponível em: https://doi.org/10.1002/prot.24538. Acesso em: 20 out. 2025.
APA
Khoury, G. A., Liwo, A., Khatib, F., Zhou, H., Chopra, G., Bacardit, J., et al. (2014). Wefold: a coopetition for protein structure prediction. Proteins, 82( 9), 1850-1868. doi:10.1002/prot.24538
NLM
Khoury GA, Liwo A, Khatib F, Zhou H, Chopra G, Bacardit J, Bortot LO, Faccioli RA, Deng X, He Y, Krupa P, Li J, Mozolewska MA, Sieradzan AK, Smadbeck J, Wirecki T, Cooper S, Flatten J, Xu K, Baker D, Cheng J, Delbem ACB, Floudas CA, Keasar C, Levitt M, Popovic Z, Scheraga HA, Zhou H, Crivelli SN. Wefold: a coopetition for protein structure prediction [Internet]. Proteins. 2014 ; 82( 9): 1850-1868.[citado 2025 out. 20 ] Available from: https://doi.org/10.1002/prot.24538
Vancouver
Khoury GA, Liwo A, Khatib F, Zhou H, Chopra G, Bacardit J, Bortot LO, Faccioli RA, Deng X, He Y, Krupa P, Li J, Mozolewska MA, Sieradzan AK, Smadbeck J, Wirecki T, Cooper S, Flatten J, Xu K, Baker D, Cheng J, Delbem ACB, Floudas CA, Keasar C, Levitt M, Popovic Z, Scheraga HA, Zhou H, Crivelli SN. Wefold: a coopetition for protein structure prediction [Internet]. Proteins. 2014 ; 82( 9): 1850-1868.[citado 2025 out. 20 ] Available from: https://doi.org/10.1002/prot.24538
Artigo de periodico
Solution NMR analysis of the interaction between the actinoporin sticholysin i and DHPC micelles—correlation with backbone dynamics (2014)
López-Castilla, Aracelys; Pazos, Fabiola; Schreier, Shirley ; Pires, José Ricardo
Fonte: Proteins. Unidade: IQ
Assuntos: FOSFOLIPÍDEOS, TOXINAS
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ABNT
LÓPEZ-CASTILLA, Aracelys et al. Solution NMR analysis of the interaction between the actinoporin sticholysin i and DHPC micelles—correlation with backbone dynamics. Proteins, v. 82, n. 6, p. 1022-1034, 2014Tradução . . Disponível em: https://doi.org/10.1002/prot.24475. Acesso em: 20 out. 2025.
APA
López-Castilla, A., Pazos, F., Schreier, S., & Pires, J. R. (2014). Solution NMR analysis of the interaction between the actinoporin sticholysin i and DHPC micelles—correlation with backbone dynamics. Proteins, 82( 6), 1022-1034. doi:10.1002/prot.24475
NLM
López-Castilla A, Pazos F, Schreier S, Pires JR. Solution NMR analysis of the interaction between the actinoporin sticholysin i and DHPC micelles—correlation with backbone dynamics [Internet]. Proteins. 2014 ; 82( 6): 1022-1034.[citado 2025 out. 20 ] Available from: https://doi.org/10.1002/prot.24475
Vancouver
López-Castilla A, Pazos F, Schreier S, Pires JR. Solution NMR analysis of the interaction between the actinoporin sticholysin i and DHPC micelles—correlation with backbone dynamics [Internet]. Proteins. 2014 ; 82( 6): 1022-1034.[citado 2025 out. 20 ] Available from: https://doi.org/10.1002/prot.24475
Artigo de periodico
Inferring a weighted elastic network from partial unfolding with coarse-grained simulations (2014)
Mendonça, Matheus Rodrigues de; Rizzi, Leandro G.; Contessoto, Vinicius; Leite, Vitor B. P.; Alves, Nelson Augusto
Fonte: Proteins. Unidade: FFCLRP
Assuntos: ELASTICIDADE, VIBRAÇÕES, FÍSICA
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ABNT
MENDONÇA, Matheus Rodrigues de et al. Inferring a weighted elastic network from partial unfolding with coarse-grained simulations. Proteins, v. 82, n. 1, p. 119-129, 2014Tradução . . Disponível em: https://doi.org/10.1002/prot.24381. Acesso em: 20 out. 2025.
