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Trabalho de evento-resumo periodico
Characterization of the Calcium Release-Activated Calcium (CRAC) channel from the human pathogen Schistosoma mansoni (2018)
Zeraik, Ana Eliza; Gudlur, Aparna; De Marco, Ricardo; Araújo, Ana Paula Ulian de ; Hogan, Patrick
Source: Biophysical Journal. Conference titles: Annual Meeting of the Biophysical Society. Unidade: IFSC
Subjects: SCHISTOSOMA MANSONI, ESQUISTOSSOMOSE, PLANEJAMENTO DE FÁRMACOS
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ABNT
ZERAIK, Ana Eliza et al. Characterization of the Calcium Release-Activated Calcium (CRAC) channel from the human pathogen Schistosoma mansoni. Biophysical Journal. Saint Louis: Cell Press. Disponível em: https://doi.org/10.1016/j.bpj.2017.11.1640. Acesso em: 11 nov. 2024. , 2018
APA
Zeraik, A. E., Gudlur, A., De Marco, R., Araújo, A. P. U. de, & Hogan, P. (2018). Characterization of the Calcium Release-Activated Calcium (CRAC) channel from the human pathogen Schistosoma mansoni. Biophysical Journal. Saint Louis: Cell Press. doi:10.1016/j.bpj.2017.11.1640
NLM
Zeraik AE, Gudlur A, De Marco R, Araújo APU de, Hogan P. Characterization of the Calcium Release-Activated Calcium (CRAC) channel from the human pathogen Schistosoma mansoni [Internet]. Biophysical Journal. 2018 ; 114( 3): 286a.[citado 2024 nov. 11 ] Available from: https://doi.org/10.1016/j.bpj.2017.11.1640
Vancouver
Zeraik AE, Gudlur A, De Marco R, Araújo APU de, Hogan P. Characterization of the Calcium Release-Activated Calcium (CRAC) channel from the human pathogen Schistosoma mansoni [Internet]. Biophysical Journal. 2018 ; 114( 3): 286a.[citado 2024 nov. 11 ] Available from: https://doi.org/10.1016/j.bpj.2017.11.1640
Trabalho de evento-resumo periodico
Weighted ensemble of pathways for ligand unbinding from T4 lysozyme (2017)
Nunes Alves, Ariane Ferreira; Zuckermann, Daniel M; Arantes, Guilherme Menegon
Source: Biophysical Journal. Conference titles: Annual Meeting of the Biophysical Society. Unidade: IQ
Subjects: LISOZIMAS, PROTEÍNAS
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ABNT
NUNES ALVES, Ariane Ferreira e ZUCKERMANN, Daniel M e ARANTES, Guilherme Menegon. Weighted ensemble of pathways for ligand unbinding from T4 lysozyme. Biophysical Journal. Cambridge: Instituto de Química, Universidade de São Paulo. . Acesso em: 11 nov. 2024. , 2017
APA
Nunes Alves, A. F., Zuckermann, D. M., & Arantes, G. M. (2017). Weighted ensemble of pathways for ligand unbinding from T4 lysozyme. Biophysical Journal. Cambridge: Instituto de Química, Universidade de São Paulo.
NLM
Nunes Alves AF, Zuckermann DM, Arantes GM. Weighted ensemble of pathways for ligand unbinding from T4 lysozyme. Biophysical Journal. 2017 ; 112( 3): 339a res. 1660-Plat.[citado 2024 nov. 11 ]
Vancouver
Nunes Alves AF, Zuckermann DM, Arantes GM. Weighted ensemble of pathways for ligand unbinding from T4 lysozyme. Biophysical Journal. 2017 ; 112( 3): 339a res. 1660-Plat.[citado 2024 nov. 11 ]
Trabalho de evento-resumo periodico
Orientational properties of DOPC/SM/cholesterol mixtures: a PMIRRAS study (2017)
Maté, Sabina M.; Vazquez, Romina; Pavinatto, Felippe José; Dazza-Milone, M. Antonieta; Herlax, Vanesa; Bakas, Laura; Oliveira Junior, Osvaldo Novais de ; Vela, María E.
