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Artigo de periodico
rBPI21 interacts with negative membranes endothermically promoting the formation of rigid multilamellar structures (2013)
Domingues, Marco M; Bianconi, M. Lucia; Barbosa, Leandro Ramos Souza ; Santiago, Patricia Soares; Tabak, Marcel; Castanho, Miguel A. R. Botas; Itri, Rosangela ; Santos, Nuno C
Fonte: Biochimica et Biophysica Acta - Biomembranes. Unidades: IF, IQSC
Assuntos: LIPOPOLISSACARÍDEOS, BIOQUÍMICA
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ABNT
DOMINGUES, Marco M et al. rBPI21 interacts with negative membranes endothermically promoting the formation of rigid multilamellar structures. Biochimica et Biophysica Acta - Biomembranes, v. 1828, n. 11, p. 2419-2427, 2013Tradução . . Disponível em: https://doi.org/10.1016/j.bbamem.2013.06.009. Acesso em: 05 nov. 2025.
APA
Domingues, M. M., Bianconi, M. L., Barbosa, L. R. S., Santiago, P. S., Tabak, M., Castanho, M. A. R. B., et al. (2013). rBPI21 interacts with negative membranes endothermically promoting the formation of rigid multilamellar structures. Biochimica et Biophysica Acta - Biomembranes, 1828( 11), 2419-2427. doi:10.1016/j.bbamem.2013.06.009
NLM
Domingues MM, Bianconi ML, Barbosa LRS, Santiago PS, Tabak M, Castanho MARB, Itri R, Santos NC. rBPI21 interacts with negative membranes endothermically promoting the formation of rigid multilamellar structures [Internet]. Biochimica et Biophysica Acta - Biomembranes. 2013 ; 1828( 11): 2419-2427.[citado 2025 nov. 05 ] Available from: https://doi.org/10.1016/j.bbamem.2013.06.009
Vancouver
Domingues MM, Bianconi ML, Barbosa LRS, Santiago PS, Tabak M, Castanho MARB, Itri R, Santos NC. rBPI21 interacts with negative membranes endothermically promoting the formation of rigid multilamellar structures [Internet]. Biochimica et Biophysica Acta - Biomembranes. 2013 ; 1828( 11): 2419-2427.[citado 2025 nov. 05 ] Available from: https://doi.org/10.1016/j.bbamem.2013.06.009
Artigo de periodico
Structural and stability studies of the human mtHsp70-escort protein 1: an essential mortalin co-chaperone (2013)
Dores-Silva, Paulo Roberto ; Minari, Karine ; Ramos, Carlos Henrique Inacio ; Barbosa, Leandro Ramos Souza ; Borges, Julio Cesar
Fonte: International Journal of Biological Macromolecules. Unidades: IF, IQSC
Assunto: BIOLOGIA MOLECULAR
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ABNT
DORES-SILVA, Paulo Roberto et al. Structural and stability studies of the human mtHsp70-escort protein 1: an essential mortalin co-chaperone. International Journal of Biological Macromolecules, v. 56, p. 140-148, 2013Tradução . . Disponível em: https://doi.org/10.1016/j.ijbiomac.2013.02.009. Acesso em: 05 nov. 2025.
APA
Dores-Silva, P. R., Minari, K., Ramos, C. H. I., Barbosa, L. R. S., & Borges, J. C. (2013). Structural and stability studies of the human mtHsp70-escort protein 1: an essential mortalin co-chaperone. International Journal of Biological Macromolecules, 56, 140-148. doi:10.1016/j.ijbiomac.2013.02.009
NLM
Dores-Silva PR, Minari K, Ramos CHI, Barbosa LRS, Borges JC. Structural and stability studies of the human mtHsp70-escort protein 1: an essential mortalin co-chaperone [Internet]. International Journal of Biological Macromolecules. 2013 ; 56 140-148.[citado 2025 nov. 05 ] Available from: https://doi.org/10.1016/j.ijbiomac.2013.02.009
Vancouver
Dores-Silva PR, Minari K, Ramos CHI, Barbosa LRS, Borges JC. Structural and stability studies of the human mtHsp70-escort protein 1: an essential mortalin co-chaperone [Internet]. International Journal of Biological Macromolecules. 2013 ; 56 140-148.[citado 2025 nov. 05 ] Available from: https://doi.org/10.1016/j.ijbiomac.2013.02.009
Artigo de periodico
LPS-protein aggregation influences protein partitioning in aqueous two-phase micellar systems (2013)
Lopes, André Moreni ; Santos-Ebinuma, Valéria de Carvalho; Novaes, Letícia Celia de Lencastre ; Molino, João Vitor Dutra ; Barbosa, Leandro Ramos Souza ; Pessoa Junior, Adalberto ; Rangel-Yagui, Carlota de Oliveira
Fonte: Applied Microbiology and Biotechnology. Unidades: IF, FCF
Assuntos: PROTEÍNAS DE FLUORESCÊNCIA VERDE, ENDOTOXINAS
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ABNT
LOPES, André Moreni et al. LPS-protein aggregation influences protein partitioning in aqueous two-phase micellar systems. Applied Microbiology and Biotechnology, v. 97, n. 14, p. 6201-6209, 2013Tradução . . Disponível em: https://doi.org/10.1007/s00253-013-4922-x. Acesso em: 05 nov. 2025.