APA
Mendonça, M. R. de, Rizzi, L. G., Contessoto, V., Leite, V. B. P., & Alves, N. A. (2014). Inferring a weighted elastic network from partial unfolding with coarse-grained simulations. Proteins, 82( 1), 119-129. doi:10.1002/prot.24381
NLM
Mendonça MR de, Rizzi LG, Contessoto V, Leite VBP, Alves NA. Inferring a weighted elastic network from partial unfolding with coarse-grained simulations [Internet]. Proteins. 2014 ; 82( 1): 119-129.[citado 2025 out. 20 ] Available from: https://doi.org/10.1002/prot.24381
Vancouver
Mendonça MR de, Rizzi LG, Contessoto V, Leite VBP, Alves NA. Inferring a weighted elastic network from partial unfolding with coarse-grained simulations [Internet]. Proteins. 2014 ; 82( 1): 119-129.[citado 2025 out. 20 ] Available from: https://doi.org/10.1002/prot.24381
Artigo de periodico
Analyzing the effect of homogeneous frustration in protein folding (2013)
Contessoto, Vinícius; Lima, Debora T.; Oliveira, Ronaldo J.; Bruni, Aline Thais; Chahine, Jorge; Leite, Vitor B. P.
Fonte: Proteins. Unidade: FFCLRP
Assuntos: PROTEÍNAS (QUÍMICA;METABOLISMO), TERMODINÂMICA, ANÁLISE MULTIVARIADA
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CONTESSOTO, Vinícius et al. Analyzing the effect of homogeneous frustration in protein folding. Proteins, v. 81, n. 10, p. 1727\20131737, 2013Tradução . . Disponível em: https://doi.org/10.1002/prot.24309. Acesso em: 20 out. 2025.
APA
Contessoto, V., Lima, D. T., Oliveira, R. J., Bruni, A. T., Chahine, J., & Leite, V. B. P. (2013). Analyzing the effect of homogeneous frustration in protein folding. Proteins, 81( 10), 1727\20131737. doi:10.1002/prot.24309
NLM
Contessoto V, Lima DT, Oliveira RJ, Bruni AT, Chahine J, Leite VBP. Analyzing the effect of homogeneous frustration in protein folding [Internet]. Proteins. 2013 ; 81( 10): 1727\20131737.[citado 2025 out. 20 ] Available from: https://doi.org/10.1002/prot.24309
Vancouver
Contessoto V, Lima DT, Oliveira RJ, Bruni AT, Chahine J, Leite VBP. Analyzing the effect of homogeneous frustration in protein folding [Internet]. Proteins. 2013 ; 81( 10): 1727\20131737.[citado 2025 out. 20 ] Available from: https://doi.org/10.1002/prot.24309
Artigo de periodico
Mechanism of reactant and product dissociation from the anthrax edema factor: a locally enhanced sampling and steered molecular dynamics study (2011)
Martínez, Leandro; Malliavin, Thérèse E.; Blondel, Arnaud
Fonte: Proteins. Unidade: IFSC
Assuntos: HORMÔNIOS TIREOIDIANOS, ENZIMAS, SIMULAÇÃO, TRANSDUÇÃO DE SINAL CELULAR, RECEPTORES HORMONAIS, DNA
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MARTÍNEZ, Leandro e MALLIAVIN, Thérèse E. e BLONDEL, Arnaud. Mechanism of reactant and product dissociation from the anthrax edema factor: a locally enhanced sampling and steered molecular dynamics study. Proteins, v. 79, n. 5, p. 1649-1661, 2011Tradução . . Disponível em: https://doi.org/10.1002/prot.22991. Acesso em: 20 out. 2025.
