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Artigo de periodico
Extension of sticholysins N-terminal α-helix signals membrane lipids to acquire curvature for toroidal pore formation (2025)
Schreier, Shirley ; Paulino, Joana ; Carretero, Gustavo P.B ; Barbosa, Leandro Ramos Souza ; Cilli, Eduardo Maffud ; Alvarez, Carlos; Ros, Uris
Fonte: Biochemical and Biophysical Research Communications. Unidades: IQ, IF
Assuntos: PROTEÍNAS, LIPÍDEOS
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ABNT
SCHREIER, Shirley et al. Extension of sticholysins N-terminal α-helix signals membrane lipids to acquire curvature for toroidal pore formation. Biochemical and Biophysical Research Communications, v. 742, p. 1-11 art. 151071, 2025Tradução . . Disponível em: https://dx.doi.org/10.1016/j.bbrc.2024.151071. Acesso em: 19 nov. 2025.
APA
Schreier, S., Paulino, J., Carretero, G. P. B., Barbosa, L. R. S., Cilli, E. M., Alvarez, C., & Ros, U. (2025). Extension of sticholysins N-terminal α-helix signals membrane lipids to acquire curvature for toroidal pore formation. Biochemical and Biophysical Research Communications, 742, 1-11 art. 151071. doi:10.1016/j.bbrc.2024.151071
NLM
Schreier S, Paulino J, Carretero GPB, Barbosa LRS, Cilli EM, Alvarez C, Ros U. Extension of sticholysins N-terminal α-helix signals membrane lipids to acquire curvature for toroidal pore formation [Internet]. Biochemical and Biophysical Research Communications. 2025 ; 742 1-11 art. 151071.[citado 2025 nov. 19 ] Available from: https://dx.doi.org/10.1016/j.bbrc.2024.151071
Vancouver
Schreier S, Paulino J, Carretero GPB, Barbosa LRS, Cilli EM, Alvarez C, Ros U. Extension of sticholysins N-terminal α-helix signals membrane lipids to acquire curvature for toroidal pore formation [Internet]. Biochemical and Biophysical Research Communications. 2025 ; 742 1-11 art. 151071.[citado 2025 nov. 19 ] Available from: https://dx.doi.org/10.1016/j.bbrc.2024.151071
Artigo de periodico
Sorghum bicolor SbHSP110 has an elongated shape and is able of protecting against aggregation and replacing human HSPH1/HSP110 in refolding and disaggregation assays (2023)
Franco, Juliana C.; Barbosa, Leandro Ramos Souza
Fonte: Biopolymers. Unidade: IF
Assuntos: BIOFÍSICA, BIOPOLÍMEROS, PROTEÍNAS, BIOLOGIA MOLECULAR
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ABNT
FRANCO, Juliana C. e BARBOSA, Leandro Ramos Souza. Sorghum bicolor SbHSP110 has an elongated shape and is able of protecting against aggregation and replacing human HSPH1/HSP110 in refolding and disaggregation assays. Biopolymers, v. 114, n. 2, 2023Tradução . . Disponível em: https://doi.org/10.1002/bip.23532. Acesso em: 19 nov. 2025.
APA
Franco, J. C., & Barbosa, L. R. S. (2023). Sorghum bicolor SbHSP110 has an elongated shape and is able of protecting against aggregation and replacing human HSPH1/HSP110 in refolding and disaggregation assays. Biopolymers, 114( 2). doi:10.1002/bip.23532
NLM
Franco JC, Barbosa LRS. Sorghum bicolor SbHSP110 has an elongated shape and is able of protecting against aggregation and replacing human HSPH1/HSP110 in refolding and disaggregation assays [Internet]. Biopolymers. 2023 ; 114( 2):[citado 2025 nov. 19 ] Available from: https://doi.org/10.1002/bip.23532
Vancouver
Franco JC, Barbosa LRS. Sorghum bicolor SbHSP110 has an elongated shape and is able of protecting against aggregation and replacing human HSPH1/HSP110 in refolding and disaggregation assays [Internet]. Biopolymers. 2023 ; 114( 2):[citado 2025 nov. 19 ] Available from: https://doi.org/10.1002/bip.23532
Artigo de periodico
Assembly principles of the human R2TP chaperone complex reveal the presence of R2T and R2P complexes (2022)
Seraphim, Thiago V ; Nano, Nardin; Cheung, Yiu Wing Sunny; Aluksanasuwan, Siripat; Colleti, Carolina; Mao, Yu-Qian; Bhandari, Vaibhav; Young, Gavin; Holl, Larissa; Phanse, Sadhna; Gordiyenko, Yuliya; Southworth, Daniel R.; Robinson, Carol V.; Thongboonkerd, Visith; Gava, Lisandra M ; Borges, Julio Cesar ; Babu, Mohan; Barbosa, Leandro Ramos Souza ; Ramos, Carlos H. I. ; Kukura, Philipp; Houry, Walid A.