Source: Biophysical Journal. Conference titles: Annual Meeting of the Biophysical Society. Unidade: IFSC
Subjects: LIPÍDEOS DA MEMBRANA, MEMBRANA PLASMÁTICA, COLESTEROL, FILMES FINOS
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ABNT
MATÉ, Sabina M. et al. Orientational properties of DOPC/SM/cholesterol mixtures: a PMIRRAS study. Biophysical Journal. Saint Louis: Cell Press. Disponível em: https://doi.org/10.1016/j.bpj.2016.11.488. Acesso em: 11 nov. 2024. , 2017
APA
Maté, S. M., Vazquez, R., Pavinatto, F. J., Dazza-Milone, M. A., Herlax, V., Bakas, L., et al. (2017). Orientational properties of DOPC/SM/cholesterol mixtures: a PMIRRAS study. Biophysical Journal. Saint Louis: Cell Press. doi:10.1016/j.bpj.2016.11.488
NLM
Maté SM, Vazquez R, Pavinatto FJ, Dazza-Milone MA, Herlax V, Bakas L, Oliveira Junior ON de, Vela ME. Orientational properties of DOPC/SM/cholesterol mixtures: a PMIRRAS study [Internet]. Biophysical Journal. 2017 ; 112( 3): 82a.[citado 2024 nov. 11 ] Available from: https://doi.org/10.1016/j.bpj.2016.11.488
Vancouver
Maté SM, Vazquez R, Pavinatto FJ, Dazza-Milone MA, Herlax V, Bakas L, Oliveira Junior ON de, Vela ME. Orientational properties of DOPC/SM/cholesterol mixtures: a PMIRRAS study [Internet]. Biophysical Journal. 2017 ; 112( 3): 82a.[citado 2024 nov. 11 ] Available from: https://doi.org/10.1016/j.bpj.2016.11.488
Trabalho de evento-resumo periodico
STIM-Orai interaction in Schistosoma Mansoni indicates the existence of functional store-operated calcium entry in the parasite (2016)
Zeraik, Ana Eliza; Fontes, Marina Gabriel; Lopes, Jose Luiz Souza; Araújo, Ana Paula Ulian de ; De Marco, Ricardo
Source: Biophysical Journal. Conference titles: Annual Meeting of the Biophysical Society. Unidade: IFSC
Subjects: ESQUISTOSSOMOSE, SCHISTOSOMA MANSONI
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ABNT
ZERAIK, Ana Eliza et al. STIM-Orai interaction in Schistosoma Mansoni indicates the existence of functional store-operated calcium entry in the parasite. Biophysical Journal. Saint Louis: Cell Press. Disponível em: https://doi.org/10.1016/j.bpj.2015.11.1441. Acesso em: 11 nov. 2024. , 2016
APA
Zeraik, A. E., Fontes, M. G., Lopes, J. L. S., Araújo, A. P. U. de, & De Marco, R. (2016). STIM-Orai interaction in Schistosoma Mansoni indicates the existence of functional store-operated calcium entry in the parasite. Biophysical Journal. Saint Louis: Cell Press. doi:10.1016/j.bpj.2015.11.1441
NLM
Zeraik AE, Fontes MG, Lopes JLS, Araújo APU de, De Marco R. STIM-Orai interaction in Schistosoma Mansoni indicates the existence of functional store-operated calcium entry in the parasite [Internet]. Biophysical Journal. 2016 ; 110( 3): 264a.[citado 2024 nov. 11 ] Available from: https://doi.org/10.1016/j.bpj.2015.11.1441
Vancouver
Zeraik AE, Fontes MG, Lopes JLS, Araújo APU de, De Marco R. STIM-Orai interaction in Schistosoma Mansoni indicates the existence of functional store-operated calcium entry in the parasite [Internet]. Biophysical Journal. 2016 ; 110( 3): 264a.[citado 2024 nov. 11 ] Available from: https://doi.org/10.1016/j.bpj.2015.11.1441