APA
Lopes, A. M., Santos-Ebinuma, V. de C., Novaes, L. C. de L., Molino, J. V. D., Barbosa, L. R. S., Pessoa Junior, A., & Rangel-Yagui, C. de O. (2013). LPS-protein aggregation influences protein partitioning in aqueous two-phase micellar systems. Applied Microbiology and Biotechnology, 97( 14), 6201-6209. doi:10.1007/s00253-013-4922-x
NLM
Lopes AM, Santos-Ebinuma V de C, Novaes LC de L, Molino JVD, Barbosa LRS, Pessoa Junior A, Rangel-Yagui C de O. LPS-protein aggregation influences protein partitioning in aqueous two-phase micellar systems [Internet]. Applied Microbiology and Biotechnology. 2013 ; 97( 14): 6201-6209.[citado 2025 nov. 05 ] Available from: https://doi.org/10.1007/s00253-013-4922-x
Vancouver
Lopes AM, Santos-Ebinuma V de C, Novaes LC de L, Molino JVD, Barbosa LRS, Pessoa Junior A, Rangel-Yagui C de O. LPS-protein aggregation influences protein partitioning in aqueous two-phase micellar systems [Internet]. Applied Microbiology and Biotechnology. 2013 ; 97( 14): 6201-6209.[citado 2025 nov. 05 ] Available from: https://doi.org/10.1007/s00253-013-4922-x
Trabalho de evento-anais periodico
The influence of both urea and 2,2,2-trifluoroethanol in the amyloid fibril formation of bovine serum albumin (2013)
Brito, Lenilson Tôrres; Barbosa, Leandro Ramos Souza
Fonte: CELL PRESS. Nome do evento: Annual Meeting of the Biophysical-Society LVII. Unidade: IF
Assuntos: ESPECTROSCOPIA, FLUORESCÊNCIA
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ABNT
BRITO, Lenilson Tôrres e BARBOSA, Leandro Ramos Souza. The influence of both urea and 2,2,2-trifluoroethanol in the amyloid fibril formation of bovine serum albumin. CELL PRESS. Massachusetts: CELL PRESS. Disponível em: http://www.sciencedirect.com/science/article/pii/S0006349512034030. Acesso em: 05 nov. 2025. , 2013
APA
Brito, L. T., & Barbosa, L. R. S. (2013). The influence of both urea and 2,2,2-trifluoroethanol in the amyloid fibril formation of bovine serum albumin. CELL PRESS. Massachusetts: CELL PRESS. Recuperado de http://www.sciencedirect.com/science/article/pii/S0006349512034030
NLM
Brito LT, Barbosa LRS. The influence of both urea and 2,2,2-trifluoroethanol in the amyloid fibril formation of bovine serum albumin [Internet]. CELL PRESS. 2013 ;104( ja 2013): 387A .[citado 2025 nov. 05 ] Available from: http://www.sciencedirect.com/science/article/pii/S0006349512034030
Vancouver
Brito LT, Barbosa LRS. The influence of both urea and 2,2,2-trifluoroethanol in the amyloid fibril formation of bovine serum albumin [Internet]. CELL PRESS. 2013 ;104( ja 2013): 387A .[citado 2025 nov. 05 ] Available from: http://www.sciencedirect.com/science/article/pii/S0006349512034030
Artigo de periodico
Low resolution structural studies indicate that the activator of Hsp90 ATPase 1 (Aha1) of leishmania braziliensis Has an elongated shape which allows its interaction with both N- and M-domains of Hsp90 (2013)
Seraphim, Thiago Vargas ; Alves, Marina M; Silva, Indjara Mallmann da; Gomes, Francisco Edvan Rodrigues; Silva, Kelly Prata; Murta, Silvane M. F; Barbosa, Leandro Ramos Souza ; Borges, Julio Cesar
Fonte: PLoS ONE. Unidades: IF, IQSC
Assuntos: PROTEÍNAS, LEISHMANIA BRASILIENSIS
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ABNT
SERAPHIM, Thiago Vargas et al. Low resolution structural studies indicate that the activator of Hsp90 ATPase 1 (Aha1) of leishmania braziliensis Has an elongated shape which allows its interaction with both N- and M-domains of Hsp90. PLoS ONE, v. 8, n. 6, p. e 66822, 2013Tradução . . Disponível em: https://doi.org/10.1371/journal.pone.0066822. Acesso em: 05 nov. 2025.