Fonte: Structure. Unidades: IQSC, IF
Assuntos: BIOQUÍMICA, BIOFÍSICA, MACROMOLÉCULA, PROTEÍNAS
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ABNT
SERAPHIM, Thiago V et al. Assembly principles of the human R2TP chaperone complex reveal the presence of R2T and R2P complexes. Structure, v. 30, p. 156–171, 2022Tradução . . Disponível em: https://doi.org/10.1016/j.str.2021.08.002. Acesso em: 19 nov. 2025.
APA
Seraphim, T. V., Nano, N., Cheung, Y. W. S., Aluksanasuwan, S., Colleti, C., Mao, Y. -Q., et al. (2022). Assembly principles of the human R2TP chaperone complex reveal the presence of R2T and R2P complexes. Structure, 30, 156–171. doi:10.1016/j.str.2021.08.002
NLM
Seraphim TV, Nano N, Cheung YWS, Aluksanasuwan S, Colleti C, Mao Y-Q, Bhandari V, Young G, Holl L, Phanse S, Gordiyenko Y, Southworth DR, Robinson CV, Thongboonkerd V, Gava LM, Borges JC, Babu M, Barbosa LRS, Ramos CHI, Kukura P, Houry WA. Assembly principles of the human R2TP chaperone complex reveal the presence of R2T and R2P complexes [Internet]. Structure. 2022 ; 30 156–171.[citado 2025 nov. 19 ] Available from: https://doi.org/10.1016/j.str.2021.08.002
Vancouver
Seraphim TV, Nano N, Cheung YWS, Aluksanasuwan S, Colleti C, Mao Y-Q, Bhandari V, Young G, Holl L, Phanse S, Gordiyenko Y, Southworth DR, Robinson CV, Thongboonkerd V, Gava LM, Borges JC, Babu M, Barbosa LRS, Ramos CHI, Kukura P, Houry WA. Assembly principles of the human R2TP chaperone complex reveal the presence of R2T and R2P complexes [Internet]. Structure. 2022 ; 30 156–171.[citado 2025 nov. 19 ] Available from: https://doi.org/10.1016/j.str.2021.08.002
Artigo de periodico
Structural, thermodynamic and functional studies of human 71 kDa heat shock cognate protein (HSPA8/hHsc70) (2021)
Silva, Noeli Soares Melo da ; Rodrigues, Luiz Fernando de Camargo ; Silva, Paulo Roberto Dores ; Montanari, Carlos Alberto ; Ramos, Carlos Henrique Inacio; Barbosa, Leandro Ramos Souza ; Borges, Julio Cesar
Fonte: Biochimica et Biophysica Acta - Proteins and Proteomics. Unidades: IQSC, IF, FM
Assuntos: BIOQUÍMICA, PROTEÍNAS
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ABNT
SILVA, Noeli Soares Melo da et al. Structural, thermodynamic and functional studies of human 71 kDa heat shock cognate protein (HSPA8/hHsc70). Biochimica et Biophysica Acta - Proteins and Proteomics, v. 1869, 2021Tradução . . Disponível em: https://doi.org/10.1016/j.bbapap.2021.140719. Acesso em: 19 nov. 2025.
APA
Silva, N. S. M. da, Rodrigues, L. F. de C., Silva, P. R. D., Montanari, C. A., Ramos, C. H. I., Barbosa, L. R. S., & Borges, J. C. (2021). Structural, thermodynamic and functional studies of human 71 kDa heat shock cognate protein (HSPA8/hHsc70). Biochimica et Biophysica Acta - Proteins and Proteomics, 1869. doi:10.1016/j.bbapap.2021.140719
NLM
Silva NSM da, Rodrigues LF de C, Silva PRD, Montanari CA, Ramos CHI, Barbosa LRS, Borges JC. Structural, thermodynamic and functional studies of human 71 kDa heat shock cognate protein (HSPA8/hHsc70) [Internet]. Biochimica et Biophysica Acta - Proteins and Proteomics. 2021 ; 1869[citado 2025 nov. 19 ] Available from: https://doi.org/10.1016/j.bbapap.2021.140719
Vancouver
Silva NSM da, Rodrigues LF de C, Silva PRD, Montanari CA, Ramos CHI, Barbosa LRS, Borges JC. Structural, thermodynamic and functional studies of human 71 kDa heat shock cognate protein (HSPA8/hHsc70) [Internet]. Biochimica et Biophysica Acta - Proteins and Proteomics. 2021 ; 1869[citado 2025 nov. 19 ] Available from: https://doi.org/10.1016/j.bbapap.2021.140719
Artigo de periodico
Insights into the structure and function of the C-terminus of SGTs (small glutamine-rich TPR-containing proteins): A study of the Aedes aegypti homolog (2021)
Quel, Natália G.; Rodrigues, Luiz Fernando de Camargo ; Aragão, Annelize Z. B.; Pinheiro, Glaucia M. S.; Camacho, Rafael P.; Souto, Denio E. P.; Kubota, Lauro Tatsuo; Barbosa, Leandro Ramos Souza ; Ramos, Carlos H. I.