Trabalho de evento-resumo periodico
Non-equilibrium molecular dynamics to simulate shear stress on angiotensin II type 1 (AT1) receptor (2016)
Sá, Matheus Malta de; Modestia, Silvestre Massimo; Rangel-Yagui, Carlota de Oliveira ; Krieger, José Eduardo
Source: Biophysical Journal. Conference titles: Annual Meeting of the Biophysical Society. Unidades: FM, FCF
Subjects: ANGIOTENSINA II, RECEPTORES
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ABNT
SÁ, Matheus Malta de et al. Non-equilibrium molecular dynamics to simulate shear stress on angiotensin II type 1 (AT1) receptor. Biophysical Journal. Saint Louis: Faculdade de Medicina, Universidade de São Paulo. . Acesso em: 11 nov. 2024. , 2016
APA
Sá, M. M. de, Modestia, S. M., Rangel-Yagui, C. de O., & Krieger, J. E. (2016). Non-equilibrium molecular dynamics to simulate shear stress on angiotensin II type 1 (AT1) receptor. Biophysical Journal. Saint Louis: Faculdade de Medicina, Universidade de São Paulo.
NLM
Sá MM de, Modestia SM, Rangel-Yagui C de O, Krieger JE. Non-equilibrium molecular dynamics to simulate shear stress on angiotensin II type 1 (AT1) receptor. Biophysical Journal. 2016 ; 110( 3): 325a res. 1600-Pos Board B577.[citado 2024 nov. 11 ]
Vancouver
Sá MM de, Modestia SM, Rangel-Yagui C de O, Krieger JE. Non-equilibrium molecular dynamics to simulate shear stress on angiotensin II type 1 (AT1) receptor. Biophysical Journal. 2016 ; 110( 3): 325a res. 1600-Pos Board B577.[citado 2024 nov. 11 ]
Trabalho de evento-resumo periodico
Does the golgi reassembly and stacking protein (GRASP) behave as a well-structured protein in solution? (2015)
Mendes, Luís Felipe Santos ; Garcia, Assuero Faria; Rodrigues, Marcio L.; Costa Filho, Antônio José da
Source: Biophysical Journal. Conference titles: Annual Meeting of the Biophysical Society. Unidade: FFCLRP
Subjects: BIOFÍSICA, CRYPTOCOCCUS, INFECÇÕES OPORTUNISTAS
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ABNT
MENDES, Luís Felipe Santos et al. Does the golgi reassembly and stacking protein (GRASP) behave as a well-structured protein in solution?. Biophysical Journal. Saint Louis: Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto, Universidade de São Paulo. Disponível em: https://doi.org/10.1016/j.bpj.2014.11.1272. Acesso em: 11 nov. 2024. , 2015
APA
Mendes, L. F. S., Garcia, A. F., Rodrigues, M. L., & Costa Filho, A. J. da. (2015). Does the golgi reassembly and stacking protein (GRASP) behave as a well-structured protein in solution? Biophysical Journal. Saint Louis: Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto, Universidade de São Paulo. doi:10.1016/j.bpj.2014.11.1272
NLM
Mendes LFS, Garcia AF, Rodrigues ML, Costa Filho AJ da. Does the golgi reassembly and stacking protein (GRASP) behave as a well-structured protein in solution? [Internet]. Biophysical Journal. 2015 ; 108( 2): 230a.[citado 2024 nov. 11 ] Available from: https://doi.org/10.1016/j.bpj.2014.11.1272
Vancouver