APA
Seraphim, T. V., Alves, M. M., Silva, I. M. da, Gomes, F. E. R., Silva, K. P., Murta, S. M. F., et al. (2013). Low resolution structural studies indicate that the activator of Hsp90 ATPase 1 (Aha1) of leishmania braziliensis Has an elongated shape which allows its interaction with both N- and M-domains of Hsp90. PLoS ONE, 8( 6), e 66822. doi:10.1371/journal.pone.0066822
NLM
Seraphim TV, Alves MM, Silva IM da, Gomes FER, Silva KP, Murta SMF, Barbosa LRS, Borges JC. Low resolution structural studies indicate that the activator of Hsp90 ATPase 1 (Aha1) of leishmania braziliensis Has an elongated shape which allows its interaction with both N- and M-domains of Hsp90 [Internet]. PLoS ONE. 2013 ; 8( 6): e 66822.[citado 2025 nov. 05 ] Available from: https://doi.org/10.1371/journal.pone.0066822
Vancouver
Seraphim TV, Alves MM, Silva IM da, Gomes FER, Silva KP, Murta SMF, Barbosa LRS, Borges JC. Low resolution structural studies indicate that the activator of Hsp90 ATPase 1 (Aha1) of leishmania braziliensis Has an elongated shape which allows its interaction with both N- and M-domains of Hsp90 [Internet]. PLoS ONE. 2013 ; 8( 6): e 66822.[citado 2025 nov. 05 ] Available from: https://doi.org/10.1371/journal.pone.0066822
Parte de monografia/livro
Small-Angle X-Ray Scattering Applied to Proteins in Solution (2013)
Barbosa, Leandro Ramos Souza ; Spinozzi, Francesco; Mariani, Paolo; Itri, Rosangela
Fonte: Proteins in Solution and at Interfaces: Methods and Applications in Biotechnology and Materials Science. Unidade: IF
Assuntos: BIOTECNOLOGIA, ALBUMINAS, PROTEÍNAS, ESPALHAMENTO DE RAIOS X A BAIXOS ÂNGULOS
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ABNT
BARBOSA, Leandro Ramos Souza et al. Small-Angle X-Ray Scattering Applied to Proteins in Solution. Proteins in Solution and at Interfaces: Methods and Applications in Biotechnology and Materials Science. Tradução . Hoboken, NJ: John Wiley & Sons, 2013. . Disponível em: http://onlinelibrary.wiley.com/doi/10.1002/9781118523063.ch3/summary. Acesso em: 05 nov. 2025.
APA
Barbosa, L. R. S., Spinozzi, F., Mariani, P., & Itri, R. (2013). Small-Angle X-Ray Scattering Applied to Proteins in Solution. In Proteins in Solution and at Interfaces: Methods and Applications in Biotechnology and Materials Science. Hoboken, NJ: John Wiley & Sons. Recuperado de http://onlinelibrary.wiley.com/doi/10.1002/9781118523063.ch3/summary
NLM
Barbosa LRS, Spinozzi F, Mariani P, Itri R. Small-Angle X-Ray Scattering Applied to Proteins in Solution [Internet]. In: Proteins in Solution and at Interfaces: Methods and Applications in Biotechnology and Materials Science. Hoboken, NJ: John Wiley & Sons; 2013. [citado 2025 nov. 05 ] Available from: http://onlinelibrary.wiley.com/doi/10.1002/9781118523063.ch3/summary
Vancouver
Barbosa LRS, Spinozzi F, Mariani P, Itri R. Small-Angle X-Ray Scattering Applied to Proteins in Solution [Internet]. In: Proteins in Solution and at Interfaces: Methods and Applications in Biotechnology and Materials Science. Hoboken, NJ: John Wiley & Sons; 2013. [citado 2025 nov. 05 ] Available from: http://onlinelibrary.wiley.com/doi/10.1002/9781118523063.ch3/summary

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