Fonte: Biochimie. Unidade: IF
Assuntos: BIOFÍSICA, BIOQUÍMICA, FÍSICA MOLECULAR, PROTEÍNAS, PROTEÍNAS, PROTEÍNAS, GLUTAMINA, AEDES, MEMBRANAS CELULARES, ESPALHAMENTO DE RAIOS X A BAIXOS ÂNGULOS
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ABNT
QUEL, Natália G. et al. Insights into the structure and function of the C-terminus of SGTs (small glutamine-rich TPR-containing proteins): A study of the Aedes aegypti homolog. Biochimie, v. 187, p. 131-143, 2021Tradução . . Disponível em: https://doi.org/10.1016/j.biochi.2021.05.012. Acesso em: 19 nov. 2025.
APA
Quel, N. G., Rodrigues, L. F. de C., Aragão, A. Z. B., Pinheiro, G. M. S., Camacho, R. P., Souto, D. E. P., et al. (2021). Insights into the structure and function of the C-terminus of SGTs (small glutamine-rich TPR-containing proteins): A study of the Aedes aegypti homolog. Biochimie, 187, 131-143. doi:10.1016/j.biochi.2021.05.012
NLM
Quel NG, Rodrigues LF de C, Aragão AZB, Pinheiro GMS, Camacho RP, Souto DEP, Kubota LT, Barbosa LRS, Ramos CHI. Insights into the structure and function of the C-terminus of SGTs (small glutamine-rich TPR-containing proteins): A study of the Aedes aegypti homolog [Internet]. Biochimie. 2021 ; 187 131-143.[citado 2025 nov. 19 ] Available from: https://doi.org/10.1016/j.biochi.2021.05.012
Vancouver
Quel NG, Rodrigues LF de C, Aragão AZB, Pinheiro GMS, Camacho RP, Souto DEP, Kubota LT, Barbosa LRS, Ramos CHI. Insights into the structure and function of the C-terminus of SGTs (small glutamine-rich TPR-containing proteins): A study of the Aedes aegypti homolog [Internet]. Biochimie. 2021 ; 187 131-143.[citado 2025 nov. 19 ] Available from: https://doi.org/10.1016/j.biochi.2021.05.012
Artigo de periodico
Structural studies of the Hsp70/Hsp90 organizing protein of Plasmodium falciparum and its modulation of Hsp70 and Hsp90 ATPase activities (2020)
Silva, Noeli Soares Melo da; Reis, Dayane Eliara Bertolino; Silva, Paulo R. D; Annetta, Fátima Beatriz; Seraphim, Thiago Vargas; Barbosa, Leandro Ramos Souza ; Borges, Julio Cesar
Fonte: Biochimica et Biophysica Acta - Proteins and Proteomics. Unidades: IF, IQSC, Interunidades em Bioinformática
Assunto: PROTEÍNAS
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ABNT
SILVA, Noeli Soares Melo da et al. Structural studies of the Hsp70/Hsp90 organizing protein of Plasmodium falciparum and its modulation of Hsp70 and Hsp90 ATPase activities. Biochimica et Biophysica Acta - Proteins and Proteomics, v. 1868, n. 1, p. 140282, 2020Tradução . . Disponível em: https://doi.org/10.1016/j.bbapap.2019.140282. Acesso em: 19 nov. 2025.
APA
Silva, N. S. M. da, Reis, D. E. B., Silva, P. R. D., Annetta, F. B., Seraphim, T. V., Barbosa, L. R. S., & Borges, J. C. (2020). Structural studies of the Hsp70/Hsp90 organizing protein of Plasmodium falciparum and its modulation of Hsp70 and Hsp90 ATPase activities. Biochimica et Biophysica Acta - Proteins and Proteomics, 1868( 1), 140282. doi:10.1016/j.bbapap.2019.140282
NLM
Silva NSM da, Reis DEB, Silva PRD, Annetta FB, Seraphim TV, Barbosa LRS, Borges JC. Structural studies of the Hsp70/Hsp90 organizing protein of Plasmodium falciparum and its modulation of Hsp70 and Hsp90 ATPase activities [Internet]. Biochimica et Biophysica Acta - Proteins and Proteomics. 2020 ; 1868( 1): 140282.[citado 2025 nov. 19 ] Available from: https://doi.org/10.1016/j.bbapap.2019.140282
Vancouver
Silva NSM da, Reis DEB, Silva PRD, Annetta FB, Seraphim TV, Barbosa LRS, Borges JC. Structural studies of the Hsp70/Hsp90 organizing protein of Plasmodium falciparum and its modulation of Hsp70 and Hsp90 ATPase activities [Internet]. Biochimica et Biophysica Acta - Proteins and Proteomics. 2020 ; 1868( 1): 140282.[citado 2025 nov. 19 ] Available from: https://doi.org/10.1016/j.bbapap.2019.140282
Artigo de periodico
Solution structure of Plasmodium falciparum Hsp90 indicates a high flexible dimer (2020)
Silva, Noeli Soares Melo da; Torricillas, Marcela da Silva; Minari, Karine; Barbosa, Leandro Ramos Souza ; Seraphim, Thiago V; Borges, Julio Cesar
Fonte: Archives of Biochemistry and Biophysics. Unidades: IQSC, IF
Assunto: PROTEÍNAS
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ABNT
SILVA, Noeli Soares Melo da et al. Solution structure of Plasmodium falciparum Hsp90 indicates a high flexible dimer. Archives of Biochemistry and Biophysics, v. 690, p. 108468, 2020Tradução . . Disponível em: https://doi.org/10.1016/j.abb.2020.108468. Acesso em: 19 nov. 2025.