Mendes LFS, Garcia AF, Rodrigues ML, Costa Filho AJ da. Does the golgi reassembly and stacking protein (GRASP) behave as a well-structured protein in solution? [Internet]. Biophysical Journal. 2015 ; 108( 2): 230a.[citado 2024 nov. 11 ] Available from: https://doi.org/10.1016/j.bpj.2014.11.1272
Trabalho de evento-resumo periodico
Characterization of amynthas gracilis hemoglobin (HbAg) and its subunits by AUC and MALDI-TOF-MS (2015)
Santiago, Patricia Soares; Carvalho, Francisco Adriano; Oliveira, Jonathan B S; Linhares, Angela P D; Morgante, Patrícia Gleydes; Carvalho, Jose Wilson Pires; Tabak, Marcel
Source: Biophysical Journal. Conference titles: Annual Meeting of the Biophysical Society. Unidade: IQSC
Assunto: BIOFÍSICA
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ABNT
SANTIAGO, Patricia Soares et al. Characterization of amynthas gracilis hemoglobin (HbAg) and its subunits by AUC and MALDI-TOF-MS. Biophysical Journal. St Louis: Cell Press. . Acesso em: 11 nov. 2024. , 2015
APA
Santiago, P. S., Carvalho, F. A., Oliveira, J. B. S., Linhares, A. P. D., Morgante, P. G., Carvalho, J. W. P., & Tabak, M. (2015). Characterization of amynthas gracilis hemoglobin (HbAg) and its subunits by AUC and MALDI-TOF-MS. Biophysical Journal. St Louis: Cell Press.
NLM
Santiago PS, Carvalho FA, Oliveira JBS, Linhares APD, Morgante PG, Carvalho JWP, Tabak M. Characterization of amynthas gracilis hemoglobin (HbAg) and its subunits by AUC and MALDI-TOF-MS. Biophysical Journal. 2015 ; 108( 2): 375A.[citado 2024 nov. 11 ]
Vancouver
Santiago PS, Carvalho FA, Oliveira JBS, Linhares APD, Morgante PG, Carvalho JWP, Tabak M. Characterization of amynthas gracilis hemoglobin (HbAg) and its subunits by AUC and MALDI-TOF-MS. Biophysical Journal. 2015 ; 108( 2): 375A.[citado 2024 nov. 11 ]
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)
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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: 11 nov. 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 nov. 11 ] 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 nov. 11 ] Available from: http://www.cell.com/biophysj/abstract/S0006-3495(13)01778-5
Trabalho de evento-resumo periodico
A computational method including protein flexibility to estimate affinities with small ligands (2014)
Alves, Ariane Ferreira Nunes; Arantes, Guilherme Menegon
Source: Biophysical Journal. Conference titles: Annual Meeting of the Biophysical Society. Unidade: IQ
Subjects: LISOZIMAS, BIOINFORMÁTICA
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ABNT
ALVES, Ariane Ferreira Nunes e ARANTES, Guilherme Menegon. A computational method including protein flexibility to estimate affinities with small ligands. Biophysical Journal. Cambridge: Instituto de Química, Universidade de São Paulo. . Acesso em: 11 nov. 2024. , 2014
APA
Alves, A. F. N., & Arantes, G. M. (2014). A computational method including protein flexibility to estimate affinities with small ligands. Biophysical Journal. Cambridge: Instituto de Química, Universidade de São Paulo.
