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Artigo de periodico
How and when to measure mitochondrial inner membrane potentials (2024)
Kowaltowski, Alicia Juliana ; Abdulkader, Fernando
Source: Biophysical Journal. Unidade: IQ
Subjects: MITOCÔNDRIAS, DOENÇAS METABÓLICAS
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KOWALTOWSKI, Alicia Juliana e ABDULKADER, Fernando. How and when to measure mitochondrial inner membrane potentials. Biophysical Journal, 2024Tradução . . Disponível em: https://dx.doi.org/10.1016/j.bpj.2024.03.011. Acesso em: 02 nov. 2024.
APA
Kowaltowski, A. J., & Abdulkader, F. (2024). How and when to measure mitochondrial inner membrane potentials. Biophysical Journal. doi:10.1016/j.bpj.2024.03.011
NLM
Kowaltowski AJ, Abdulkader F. How and when to measure mitochondrial inner membrane potentials [Internet]. Biophysical Journal. 2024 ;[citado 2024 nov. 02 ] Available from: https://dx.doi.org/10.1016/j.bpj.2024.03.011
Vancouver
Kowaltowski AJ, Abdulkader F. How and when to measure mitochondrial inner membrane potentials [Internet]. Biophysical Journal. 2024 ;[citado 2024 nov. 02 ] Available from: https://dx.doi.org/10.1016/j.bpj.2024.03.011
Artigo de periodico
A look at membrane curvature and remodeling with SuAVE — Surface Assessment Via grid Evaluation (2022)
Santos, Denys; Coutinho, Kaline Rabelo ; Soares, Thereza A.
Source: Biophysical Journal. Unidade: IF
Subjects: BIOFÍSICA, FÍSICO-QUÍMICA, MEMBRANAS CELULARES, LIPÍDEOS DA MEMBRANA, CURVATURA CONSTANTE, PROGRAMAÇÃO MATEMÁTICA, SIMULAÇÃO DE SISTEMAS
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SANTOS, Denys e COUTINHO, Kaline Rabelo e SOARES, Thereza A. A look at membrane curvature and remodeling with SuAVE — Surface Assessment Via grid Evaluation. Biophysical Journal, v. 121, n. 3, p. 6-6, 2022Tradução . . Disponível em: https://doi.org/10.1016/j.bpj.2021.11.2674. Acesso em: 02 nov. 2024.
APA
Santos, D., Coutinho, K. R., & Soares, T. A. (2022). A look at membrane curvature and remodeling with SuAVE — Surface Assessment Via grid Evaluation. Biophysical Journal, 121( 3), 6-6. doi:10.1016/j.bpj.2021.11.2674
NLM
Santos D, Coutinho KR, Soares TA. A look at membrane curvature and remodeling with SuAVE — Surface Assessment Via grid Evaluation [Internet]. Biophysical Journal. 2022 ; 121( 3): 6-6.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.bpj.2021.11.2674
Vancouver
Santos D, Coutinho KR, Soares TA. A look at membrane curvature and remodeling with SuAVE — Surface Assessment Via grid Evaluation [Internet]. Biophysical Journal. 2022 ; 121( 3): 6-6.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.bpj.2021.11.2674
Artigo de periodico
Molecular insights on CALX-CBD12 interdomain dynamics from MD simulations, RDCs, and SAXS (2021)
Degenhardt, Maximilia Frazão de Souza ; Vitale, Phelipe Augusto Mariano ; Abiko, Layara Akemi ; Zacharias, Martin; Sattler, Michael; Oliveira, Cristiano Luis Pinto de ; Salinas, Roberto Kopke
Source: Biophysical Journal. Unidades: IF, IQ
Subjects: MACROMOLÉCULA, EXTRUSÃO
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DEGENHARDT, Maximilia Frazão de Souza et al. Molecular insights on CALX-CBD12 interdomain dynamics from MD simulations, RDCs, and SAXS. Biophysical Journal, v. 120, n. 17, p. 3664-3675, 2021Tradução . . Disponível em: https://doi.org/10.1101/2020.12.18.423531. Acesso em: 02 nov. 2024.