APA
Silva, N. S. M. da, Torricillas, M. da S., Minari, K., Barbosa, L. R. S., Seraphim, T. V., & Borges, J. C. (2020). Solution structure of Plasmodium falciparum Hsp90 indicates a high flexible dimer. Archives of Biochemistry and Biophysics, 690, 108468. doi:10.1016/j.abb.2020.108468
NLM
Silva NSM da, Torricillas M da S, Minari K, Barbosa LRS, Seraphim TV, Borges JC. Solution structure of Plasmodium falciparum Hsp90 indicates a high flexible dimer [Internet]. Archives of Biochemistry and Biophysics. 2020 ; 690 108468.[citado 2025 nov. 19 ] Available from: https://doi.org/10.1016/j.abb.2020.108468
Vancouver
Silva NSM da, Torricillas M da S, Minari K, Barbosa LRS, Seraphim TV, Borges JC. Solution structure of Plasmodium falciparum Hsp90 indicates a high flexible dimer [Internet]. Archives of Biochemistry and Biophysics. 2020 ; 690 108468.[citado 2025 nov. 19 ] Available from: https://doi.org/10.1016/j.abb.2020.108468
Trabalho de evento-resumo
Teaching an old dog new tricks: new strategies for saxs data analysis of proteins in solution (2020)
Rodrigues, Luiz F. C.; Silva, Noeli Soares Melo da ; Dores-Silva, Paulo R ; Quel, Natália Galdi ; Pinheiro, Glaucia M. S ; Borges, Julio Cesar ; Ramos, Carlos H. I. ; Barbosa, Leandro Ramos Souza
Fonte: Abstract Book. Nome do evento: RAU Annual Users Meeting LNLS/CNPEM. Unidades: IQSC, IF
Assuntos: ESPALHAMENTO DE RAIOS X A BAIXOS ÂNGULOS, PROTEÍNAS
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ABNT
RODRIGUES, Luiz F. C. et al. Teaching an old dog new tricks: new strategies for saxs data analysis of proteins in solution. 2020, Anais.. Campinas: Instituto de Química de São Carlos, Universidade de São Paulo, 2020. Disponível em: http://pages.cnpem.br/rau/wp-content/uploads/sites/8/2020/12/30thRAU_Abstract-BookV2.pdf. Acesso em: 19 nov. 2025.
APA
Rodrigues, L. F. C., Silva, N. S. M. da, Dores-Silva, P. R., Quel, N. G., Pinheiro, G. M. S., Borges, J. C., et al. (2020). Teaching an old dog new tricks: new strategies for saxs data analysis of proteins in solution. In Abstract Book. Campinas: Instituto de Química de São Carlos, Universidade de São Paulo. Recuperado de http://pages.cnpem.br/rau/wp-content/uploads/sites/8/2020/12/30thRAU_Abstract-BookV2.pdf
NLM
Rodrigues LFC, Silva NSM da, Dores-Silva PR, Quel NG, Pinheiro GMS, Borges JC, Ramos CHI, Barbosa LRS. Teaching an old dog new tricks: new strategies for saxs data analysis of proteins in solution [Internet]. Abstract Book. 2020 ;[citado 2025 nov. 19 ] Available from: http://pages.cnpem.br/rau/wp-content/uploads/sites/8/2020/12/30thRAU_Abstract-BookV2.pdf
Vancouver
Rodrigues LFC, Silva NSM da, Dores-Silva PR, Quel NG, Pinheiro GMS, Borges JC, Ramos CHI, Barbosa LRS. Teaching an old dog new tricks: new strategies for saxs data analysis of proteins in solution [Internet]. Abstract Book. 2020 ;[citado 2025 nov. 19 ] Available from: http://pages.cnpem.br/rau/wp-content/uploads/sites/8/2020/12/30thRAU_Abstract-BookV2.pdf
Artigo de periodico
Studies on the effect of the J-domain on the substrate binding domain (SBD) of Hsp70 using a chimeric human J-SBD polypeptide (2019)
Tiroli-Cepeda, Ana Olivia; Seraphim, Thiago Vargas; Pinheiro, Glaucia M. S; Souto, Dênio Emanuel Pires; Kubota, Lauro Tatsuo; Borges, Julio Cesar ; Barbosa, Leandro Ramos Souza ; Ramos, Carlos H. I
Fonte: International Journal of Biological Macromolecules. Unidades: IQSC, IF
Assunto: PROTEÍNAS
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ABNT
TIROLI-CEPEDA, Ana Olivia et al. Studies on the effect of the J-domain on the substrate binding domain (SBD) of Hsp70 using a chimeric human J-SBD polypeptide. International Journal of Biological Macromolecules, v. 124, p. 111-120, 2019Tradução . . Disponível em: https://doi.org/10.1016/j.ijbiomac.2018.11.130. Acesso em: 19 nov. 2025.
