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Trabalho de evento-resumo periodico
The interaction between the antimicrobial peptide K-Hya1 and model membranes: distinct action in neutral or negatively charged bilayers (2014)
Enoki, Thais Azevedo; Riske, Karin A.; Perez, Katia R.; Lorenzon, Esteban N.; Cilli, Eduardo M.; Lamy, Maria Teresa Moura
Source: Biophysical Journal. Conference titles: Annual Meeting of the Biophysical Society. Unidade: IF
Subjects: PEPTÍDEOS, PROTEÍNAS (ESTUDO)
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
ABNT
ENOKI, Thais Azevedo et al. The interaction between the antimicrobial peptide K-Hya1 and model membranes: distinct action in neutral or negatively charged bilayers. Biophysical Journal. Saint Louis: Cell Press. Disponível em: http://www.cell.com/biophysj/abstract/S0006-3495(13)01778-5. Acesso em: 26 dez. 2024. , 2014
APA
Enoki, T. A., Riske, K. A., Perez, K. R., Lorenzon, E. N., Cilli, E. M., & Lamy, M. T. M. (2014). The interaction between the antimicrobial peptide K-Hya1 and model membranes: distinct action in neutral or negatively charged bilayers. Biophysical Journal. Saint Louis: Cell Press. Recuperado de http://www.cell.com/biophysj/abstract/S0006-3495(13)01778-5
NLM
Enoki TA, Riske KA, Perez KR, Lorenzon EN, Cilli EM, Lamy MTM. The interaction between the antimicrobial peptide K-Hya1 and model membranes: distinct action in neutral or negatively charged bilayers [Internet]. Biophysical Journal. 2014 ; 106( ja 2014): 85A.[citado 2024 dez. 26 ] Available from: http://www.cell.com/biophysj/abstract/S0006-3495(13)01778-5
Vancouver
Enoki TA, Riske KA, Perez KR, Lorenzon EN, Cilli EM, Lamy MTM. The interaction between the antimicrobial peptide K-Hya1 and model membranes: distinct action in neutral or negatively charged bilayers [Internet]. Biophysical Journal. 2014 ; 106( ja 2014): 85A.[citado 2024 dez. 26 ] Available from: http://www.cell.com/biophysj/abstract/S0006-3495(13)01778-5
Trabalho de evento-resumo periodico
The conformational flexibility of an internal fusion peptide from sars-Cov spike glycoprotein is modulated by lipid membrane composition (2014)
Basso, Luis G. M.; Fernandes, Tácio V. A.; Lima, José Fernando de; Crusca Junior, Edson; Vicente, Eduardo F.; Cilli, Eduardo M.; Pascutti, Pedro G.; Costa Filho, Antônio José da
Source: Biophysical Journal. Conference titles: Annual Meeting of the Biophysical Society. Unidades: IFSC, FFCLRP
Subjects: PEPTÍDEOS, PROTEÍNAS (ESTUDO)
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
ABNT
BASSO, Luis G. M. et al. The conformational flexibility of an internal fusion peptide from sars-Cov spike glycoprotein is modulated by lipid membrane composition. Biophysical Journal. Saint Louis: Cell Press. Disponível em: https://doi.org/10.1016/j.bpj.2013.11.1720. Acesso em: 26 dez. 2024. , 2014
APA
Basso, L. G. M., Fernandes, T. V. A., Lima, J. F. de, Crusca Junior, E., Vicente, E. F., Cilli, E. M., et al. (2014). The conformational flexibility of an internal fusion peptide from sars-Cov spike glycoprotein is modulated by lipid membrane composition. Biophysical Journal. Saint Louis: Cell Press. doi:10.1016/j.bpj.2013.11.1720
NLM
Basso LGM, Fernandes TVA, Lima JF de, Crusca Junior E, Vicente EF, Cilli EM, Pascutti PG, Costa Filho AJ da. The conformational flexibility of an internal fusion peptide from sars-Cov spike glycoprotein is modulated by lipid membrane composition [Internet]. Biophysical Journal. 2014 ; 106( Ja 2014): 295a.[citado 2024 dez. 26 ] Available from: https://doi.org/10.1016/j.bpj.2013.11.1720