APA
Degenhardt, M. F. de S., Vitale, P. A. M., Abiko, L. A., Zacharias, M., Sattler, M., Oliveira, C. L. P. de, & Salinas, R. K. (2021). Molecular insights on CALX-CBD12 interdomain dynamics from MD simulations, RDCs, and SAXS. Biophysical Journal, 120( 17), 3664-3675. doi:10.1101/2020.12.18.423531
NLM
Degenhardt MF de S, Vitale PAM, Abiko LA, Zacharias M, Sattler M, Oliveira CLP de, Salinas RK. Molecular insights on CALX-CBD12 interdomain dynamics from MD simulations, RDCs, and SAXS [Internet]. Biophysical Journal. 2021 ; 120( 17): 3664-3675.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1101/2020.12.18.423531
Vancouver
Degenhardt MF de S, Vitale PAM, Abiko LA, Zacharias M, Sattler M, Oliveira CLP de, Salinas RK. Molecular insights on CALX-CBD12 interdomain dynamics from MD simulations, RDCs, and SAXS [Internet]. Biophysical Journal. 2021 ; 120( 17): 3664-3675.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1101/2020.12.18.423531
Trabalho de evento-resumo periodico
Correlation Between Photosensitizer-Mediated Oxidative Stress and Aging Stress for Red Blood Cell Membrane Mechanical Property (2020)
Kinoshita, Koji; Scanavachi, Gustavo; Tsubone, Tayana M. ; Solovyeva, Vita; Brewer, Jonathan; Itri, Rosangela
Source: Biophysical Journal. Conference titles: 64th Annual Meeting of the Biophysical-Society. Unidade: IF
Subjects: BIOFÍSICA, FÍSICO-QUÍMICA ORGÂNICA, ESTRESSE OXIDATIVO, CÉLULAS SANGUÍNEAS, ESPALHAMENTO DE RAIOS X A BAIXOS ÂNGULOS, NANOPARTÍCULAS, PROTEÍNAS DA MEMBRANA, NANOPARTÍCULAS, NANOPARTÍCULAS, MEMBRANA PLASMÁTICA
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KINOSHITA, Koji et al. Correlation Between Photosensitizer-Mediated Oxidative Stress and Aging Stress for Red Blood Cell Membrane Mechanical Property. Biophysical Journal. Maryland: Biophysical Society. Disponível em: https://doi.org/10.1016/j.bpj.2019.11.2462. Acesso em: 02 nov. 2024. , 2020
APA
Kinoshita, K., Scanavachi, G., Tsubone, T. M., Solovyeva, V., Brewer, J., & Itri, R. (2020). Correlation Between Photosensitizer-Mediated Oxidative Stress and Aging Stress for Red Blood Cell Membrane Mechanical Property. Biophysical Journal. Maryland: Biophysical Society. doi:10.1016/j.bpj.2019.11.2462
NLM
Kinoshita K, Scanavachi G, Tsubone TM, Solovyeva V, Brewer J, Itri R. Correlation Between Photosensitizer-Mediated Oxidative Stress and Aging Stress for Red Blood Cell Membrane Mechanical Property [Internet]. Biophysical Journal. 2020 ; 118( 3): 439A-439A.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.bpj.2019.11.2462
Vancouver
Kinoshita K, Scanavachi G, Tsubone TM, Solovyeva V, Brewer J, Itri R. Correlation Between Photosensitizer-Mediated Oxidative Stress and Aging Stress for Red Blood Cell Membrane Mechanical Property [Internet]. Biophysical Journal. 2020 ; 118( 3): 439A-439A.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.bpj.2019.11.2462
Trabalho de evento-resumo periodico
Aluminium Interacts Differently with Lipid Bilayers and Modulates the Plasma Membrane Calcium ATPASE (PMCA) Activity (2020)
Sautu, Marilina de; Scanavachi, Gustavo; Gomes, Mariela Soledad Ferreira; Rossi, Juan Pablo F.; Itri, Rosangela ; Mangialavori, Irene C.