APA
Tiroli-Cepeda, A. O., Seraphim, T. V., Pinheiro, G. M. S., Souto, D. E. P., Kubota, L. T., Borges, J. C., et al. (2019). Studies on the effect of the J-domain on the substrate binding domain (SBD) of Hsp70 using a chimeric human J-SBD polypeptide. International Journal of Biological Macromolecules, 124, 111-120. doi:10.1016/j.ijbiomac.2018.11.130
NLM
Tiroli-Cepeda AO, Seraphim TV, Pinheiro GMS, Souto DEP, Kubota LT, Borges JC, Barbosa LRS, Ramos CHI. Studies on the effect of the J-domain on the substrate binding domain (SBD) of Hsp70 using a chimeric human J-SBD polypeptide [Internet]. International Journal of Biological Macromolecules. 2019 ;124 111-120.[citado 2025 nov. 19 ] Available from: https://doi.org/10.1016/j.ijbiomac.2018.11.130
Vancouver
Tiroli-Cepeda AO, Seraphim TV, Pinheiro GMS, Souto DEP, Kubota LT, Borges JC, Barbosa LRS, Ramos CHI. Studies on the effect of the J-domain on the substrate binding domain (SBD) of Hsp70 using a chimeric human J-SBD polypeptide [Internet]. International Journal of Biological Macromolecules. 2019 ;124 111-120.[citado 2025 nov. 19 ] Available from: https://doi.org/10.1016/j.ijbiomac.2018.11.130
Trabalho de evento-resumo
Nanostructures for protein drug delivery (2017)
Rangel-Yagui, Carlota de Oliveira ; Vasconcelos, Juliana de Almeida Pachioni; Lopes, André Moreni; Apolinário, Alexsandra Conceição; Oses, Johanna Karina Valenzuela; Costa, Juliana Souza Ribeiro; Nascimento, Laura de Oliveira; Pessoa Junior, Adalberto ; Barbosa, Leandro Ramos Souza
Fonte: Abstracts. Nome do evento: Brazilian Biophysical Society Congress. Unidades: FCF, IF
Assuntos: PROTEÍNAS, NANOTECNOLOGIA
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ABNT
RANGEL-YAGUI, Carlota de Oliveira et al. Nanostructures for protein drug delivery. 2017, Anais.. Rio de Janeiro: Sociedade Brasileira de Biofísica/SBBF, 2017. Disponível em: http://www.sbbf.org.br/xliisbbf2017/wp-content/uploads/2017/05/Scientific-Program-SBBf2017.pdf. Acesso em: 19 nov. 2025.
APA
Rangel-Yagui, C. de O., Vasconcelos, J. de A. P., Lopes, A. M., Apolinário, A. C., Oses, J. K. V., Costa, J. S. R., et al. (2017). Nanostructures for protein drug delivery. In Abstracts. Rio de Janeiro: Sociedade Brasileira de Biofísica/SBBF. Recuperado de http://www.sbbf.org.br/xliisbbf2017/wp-content/uploads/2017/05/Scientific-Program-SBBf2017.pdf
NLM
Rangel-Yagui C de O, Vasconcelos J de AP, Lopes AM, Apolinário AC, Oses JKV, Costa JSR, Nascimento L de O, Pessoa Junior A, Barbosa LRS. Nanostructures for protein drug delivery [Internet]. Abstracts. 2017 ;[citado 2025 nov. 19 ] Available from: http://www.sbbf.org.br/xliisbbf2017/wp-content/uploads/2017/05/Scientific-Program-SBBf2017.pdf
Vancouver
Rangel-Yagui C de O, Vasconcelos J de AP, Lopes AM, Apolinário AC, Oses JKV, Costa JSR, Nascimento L de O, Pessoa Junior A, Barbosa LRS. Nanostructures for protein drug delivery [Internet]. Abstracts. 2017 ;[citado 2025 nov. 19 ] Available from: http://www.sbbf.org.br/xliisbbf2017/wp-content/uploads/2017/05/Scientific-Program-SBBf2017.pdf
Artigo de periodico
Repurposing doxycycline for synucleinopathies: remodelling of α-synuclein oligomers towards non-toxic parallel beta-sheet structured species (2017)
González-Lizárraga, Florencia; Socías, Sergio B; Ávila, César L; Torres-Bugeau, Clarisa M; Barbosa, Leandro Ramos Souza ; Binolfi, Andres; Sepúlveda-Díaz, Julia E; Del-Bel, Elaine; Fernandez, Claudio O; Papy-Garcia, Dulce; Itri, Rosangela ; Raisman-Vozari Rita; Chehín, Rosana N
Fonte: Scientific Reports. Unidades: IF, FORP
Assuntos: DOENÇAS NEURODEGENERATIVAS, PROTEÍNAS, BIOFÍSICA
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ABNT
GONZÁLEZ-LIZÁRRAGA, Florencia et al. Repurposing doxycycline for synucleinopathies: remodelling of α-synuclein oligomers towards non-toxic parallel beta-sheet structured species. Scientific Reports, v. 7, n. 41755, p. 1-13, 2017Tradução . . Disponível em: https://doi.org/10.1038/srep41755. Acesso em: 19 nov. 2025.