NLM
Alves AFN, Arantes GM. A computational method including protein flexibility to estimate affinities with small ligands. Biophysical Journal. 2014 ; 106( 2): 408-409 res. 2062.[citado 2024 nov. 11 ]
Vancouver
Alves AFN, Arantes GM. A computational method including protein flexibility to estimate affinities with small ligands. Biophysical Journal. 2014 ; 106( 2): 408-409 res. 2062.[citado 2024 nov. 11 ]
Trabalho de evento-resumo periodico
Peptide: lipid ratio and membrane surface charge modulate the mechanism of action of the antimicrobial peptide BP100 (2014)
Schreier, Shirley ; Manzini, Mariana Canale; Perez, Katia Regina; Riske, Karin do Amaral; Bozelli Junior, José Carlos; Politi, Mário José ; Valente, Ana P; Almeida, Fábio C; Chaimovich Guralnik, Hernan ; Rodrigues, Magali Aparecida; Bemquerer, Marcelo Porto; Cuccovia, Iolanda Midea
Source: Biophysical Journal. Conference titles: Annual Meeting of the Biophysical Society. Unidade: IQ
Subjects: PEPTÍDEOS, BIOQUÍMICA
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ABNT
SCHREIER, Shirley et al. Peptide: lipid ratio and membrane surface charge modulate the mechanism of action of the antimicrobial peptide BP100. Biophysical Journal. Cambridge: Instituto de Química, Universidade de São Paulo. . Acesso em: 11 nov. 2024. , 2014
APA
Schreier, S., Manzini, M. C., Perez, K. R., Riske, K. do A., Bozelli Junior, J. C., Politi, M. J., et al. (2014). Peptide: lipid ratio and membrane surface charge modulate the mechanism of action of the antimicrobial peptide BP100. Biophysical Journal. Cambridge: Instituto de Química, Universidade de São Paulo.
NLM
Schreier S, Manzini MC, Perez KR, Riske K do A, Bozelli Junior JC, Politi MJ, Valente AP, Almeida FC, Chaimovich Guralnik H, Rodrigues MA, Bemquerer MP, Cuccovia IM. Peptide: lipid ratio and membrane surface charge modulate the mechanism of action of the antimicrobial peptide BP100. Biophysical Journal. 2014 ; 106( 2): 441 res. 2230.[citado 2024 nov. 11 ]
Vancouver
Schreier S, Manzini MC, Perez KR, Riske K do A, Bozelli Junior JC, Politi MJ, Valente AP, Almeida FC, Chaimovich Guralnik H, Rodrigues MA, Bemquerer MP, Cuccovia IM. Peptide: lipid ratio and membrane surface charge modulate the mechanism of action of the antimicrobial peptide BP100. Biophysical Journal. 2014 ; 106( 2): 441 res. 2230.[citado 2024 nov. 11 ]
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)
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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: 11 nov. 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 nov. 11 ] 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 nov. 11 ] 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)
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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: 11 nov. 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 nov. 11 ] 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 nov. 11 ] 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)
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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: 11 nov. 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 nov. 11 ] 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 nov. 11 ] Available from: http://www.cell.com/biophysj/fulltext/S0006-3495(13)04109-X
Trabalho de evento-resumo periodico
Accurate simulation of ubiquinone partition and diffusion in a bacterial like membrane model: towards reliable estimates of the energetics involved in the Q-cycle mechanism of cytocrome Bc1 (2014)
Galassi, Vanesa V; Silva, João P. V. Camargo da; Arantes, Guilherme Menegon
Source: Biophysical Journal. Conference titles: Annual Meeting of the Biophysical Society. Unidade: IQ
Subjects: BIOINFORMÁTICA, CATÁLISE
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ABNT
GALASSI, Vanesa V e SILVA, João P. V. Camargo da e ARANTES, Guilherme Menegon. Accurate simulation of ubiquinone partition and diffusion in a bacterial like membrane model: towards reliable estimates of the energetics involved in the Q-cycle mechanism of cytocrome Bc1. Biophysical Journal. Cambridge: Instituto de Química, Universidade de São Paulo. . Acesso em: 11 nov. 2024. , 2014
APA
Galassi, V. V., Silva, J. P. V. C. da, & Arantes, G. M. (2014). Accurate simulation of ubiquinone partition and diffusion in a bacterial like membrane model: towards reliable estimates of the energetics involved in the Q-cycle mechanism of cytocrome Bc1. Biophysical Journal. Cambridge: Instituto de Química, Universidade de São Paulo.