Source: Biophysical Journal. Conference titles: 64th Annual Meeting of the Biophysical-Society. Unidade: IF
Subjects: BIOFÍSICA, FÍSICO-QUÍMICA ORGÂNICA, ESPALHAMENTO DE RAIOS X A BAIXOS ÂNGULOS, PROTEÍNAS DA MEMBRANA, NANOPARTÍCULAS, MEMBRANA PLASMÁTICA, LIPÍDEOS DA MEMBRANA, ALUMÍNIO, CÁLCIO
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ABNT
SAUTU, Marilina de et al. Aluminium Interacts Differently with Lipid Bilayers and Modulates the Plasma Membrane Calcium ATPASE (PMCA) Activity. Biophysical Journal. Maryland: Biophysical Society. Disponível em: https://doi.org/10.1016/j.bpj.2019.11.2911. Acesso em: 02 nov. 2024. , 2020
APA
Sautu, M. de, Scanavachi, G., Gomes, M. S. F., Rossi, J. P. F., Itri, R., & Mangialavori, I. C. (2020). Aluminium Interacts Differently with Lipid Bilayers and Modulates the Plasma Membrane Calcium ATPASE (PMCA) Activity. Biophysical Journal. Maryland: Biophysical Society. doi:10.1016/j.bpj.2019.11.2911
NLM
Sautu M de, Scanavachi G, Gomes MSF, Rossi JPF, Itri R, Mangialavori IC. Aluminium Interacts Differently with Lipid Bilayers and Modulates the Plasma Membrane Calcium ATPASE (PMCA) Activity [Internet]. Biophysical Journal. 2020 ; 118( 3): 530A-530A.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.bpj.2019.11.2911
Vancouver
Sautu M de, Scanavachi G, Gomes MSF, Rossi JPF, Itri R, Mangialavori IC. Aluminium Interacts Differently with Lipid Bilayers and Modulates the Plasma Membrane Calcium ATPASE (PMCA) Activity [Internet]. Biophysical Journal. 2020 ; 118( 3): 530A-530A.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.bpj.2019.11.2911
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: 02 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. 02 ] 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. 02 ] Available from: https://doi.org/10.1016/j.bpj.2017.11.1640
Artigo de periodico
A negative slope conductance of the persistent sodium current prolongs subthreshold depolarizations (2017)
Ceballos, Cesar C.; Roque, Antonio Carlos; Leão, Ricardo Maurício Xavier
Source: Biophysical Journal. Unidades: FFCLRP, FMRP
Subjects: NEURÔNIOS, HIPOCAMPO, SÓDIO
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ABNT
CEBALLOS, Cesar C. e ROQUE, Antonio Carlos e LEÃO, Ricardo Maurício Xavier. A negative slope conductance of the persistent sodium current prolongs subthreshold depolarizations. Biophysical Journal, v. 113, n. 10, p. 2207-22017, 2017Tradução . . Disponível em: https://doi.org/10.1016/j.bpj.2017.06.047. Acesso em: 02 nov. 2024.
APA
Ceballos, C. C., Roque, A. C., & Leão, R. M. X. (2017). A negative slope conductance of the persistent sodium current prolongs subthreshold depolarizations. Biophysical Journal, 113( 10), 2207-22017. doi:10.1016/j.bpj.2017.06.047
NLM
Ceballos CC, Roque AC, Leão RMX. A negative slope conductance of the persistent sodium current prolongs subthreshold depolarizations [Internet]. Biophysical Journal. 2017 ; 113( 10): 2207-22017.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.bpj.2017.06.047
Vancouver
Ceballos CC, Roque AC, Leão RMX. A negative slope conductance of the persistent sodium current prolongs subthreshold depolarizations [Internet]. Biophysical Journal. 2017 ; 113( 10): 2207-22017.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.bpj.2017.06.047
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: 02 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. 02 ] 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. 02 ] 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: 02 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. 02 ] 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. 02 ] Available from: https://doi.org/10.1016/j.bpj.2015.11.1441
Artigo de periodico
Heterotypic coiled-coil formation is essential for the correct assembly of the septin heterofilament (2016)
Sala, Fernanda A.; Valadares, Napoleão F.; Macedo, Joci N. A.; Borges, Julio Cesar ; Garratt, Richard Charles
Source: Biophysical Journal. Unidades: IQSC, IFSC
Subjects: MACROMOLÉCULA, ESTRUTURA MOLECULAR (QUÍMICA TEÓRICA), PROTEÍNAS
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ABNT
SALA, Fernanda A. et al. Heterotypic coiled-coil formation is essential for the correct assembly of the septin heterofilament. Biophysical Journal, v. 111, n. 12, p. 2608-2619, 2016Tradução . . Disponível em: https://doi.org/10.1016/j.bpj.2016.10.032. Acesso em: 02 nov. 2024.