APA
González-Lizárraga, F., Socías, S. B., Ávila, C. L., Torres-Bugeau, C. M., Barbosa, L. R. S., Binolfi, A., et al. (2017). Repurposing doxycycline for synucleinopathies: remodelling of α-synuclein oligomers towards non-toxic parallel beta-sheet structured species. Scientific Reports, 7( 41755), 1-13. doi:10.1038/srep41755
NLM
González-Lizárraga F, Socías SB, Ávila CL, Torres-Bugeau CM, Barbosa LRS, Binolfi A, Sepúlveda-Díaz JE, Del-Bel E, Fernandez CO, Papy-Garcia D, Itri R, Raisman-Vozari Rita, Chehín RN. Repurposing doxycycline for synucleinopathies: remodelling of α-synuclein oligomers towards non-toxic parallel beta-sheet structured species [Internet]. Scientific Reports. 2017 ; 7( 41755): 1-13.[citado 2025 nov. 19 ] Available from: https://doi.org/10.1038/srep41755
Vancouver
González-Lizárraga F, Socías SB, Ávila CL, Torres-Bugeau CM, Barbosa LRS, Binolfi A, Sepúlveda-Díaz JE, Del-Bel E, Fernandez CO, Papy-Garcia D, Itri R, Raisman-Vozari Rita, Chehín RN. Repurposing doxycycline for synucleinopathies: remodelling of α-synuclein oligomers towards non-toxic parallel beta-sheet structured species [Internet]. Scientific Reports. 2017 ; 7( 41755): 1-13.[citado 2025 nov. 19 ] Available from: https://doi.org/10.1038/srep41755
Artigo de periodico
A review of multi-domain and flexible molecular chaperones studies by small-angle X-ray scattering (2016)
Borges, Julio Cesar ; Seraphim, Thiago Vargas; Dores-Silva, Paulo Roberto das; Barbosa, Leandro Ramos Souza
Fonte: Biophysical Reviews. Unidades: IQSC, IF
Assuntos: PROTEÍNAS, BIOQUÍMICA CELULAR
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ABNT
BORGES, Julio Cesar et al. A review of multi-domain and flexible molecular chaperones studies by small-angle X-ray scattering. Biophysical Reviews, 2016Tradução . . Disponível em: https://doi.org/10.1007/s12551-016-0194-x. Acesso em: 19 nov. 2025.
APA
Borges, J. C., Seraphim, T. V., Dores-Silva, P. R. das, & Barbosa, L. R. S. (2016). A review of multi-domain and flexible molecular chaperones studies by small-angle X-ray scattering. Biophysical Reviews. doi:10.1007/s12551-016-0194-x
NLM
Borges JC, Seraphim TV, Dores-Silva PR das, Barbosa LRS. A review of multi-domain and flexible molecular chaperones studies by small-angle X-ray scattering [Internet]. Biophysical Reviews. 2016 ;[citado 2025 nov. 19 ] Available from: https://doi.org/10.1007/s12551-016-0194-x
Vancouver
Borges JC, Seraphim TV, Dores-Silva PR das, Barbosa LRS. A review of multi-domain and flexible molecular chaperones studies by small-angle X-ray scattering [Internet]. Biophysical Reviews. 2016 ;[citado 2025 nov. 19 ] Available from: https://doi.org/10.1007/s12551-016-0194-x
Trabalho de evento-resumo periodico
Development and characterization of PEG-PCL polymersomers for protein encapsulation (2015)
Pachioni-Vasconcelos, Juliana de Almeida; Lopes, André Moreni; Apolinário, Alexsandra Conceição; Barbosa, Leandro; Rangel-Yagui, Carlota de Oliveira
Fonte: Brazilian Journal of Pharmaceutical Sciences. Nome do evento: Pharmaceutical Science and Technology Meeting of the Faculty of Pharmaceutical Sciences, University of São Paulo. Unidades: IF, FCF
Assuntos: PROTEÍNAS, NANOTECNOLOGIA
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ABNT
PACHIONI-VASCONCELOS, Juliana de Almeida et al. Development and characterization of PEG-PCL polymersomers for protein encapsulation. Brazilian Journal of Pharmaceutical Sciences. São Paulo: Instituto de Física, Universidade de São Paulo. . Acesso em: 19 nov. 2025. , 2015
APA
Pachioni-Vasconcelos, J. de A., Lopes, A. M., Apolinário, A. C., Barbosa, L., & Rangel-Yagui, C. de O. (2015). Development and characterization of PEG-PCL polymersomers for protein encapsulation. Brazilian Journal of Pharmaceutical Sciences. São Paulo: Instituto de Física, Universidade de São Paulo.