NLM
Galassi VV, Silva JPVC da, Arantes GM. Accurate simulation of ubiquinone partition and diffusion in a bacterial like membrane model: towards reliable estimates of the energetics involved in the Q-cycle mechanism of cytocrome Bc1. Biophysical Journal. 2014 ; 106( 2): 587 res. 2965.[citado 2024 nov. 11 ]
Vancouver
Galassi VV, Silva JPVC da, Arantes GM. Accurate simulation of ubiquinone partition and diffusion in a bacterial like membrane model: towards reliable estimates of the energetics involved in the Q-cycle mechanism of cytocrome Bc1. Biophysical Journal. 2014 ; 106( 2): 587 res. 2965.[citado 2024 nov. 11 ]
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
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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: 11 nov. 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 nov. 11 ] 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 nov. 11 ] Available from: https://doi.org/10.1016/j.bpj.2013.11.2883
Trabalho de evento-resumo periodico
Combining NMR and computer simulations to evaluate Cdc25B protein flexbility (2014)
Sayegh, Raphael Santa Rosa; Tamaki, Fabio Kendi; Marana, Sandro Roberto ; Salinas, Roberto Kopke ; Arantes, Guilherme Menegon
Source: Biophysical Journal. Conference titles: Annual Meeting of the Biophysical Society. Unidade: IQ
Assunto: BIOINFORMÁTICA
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
ABNT
SAYEGH, Raphael Santa Rosa et al. Combining NMR and computer simulations to evaluate Cdc25B protein flexbility. Biophysical Journal. Cambridge: Instituto de Química, Universidade de São Paulo. . Acesso em: 11 nov. 2024. , 2014
APA
Sayegh, R. S. R., Tamaki, F. K., Marana, S. R., Salinas, R. K., & Arantes, G. M. (2014). Combining NMR and computer simulations to evaluate Cdc25B protein flexbility. Biophysical Journal. Cambridge: Instituto de Química, Universidade de São Paulo.
NLM
Sayegh RSR, Tamaki FK, Marana SR, Salinas RK, Arantes GM. Combining NMR and computer simulations to evaluate Cdc25B protein flexbility. Biophysical Journal. 2014 ; 106( 2): 688 res. 3487.[citado 2024 nov. 11 ]
Vancouver
Sayegh RSR, Tamaki FK, Marana SR, Salinas RK, Arantes GM. Combining NMR and computer simulations to evaluate Cdc25B protein flexbility. Biophysical Journal. 2014 ; 106( 2): 688 res. 3487.[citado 2024 nov. 11 ]
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: 11 nov. 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 nov. 11 ] 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 nov. 11 ] Available from: http://www.cell.com/biophysj/pdf/S0006-3495(13)05028-5.pdf
Trabalho de evento-resumo periodico
On the structural and biochemical properties of the human septins: SEPT3 (2013)
Macedo, Joci N. A.; Valadares, Napoleão F.; Marques, Ivo A.; Ferreira, Frederico M.; Damalio, Julio C. P.; Pereira, Humberto d'Muniz; Garratt, Richard Charles ; Araújo, Ana Paula Ulian de
Source: Biophysical Journal. Conference titles: Annual Meeting of the Biophysical Society. Unidade: IFSC
Subjects: PROTEÍNAS (HUMANO;ESTUDO), PROTEÍNAS RECOMBINANTES
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
ABNT
MACEDO, Joci N. A. et al. On the structural and biochemical properties of the human septins: SEPT3. Biophysical Journal. Saint Louis: Cell Press. Disponível em: https://doi.org/10.1016/j.bpj.2012.11.3144. Acesso em: 11 nov. 2024. , 2013
APA
Macedo, J. N. A., Valadares, N. F., Marques, I. A., Ferreira, F. M., Damalio, J. C. P., Pereira, H. d'M., et al. (2013). On the structural and biochemical properties of the human septins: SEPT3. Biophysical Journal. Saint Louis: Cell Press. doi:10.1016/j.bpj.2012.11.3144