APA
Sala, F. A., Valadares, N. F., Macedo, J. N. A., Borges, J. C., & Garratt, R. C. (2016). Heterotypic coiled-coil formation is essential for the correct assembly of the septin heterofilament. Biophysical Journal, 111( 12), 2608-2619. doi:10.1016/j.bpj.2016.10.032
NLM
Sala FA, Valadares NF, Macedo JNA, Borges JC, Garratt RC. Heterotypic coiled-coil formation is essential for the correct assembly of the septin heterofilament [Internet]. Biophysical Journal. 2016 ; 111( 12): 2608-2619.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.bpj.2016.10.032
Vancouver
Sala FA, Valadares NF, Macedo JNA, Borges JC, Garratt RC. Heterotypic coiled-coil formation is essential for the correct assembly of the septin heterofilament [Internet]. Biophysical Journal. 2016 ; 111( 12): 2608-2619.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.bpj.2016.10.032
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: 02 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. 02 ]
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. 02 ]
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: 02 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. 02 ] 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. 02 ] 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: 02 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. 02 ]
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. 02 ]
Artigo de periodico
Structural and thermodynamic properties of septin 3 investigated by small-angle x-Ray scattering (2015)
Ortore, Maria Grazia; Macedo, Joci N. A.; Araújo, Ana Paula Ulian de ; Ferrero, Claudio; Mariani, Paolo; Spinozzi, Francesco; Itri, Rosangela
Source: Biophysical Journal. Unidades: IFSC, IF
Subjects: PROTEÍNAS (PROPRIEDADES), ESTRUTURA MOLECULAR (FÍSICA MODERNA), RAIOS X
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ABNT
ORTORE, Maria Grazia et al. Structural and thermodynamic properties of septin 3 investigated by small-angle x-Ray scattering. Biophysical Journal, v. 108, n. 12, p. 2896-2902, 2015Tradução . . Disponível em: https://doi.org/10.1016/j.bpj.2015.05.015. Acesso em: 02 nov. 2024.
APA
Ortore, M. G., Macedo, J. N. A., Araújo, A. P. U. de, Ferrero, C., Mariani, P., Spinozzi, F., & Itri, R. (2015). Structural and thermodynamic properties of septin 3 investigated by small-angle x-Ray scattering. Biophysical Journal, 108( 12), 2896-2902. doi:10.1016/j.bpj.2015.05.015
NLM
Ortore MG, Macedo JNA, Araújo APU de, Ferrero C, Mariani P, Spinozzi F, Itri R. Structural and thermodynamic properties of septin 3 investigated by small-angle x-Ray scattering [Internet]. Biophysical Journal. 2015 ; 108( 12): 2896-2902.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.bpj.2015.05.015
Vancouver
Ortore MG, Macedo JNA, Araújo APU de, Ferrero C, Mariani P, Spinozzi F, Itri R. Structural and thermodynamic properties of septin 3 investigated by small-angle x-Ray scattering [Internet]. Biophysical Journal. 2015 ; 108( 12): 2896-2902.[citado 2024 nov. 02 ] Available from: https://doi.org/10.1016/j.bpj.2015.05.015
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: 02 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. 02 ] 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. 02 ] 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: 02 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. 02 ] 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. 02 ] 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: 02 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. 02 ] 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. 02 ] 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: 02 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. 02 ] 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. 02 ] 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: 02 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. 02 ] 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. 02 ] 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: 02 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. 02 ] 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. 02 ] Available from: http://www.cell.com/biophysj/pdf/S0006-3495(13)05028-5.pdf

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