NLM
Pachioni-Vasconcelos J de A, Lopes AM, Apolinário AC, Barbosa L, Rangel-Yagui C de O. Development and characterization of PEG-PCL polymersomers for protein encapsulation. Brazilian Journal of Pharmaceutical Sciences. 2015 ; 51 21 res. FCF038.[citado 2025 nov. 19 ]
Vancouver
Pachioni-Vasconcelos J de A, Lopes AM, Apolinário AC, Barbosa L, Rangel-Yagui C de O. Development and characterization of PEG-PCL polymersomers for protein encapsulation. Brazilian Journal of Pharmaceutical Sciences. 2015 ; 51 21 res. FCF038.[citado 2025 nov. 19 ]
Artigo de periodico
Human mitochondrial Hsp70 (Mortalin): shedding light on ATPase activity, interaction with adenosine nucleotides, solution structure and domain organization (2015)
Dores-Silva, Paulo Roberto das; Barbosa, Leandro Ramos Souza ; Ramos, Carlos Henrique Inacio; Borges, Julio Cesar
Fonte: PLoS ONE. Unidades: IF, IQSC
Assunto: PROTEÍNAS
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ABNT
DORES-SILVA, Paulo Roberto das et al. Human mitochondrial Hsp70 (Mortalin): shedding light on ATPase activity, interaction with adenosine nucleotides, solution structure and domain organization. PLoS ONE, v. 10, n. 1, 2015Tradução . . Disponível em: https://doi.org/10.1371/journal.pone.0117170. Acesso em: 19 nov. 2025.
APA
Dores-Silva, P. R. das, Barbosa, L. R. S., Ramos, C. H. I., & Borges, J. C. (2015). Human mitochondrial Hsp70 (Mortalin): shedding light on ATPase activity, interaction with adenosine nucleotides, solution structure and domain organization. PLoS ONE, 10( 1). doi:10.1371/journal.pone.0117170
NLM
Dores-Silva PR das, Barbosa LRS, Ramos CHI, Borges JC. Human mitochondrial Hsp70 (Mortalin): shedding light on ATPase activity, interaction with adenosine nucleotides, solution structure and domain organization [Internet]. PLoS ONE. 2015 ; 10( 1):[citado 2025 nov. 19 ] Available from: https://doi.org/10.1371/journal.pone.0117170
Vancouver
Dores-Silva PR das, Barbosa LRS, Ramos CHI, Borges JC. Human mitochondrial Hsp70 (Mortalin): shedding light on ATPase activity, interaction with adenosine nucleotides, solution structure and domain organization [Internet]. PLoS ONE. 2015 ; 10( 1):[citado 2025 nov. 19 ] Available from: https://doi.org/10.1371/journal.pone.0117170
Artigo de periodico
Structural characterization of heparin-induced glyceraldehyde-3-phosphate dehydrogenase protofibrils preventing 'alfa'-synuclein oligomeric species toxicity (2014)
Avila, Cesar L.; Torres-Bugeau, Clarisa M.; Chehin, Rosana N.; Ouidja, Mohand O.; Socias, Sergio B.; Raisman-Vozari, Rita; Papy-Garcia, Dulce; Soledad Celej, M.; Sales, Elisa Morandé; Itri, Rosangela ; Barbosa, Leandro Ramos Souza
Fonte: JOURNAL OF BIOLOGICAL CHEMISTRY. Unidade: IF
Assuntos: RADIOGRAFIA, PROTEÍNAS
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ABNT
AVILA, Cesar L. et al. Structural characterization of heparin-induced glyceraldehyde-3-phosphate dehydrogenase protofibrils preventing 'alfa'-synuclein oligomeric species toxicity. JOURNAL OF BIOLOGICAL CHEMISTRY, v. 289, n. 20, p. 13838-13850, 2014Tradução . . Disponível em: https://doi.org/10.1074/jbc.M113.544288. Acesso em: 19 nov. 2025.