Vancouver
Basso LGM, Fernandes TVA, Lima JF de, Crusca Junior E, Vicente EF, Cilli EM, Pascutti PG, Costa Filho AJ da. The conformational flexibility of an internal fusion peptide from sars-Cov spike glycoprotein is modulated by lipid membrane composition [Internet]. Biophysical Journal. 2014 ; 106( Ja 2014): 295a.[citado 2024 dez. 26 ] Available from: https://doi.org/10.1016/j.bpj.2013.11.1720
Trabalho de evento-resumo periodico
Unraveling the heparin-induced protofibril structure of GAPDH (2014)
Itri, Rosangela; Torres-Bugeau, Clarisa M.; Avila, Cesar L.; Chehin, Rosana N.; Sales, Elisa Morandé; Barbosa, Leandro Ramos Souza
Source: Biophysical Journal. Conference titles: Annual Meeting of the Biophysical Society. Unidade: IF
Subjects: PEPTÍDEOS, PROTEÍNAS (ESTUDO)
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
ABNT
ITRI, Rosangela et al. Unraveling the heparin-induced protofibril structure of GAPDH. Biophysical Journal. Saint Louis: Cell Press. Disponível em: http://www.cell.com/biophysj/comments/S0006-3495(13)03434-6. Acesso em: 26 dez. 2024. , 2014
APA
Itri, R., Torres-Bugeau, C. M., Avila, C. L., Chehin, R. N., Sales, E. M., & Barbosa, L. R. S. (2014). Unraveling the heparin-induced protofibril structure of GAPDH. Biophysical Journal. Saint Louis: Cell Press. Recuperado de http://www.cell.com/biophysj/comments/S0006-3495(13)03434-6
NLM
Itri R, Torres-Bugeau CM, Avila CL, Chehin RN, Sales EM, Barbosa LRS. Unraveling the heparin-induced protofibril structure of GAPDH [Internet]. Biophysical Journal. 2014 ; 106( ja 2014): 385A.[citado 2024 dez. 26 ] Available from: http://www.cell.com/biophysj/comments/S0006-3495(13)03434-6
Vancouver
Itri R, Torres-Bugeau CM, Avila CL, Chehin RN, Sales EM, Barbosa LRS. Unraveling the heparin-induced protofibril structure of GAPDH [Internet]. Biophysical Journal. 2014 ; 106( ja 2014): 385A.[citado 2024 dez. 26 ] Available from: http://www.cell.com/biophysj/comments/S0006-3495(13)03434-6
Trabalho de evento-resumo periodico
Spin labels detect the coexistence of two lipid domains along the anomalous gel-fluid transition of anionic dmpg bilayers (2014)
Pellegrina, Diogo V. S.; Duarte, Evandro Luiz; Lamy, Maria Teresa Moura
Source: Biophysical Journal. Conference titles: Annual Meeting of the Biophysical Society. Unidade: IF
Subjects: PEPTÍDEOS, PROTEÍNAS (ESTUDO)
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
ABNT
PELLEGRINA, Diogo V. S. e DUARTE, Evandro Luiz e LAMY, Maria Teresa Moura. Spin labels detect the coexistence of two lipid domains along the anomalous gel-fluid transition of anionic dmpg bilayers. Biophysical Journal. Saint Louis: Cell Press. Disponível em: http://www.cell.com/biophysj/fulltext/S0006-3495(13)04109-X. Acesso em: 26 dez. 2024. , 2014
APA
Pellegrina, D. V. S., Duarte, E. L., & Lamy, M. T. M. (2014). Spin labels detect the coexistence of two lipid domains along the anomalous gel-fluid transition of anionic dmpg bilayers. Biophysical Journal. Saint Louis: Cell Press. Recuperado de http://www.cell.com/biophysj/fulltext/S0006-3495(13)04109-X
NLM
Pellegrina DVS, Duarte EL, Lamy MTM. Spin labels detect the coexistence of two lipid domains along the anomalous gel-fluid transition of anionic dmpg bilayers [Internet]. Biophysical Journal. 2014 ; 106( ja 2014): 510A.[citado 2024 dez. 26 ] Available from: http://www.cell.com/biophysj/fulltext/S0006-3495(13)04109-X
Vancouver