NLM
Macedo JNA, Valadares NF, Marques IA, Ferreira FM, Damalio JCP, Pereira H d'M, Garratt RC, Araújo APU de. On the structural and biochemical properties of the human septins: SEPT3 [Internet]. Biophysical Journal. 2013 ; 104( Ja 2013): 567a.[citado 2024 nov. 11 ] Available from: https://doi.org/10.1016/j.bpj.2012.11.3144
Vancouver
Macedo JNA, Valadares NF, Marques IA, Ferreira FM, Damalio JCP, Pereira H d'M, Garratt RC, Araújo APU de. On the structural and biochemical properties of the human septins: SEPT3 [Internet]. Biophysical Journal. 2013 ; 104( Ja 2013): 567a.[citado 2024 nov. 11 ] Available from: https://doi.org/10.1016/j.bpj.2012.11.3144
Trabalho de evento-resumo periodico
Thionaphthoquinones destabilization of phospholipid bilayers (2013)
Di Vitta, Cláudio ; Marzorati, Liliana ; Funari, Sérgio S
Source: Biophysical Journal. Conference titles: Annual Meeting of the Biophysical Society. Unidade: IQ
Assunto: FOSFOLIPÍDEOS
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
ABNT
DI VITTA, Cláudio e MARZORATI, Liliana e FUNARI, Sérgio S. Thionaphthoquinones destabilization of phospholipid bilayers. Biophysical Journal. Cambridge: Instituto de Química, Universidade de São Paulo. . Acesso em: 11 nov. 2024. , 2013
APA
Di Vitta, C., Marzorati, L., & Funari, S. S. (2013). Thionaphthoquinones destabilization of phospholipid bilayers. Biophysical Journal. Cambridge: Instituto de Química, Universidade de São Paulo.
NLM
Di Vitta C, Marzorati L, Funari SS. Thionaphthoquinones destabilization of phospholipid bilayers. Biophysical Journal. 2013 ; 104 429a.[citado 2024 nov. 11 ]
Vancouver
Di Vitta C, Marzorati L, Funari SS. Thionaphthoquinones destabilization of phospholipid bilayers. Biophysical Journal. 2013 ; 104 429a.[citado 2024 nov. 11 ]
Trabalho de evento-resumo periodico
Synchrotron radiation circular dichroism spectroscopy of MEG14, an intrinsically disordered protein (2013)
Lopes, Jose Luiz S.; Orcia, D.; De Marco, Ricardo; Araújo, Ana Paula Ulian de
Source: Biophysical Journal. Conference titles: Annual Meeting of the Biophysical Society. Unidade: IFSC
Subjects: PROTEÍNAS (ESTUDO), ESPECTROSCOPIA, SCHISTOSOMA MANSONI
A citação é gerada automaticamente e pode não estar totalmente de acordo com as normas
ABNT
LOPES, Jose Luiz S. et al. Synchrotron radiation circular dichroism spectroscopy of MEG14, an intrinsically disordered protein. Biophysical Journal. Saint Louis: Cell Press. Disponível em: https://doi.org/10.1016/j.bpj.2012.11.1319. Acesso em: 11 nov. 2024. , 2013
APA
Lopes, J. L. S., Orcia, D., De Marco, R., & Araújo, A. P. U. de. (2013). Synchrotron radiation circular dichroism spectroscopy of MEG14, an intrinsically disordered protein. Biophysical Journal. Saint Louis: Cell Press. doi:10.1016/j.bpj.2012.11.1319
NLM
Lopes JLS, Orcia D, De Marco R, Araújo APU de. Synchrotron radiation circular dichroism spectroscopy of MEG14, an intrinsically disordered protein [Internet]. Biophysical Journal. 2013 ; 104( Ja 2013): 234a.[citado 2024 nov. 11 ] Available from: https://doi.org/10.1016/j.bpj.2012.11.1319
Vancouver
Lopes JLS, Orcia D, De Marco R, Araújo APU de. Synchrotron radiation circular dichroism spectroscopy of MEG14, an intrinsically disordered protein [Internet]. Biophysical Journal. 2013 ; 104( Ja 2013): 234a.[citado 2024 nov. 11 ] Available from: https://doi.org/10.1016/j.bpj.2012.11.1319

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