APA
Avila, C. L., Torres-Bugeau, C. M., Chehin, R. N., Ouidja, M. O., Socias, S. B., Raisman-Vozari, R., et al. (2014). Structural characterization of heparin-induced glyceraldehyde-3-phosphate dehydrogenase protofibrils preventing 'alfa'-synuclein oligomeric species toxicity. JOURNAL OF BIOLOGICAL CHEMISTRY, 289( 20), 13838-13850. doi:10.1074/jbc.M113.544288
NLM
Avila CL, Torres-Bugeau CM, Chehin RN, Ouidja MO, Socias SB, Raisman-Vozari R, Papy-Garcia D, Soledad Celej M, Sales EM, Itri R, Barbosa LRS. Structural characterization of heparin-induced glyceraldehyde-3-phosphate dehydrogenase protofibrils preventing 'alfa'-synuclein oligomeric species toxicity [Internet]. JOURNAL OF BIOLOGICAL CHEMISTRY. 2014 ; 289( 20): 13838-13850.[citado 2025 nov. 19 ] Available from: https://doi.org/10.1074/jbc.M113.544288
Vancouver
Avila CL, Torres-Bugeau CM, Chehin RN, Ouidja MO, Socias SB, Raisman-Vozari R, Papy-Garcia D, Soledad Celej M, Sales EM, Itri R, Barbosa LRS. Structural characterization of heparin-induced glyceraldehyde-3-phosphate dehydrogenase protofibrils preventing 'alfa'-synuclein oligomeric species toxicity [Internet]. JOURNAL OF BIOLOGICAL CHEMISTRY. 2014 ; 289( 20): 13838-13850.[citado 2025 nov. 19 ] Available from: https://doi.org/10.1074/jbc.M113.544288
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: 19 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. 19 ] 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. 19 ] 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: 19 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. 19 ] 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. 19 ] Available from: http://onlinelibrary.wiley.com/doi/10.1002/9781118523063.ch3/summary
Trabalho de evento-resumo periodico
Structural studies of Septin2G amyloid fibrils (2012)
Itri, Rosangela ; Sales, Elisa Morandé; Damascio, Júlio; Barbosa, Leandro Ramos Souza ; Spinozzi, Francesco; Mariani, Paolo; Araújo, Ana Paula Ulian de
Fonte: Biophysical Journal. Nome do evento: Annual Meeting of the Biophysical Society. Unidades: IF, IFSC
Assuntos: PROTEÍNAS, BIOFÍSICA
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ABNT
ITRI, Rosangela et al. Structural studies of Septin2G amyloid fibrils. Biophysical Journal. Saint Louis: Cell Press. Disponível em: https://doi.org/10.1016/j.bpj.2011.11.2087. Acesso em: 19 nov. 2025. , 2012
APA
Itri, R., Sales, E. M., Damascio, J., Barbosa, L. R. S., Spinozzi, F., Mariani, P., & Araújo, A. P. U. de. (2012). Structural studies of Septin2G amyloid fibrils. Biophysical Journal. Saint Louis: Cell Press. doi:10.1016/j.bpj.2011.11.2087
NLM
Itri R, Sales EM, Damascio J, Barbosa LRS, Spinozzi F, Mariani P, Araújo APU de. Structural studies of Septin2G amyloid fibrils [Internet]. Biophysical Journal. 2012 ; 102( Ja 2012): 381a-382a.[citado 2025 nov. 19 ] Available from: https://doi.org/10.1016/j.bpj.2011.11.2087
Vancouver
Itri R, Sales EM, Damascio J, Barbosa LRS, Spinozzi F, Mariani P, Araújo APU de. Structural studies of Septin2G amyloid fibrils [Internet]. Biophysical Journal. 2012 ; 102( Ja 2012): 381a-382a.[citado 2025 nov. 19 ] Available from: https://doi.org/10.1016/j.bpj.2011.11.2087
Artigo de periodico
Unraveling the Nanomechanical and Vibrational Properties of the Mayaro Virus ()
França, Alefe Roger Silva ; Diniz Filho, Joel Félix Silva ; Santos, Clenilton Costa dos ; Coimbra, Laís Durço ; Marques, Rafael Elias ; Barbosa, Leandro Ramos Souza ; Santos-Oliveira, Ralph ; Souza, Pedro Filho Noronha ; Alencar, Luciana Magalhães Rebelo
Fonte: ACS Omega. Unidade: IF
Assuntos: GENÉTICA, NANOPARTÍCULAS, PEPTÍDEOS, PROTEÍNAS, ESPECTROSCOPIA RAMAN, SUPERFÍCIES
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ABNT
FRANÇA, Alefe Roger Silva et al. Unraveling the Nanomechanical and Vibrational Properties of the Mayaro Virus. ACS Omega, p. 48397 - 48404, [S.d.]Tradução . . Disponível em: https://doi.org/10.1021/acsomega.4c06749. Acesso em: 19 nov. 2025.
APA
França, A. R. S., Diniz Filho, J. F. S., Santos, C. C. dos, Coimbra, L. D., Marques, R. E., Barbosa, L. R. S., et al. Unraveling the Nanomechanical and Vibrational Properties of the Mayaro Virus. ACS Omega, 48397 - 48404. doi:10.1021/acsomega.4c06749
NLM
França ARS, Diniz Filho JFS, Santos CC dos, Coimbra LD, Marques RE, Barbosa LRS, Santos-Oliveira R , Souza P F N , Alencar LMR. Unraveling the Nanomechanical and Vibrational Properties of the Mayaro Virus [Internet]. ACS Omega. 48397 - 48404.[citado 2025 nov. 19 ] Available from: https://doi.org/10.1021/acsomega.4c06749
Vancouver
França ARS, Diniz Filho JFS, Santos CC dos, Coimbra LD, Marques RE, Barbosa LRS, Santos-Oliveira R , Souza P F N , Alencar LMR. Unraveling the Nanomechanical and Vibrational Properties of the Mayaro Virus [Internet]. ACS Omega. 48397 - 48404.[citado 2025 nov. 19 ] Available from: https://doi.org/10.1021/acsomega.4c06749

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