Pellegrina DVS, Duarte EL, Lamy MTM. Spin labels detect the coexistence of two lipid domains along the anomalous gel-fluid transition of anionic dmpg bilayers [Internet]. Biophysical Journal. 2014 ; 106( ja 2014): 510A.[citado 2024 dez. 26 ] Available from: http://www.cell.com/biophysj/fulltext/S0006-3495(13)04109-X
Trabalho de evento-resumo periodico
Probing S100A12 interactions with model membranes (2014)
Lopes, Jose Luiz S.; Garcia, Assuero F.; Costa Filho, Antônio José da; Wallace, B. A.; Araújo, Ana Paula Ulian de
Source: Biophysical Journal. Conference titles: Annual Meeting of the Biophysical Society. Unidades: FFCLRP, IFSC
Subjects: PROTEÍNAS (ESTUDO), LIPOSSOMOS, LIPÍDEOS
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
ABNT
LOPES, Jose Luiz S. et al. Probing S100A12 interactions with model membranes. Biophysical Journal. Saint Louis: Cell Press. Disponível em: https://doi.org/10.1016/j.bpj.2013.11.2883. Acesso em: 26 dez. 2024. , 2014
APA
Lopes, J. L. S., Garcia, A. F., Costa Filho, A. J. da, Wallace, B. A., & Araújo, A. P. U. de. (2014). Probing S100A12 interactions with model membranes. Biophysical Journal. Saint Louis: Cell Press. doi:10.1016/j.bpj.2013.11.2883
NLM
Lopes JLS, Garcia AF, Costa Filho AJ da, Wallace BA, Araújo APU de. Probing S100A12 interactions with model membranes [Internet]. Biophysical Journal. 2014 ; 106( Ja 2014): 516a.[citado 2024 dez. 26 ] Available from: https://doi.org/10.1016/j.bpj.2013.11.2883
Vancouver
Lopes JLS, Garcia AF, Costa Filho AJ da, Wallace BA, Araújo APU de. Probing S100A12 interactions with model membranes [Internet]. Biophysical Journal. 2014 ; 106( Ja 2014): 516a.[citado 2024 dez. 26 ] Available from: https://doi.org/10.1016/j.bpj.2013.11.2883
Trabalho de evento-resumo periodico
Urea, guanidine hydrocloride and 2,2,2-trifluoroethanol can change the amyloid fibril formation of model proteins: a spectroscopic study (2014)
Barbosa, Leandro Ramos Souza; Barbosa, Leandro Ramos Souza
Source: Biophysical Journal. Conference titles: Annual Meeting of the Biophysical Society. Unidade: IF
Subjects: PEPTÍDEOS, PROTEÍNAS (ESTUDO)
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
ABNT
BARBOSA, Leandro Ramos Souza e BARBOSA, Leandro Ramos Souza. Urea, guanidine hydrocloride and 2,2,2-trifluoroethanol can change the amyloid fibril formation of model proteins: a spectroscopic study. Biophysical Journal. Saint Louis: Cell Press. Disponível em: http://www.cell.com/biophysj/pdf/S0006-3495(13)05028-5.pdf. Acesso em: 26 dez. 2024. , 2014
APA
Barbosa, L. R. S., & Barbosa, L. R. S. (2014). Urea, guanidine hydrocloride and 2,2,2-trifluoroethanol can change the amyloid fibril formation of model proteins: a spectroscopic study. Biophysical Journal. Saint Louis: Cell Press. Recuperado de http://www.cell.com/biophysj/pdf/S0006-3495(13)05028-5.pdf
NLM
Barbosa LRS, Barbosa LRS. Urea, guanidine hydrocloride and 2,2,2-trifluoroethanol can change the amyloid fibril formation of model proteins: a spectroscopic study [Internet]. Biophysical Journal. 2014 ; 106( ja 2014): 681A.[citado 2024 dez. 26 ] Available from: http://www.cell.com/biophysj/pdf/S0006-3495(13)05028-5.pdf
Vancouver
Barbosa LRS, Barbosa LRS. Urea, guanidine hydrocloride and 2,2,2-trifluoroethanol can change the amyloid fibril formation of model proteins: a spectroscopic study [Internet]. Biophysical Journal. 2014 ; 106( ja 2014): 681A.[citado 2024 dez. 26 ] Available from: http://www.cell.com/biophysj/pdf/S0006-3495(13)05028-5.pdf

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