APA
Martínez, L., Malliavin, T. E., & Blondel, A. (2011). Mechanism of reactant and product dissociation from the anthrax edema factor: a locally enhanced sampling and steered molecular dynamics study. Proteins, 79( 5), 1649-1661. doi:10.1002/prot.22991
NLM
Martínez L, Malliavin TE, Blondel A. Mechanism of reactant and product dissociation from the anthrax edema factor: a locally enhanced sampling and steered molecular dynamics study [Internet]. Proteins. 2011 ; 79( 5): 1649-1661.[citado 2025 out. 20 ] Available from: https://doi.org/10.1002/prot.22991
Vancouver
Martínez L, Malliavin TE, Blondel A. Mechanism of reactant and product dissociation from the anthrax edema factor: a locally enhanced sampling and steered molecular dynamics study [Internet]. Proteins. 2011 ; 79( 5): 1649-1661.[citado 2025 out. 20 ] Available from: https://doi.org/10.1002/prot.22991
Artigo de periodico
Systematic structural studies of iron superoxide dismutases from human parasites and a statistical coupling analysis of metal binding specificity (2009)
Bachega, José Fernando Ruggiero; Navarro, Marcos Vicente de Albuquerque Salles ; Bleicher, Lucas; Bugs, Raquel Kely Bortoleto; Dive, Daniel; Hoffmann, Pascal; Viscogliosi, Eric; Garratt, Richard Charles
Fonte: Proteins. Unidade: IFSC
Assuntos: INIBIDORES DE ENZIMAS, TRYPANOSOMA CRUZI, DOENÇA DE CHAGAS, TRIPANOSSOMOSE, ANÁLISE ESTATÍSTICA DE DADOS, CRISTALOGRAFIA FÍSICA, DOENÇAS PARASITÁRIAS, SEQUENCIAMENTO GENÉTICO, PROTEÍNAS (ESTUDO)
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BACHEGA, José Fernando Ruggiero et al. Systematic structural studies of iron superoxide dismutases from human parasites and a statistical coupling analysis of metal binding specificity. Proteins, v. 77, n. 1, p. 26-37, 2009Tradução . . Disponível em: https://doi.org/10.1002/prot.22412. Acesso em: 20 out. 2025.
APA
Bachega, J. F. R., Navarro, M. V. de A. S., Bleicher, L., Bugs, R. K. B., Dive, D., Hoffmann, P., et al. (2009). Systematic structural studies of iron superoxide dismutases from human parasites and a statistical coupling analysis of metal binding specificity. Proteins, 77( 1), 26-37. doi:10.1002/prot.22412
NLM
Bachega JFR, Navarro MV de AS, Bleicher L, Bugs RKB, Dive D, Hoffmann P, Viscogliosi E, Garratt RC. Systematic structural studies of iron superoxide dismutases from human parasites and a statistical coupling analysis of metal binding specificity [Internet]. Proteins. 2009 ; 77( 1): 26-37.[citado 2025 out. 20 ] Available from: https://doi.org/10.1002/prot.22412
Vancouver
Bachega JFR, Navarro MV de AS, Bleicher L, Bugs RKB, Dive D, Hoffmann P, Viscogliosi E, Garratt RC. Systematic structural studies of iron superoxide dismutases from human parasites and a statistical coupling analysis of metal binding specificity [Internet]. Proteins. 2009 ; 77( 1): 26-37.[citado 2025 out. 20 ] Available from: https://doi.org/10.1002/prot.22412
Artigo de periodico
Crystal structure of yeast hexokinase Pl in complex with glucose: a classical "induced fit" example revised (2008)
Kuser, Paula; Cupri, Fabio; Bleicher, Lucas; Polikarpov, Igor
Fonte: Proteins. Unidade: IFSC
Assuntos: RAIOS X (ESTRUTURA), CRISTALOGRAFIA, SACCHAROMYCES
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ABNT
KUSER, Paula et al. Crystal structure of yeast hexokinase Pl in complex with glucose: a classical "induced fit" example revised. Proteins, v. 72, n. 2, p. 731-740, 2008Tradução . . Disponível em: https://doi.org/10.1002/prot.21956. Acesso em: 20 out. 2025.
APA
Kuser, P., Cupri, F., Bleicher, L., & Polikarpov, I. (2008). Crystal structure of yeast hexokinase Pl in complex with glucose: a classical "induced fit" example revised. Proteins, 72( 2), 731-740. doi:10.1002/prot.21956
NLM
Kuser P, Cupri F, Bleicher L, Polikarpov I. Crystal structure of yeast hexokinase Pl in complex with glucose: a classical "induced fit" example revised [Internet]. Proteins. 2008 ; 72( 2): 731-740.[citado 2025 out. 20 ] Available from: https://doi.org/10.1002/prot.21956
Vancouver
Kuser P, Cupri F, Bleicher L, Polikarpov I. Crystal structure of yeast hexokinase Pl in complex with glucose: a classical "induced fit" example revised [Internet]. Proteins. 2008 ; 72( 2): 731-740.[citado 2025 out. 20 ] Available from: https://doi.org/10.1002/prot.21956

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