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Filtros : "BARBOSA, LEANDRO RAMOS SOUZA" "Estados Unidos" Limpar

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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

    Source: Biochemical and Biophysical Research Communications. Unidades: IQ, IF

    Subjects: PROTEÍNAS, LIPÍDEOS

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      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: 03 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. 03 ] 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. 03 ] Available from: https://dx.doi.org/10.1016/j.bbrc.2024.151071

  • Artigo de periodico

    Photobiomodulation of Na,K‐ATPase in native membrane fraction and reconstituted in DPPC:DPPE‐liposome (2024)

    Scanavachi, Gustavo; Yoneda, Juliana S; Sebinelli, Heitor Gobbi; Barbosa, Leandro Ramos Souza ; Ciancaglini, Pietro ; Itri, Rosangela

    Source: Photochemistry and Photobiology. Unidades: IF, FFCLRP

    Subjects: ENZIMAS, FOTOTERAPIA, LIPOSSOMOS

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      SCANAVACHI, Gustavo et al. Photobiomodulation of Na,K‐ATPase in native membrane fraction and reconstituted in DPPC:DPPE‐liposome. Photochemistry and Photobiology, v. 101, n. 1, p. 230-238, 2024Tradução . . Disponível em: https://doi.org/10.1111/php.13987. Acesso em: 03 nov. 2025.

    • APA

      Scanavachi, G., Yoneda, J. S., Sebinelli, H. G., Barbosa, L. R. S., Ciancaglini, P., & Itri, R. (2024). Photobiomodulation of Na,K‐ATPase in native membrane fraction and reconstituted in DPPC:DPPE‐liposome. Photochemistry and Photobiology, 101( 1), 230-238. doi:10.1111/php.13987

    • NLM

      Scanavachi G, Yoneda JS, Sebinelli HG, Barbosa LRS, Ciancaglini P, Itri R. Photobiomodulation of Na,K‐ATPase in native membrane fraction and reconstituted in DPPC:DPPE‐liposome [Internet]. Photochemistry and Photobiology. 2024 ; 101( 1): 230-238.[citado 2025 nov. 03 ] Available from: https://doi.org/10.1111/php.13987

    • Vancouver

      Scanavachi G, Yoneda JS, Sebinelli HG, Barbosa LRS, Ciancaglini P, Itri R. Photobiomodulation of Na,K‐ATPase in native membrane fraction and reconstituted in DPPC:DPPE‐liposome [Internet]. Photochemistry and Photobiology. 2024 ; 101( 1): 230-238.[citado 2025 nov. 03 ] Available from: https://doi.org/10.1111/php.13987

  • Artigo de periodico

    Unveiling the three-step model for the interaction of imidazolium-based ionic liquids on albumin (2023)

    Raw, Juliana ; Franco, Leandro R.; Rodrigues, Luiz Fernando de Camargo ; Barbosa, Leandro Ramos Souza

    Source: ACS Omega. Unidade: IF

    Subjects: FÍSICO-QUÍMICA, FLUÍDOS COMPLEXOS, DIFRAÇÃO POR RAIOS X, ESPECTROSCOPIA, FLUORESCÊNCIA

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      RAW, Juliana et al. Unveiling the three-step model for the interaction of imidazolium-based ionic liquids on albumin. ACS Omega, v. 8; n. 41; p. 38101-38110, 2023Tradução . . Disponível em: https://doi.org/10.1021/acsomega.3c04188. Acesso em: 03 nov. 2025.

    • APA

      Raw, J., Franco, L. R., Rodrigues, L. F. de C., & Barbosa, L. R. S. (2023). Unveiling the three-step model for the interaction of imidazolium-based ionic liquids on albumin. ACS Omega, 8; n. 41; p. 38101-38110. doi:10.1021/acsomega.3c04188

    • NLM

      Raw J, Franco LR, Rodrigues LF de C, Barbosa LRS. Unveiling the three-step model for the interaction of imidazolium-based ionic liquids on albumin [Internet]. ACS Omega. 2023 ; 8; n. 41; p. 38101-38110[citado 2025 nov. 03 ] Available from: https://doi.org/10.1021/acsomega.3c04188

    • Vancouver

      Raw J, Franco LR, Rodrigues LF de C, Barbosa LRS. Unveiling the three-step model for the interaction of imidazolium-based ionic liquids on albumin [Internet]. ACS Omega. 2023 ; 8; n. 41; p. 38101-38110[citado 2025 nov. 03 ] Available from: https://doi.org/10.1021/acsomega.3c04188

  • 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

    Source: Biopolymers. Unidade: IF

    Subjects: BIOFÍSICA, BIOPOLÍMEROS, PROTEÍNAS, BIOLOGIA MOLECULAR

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      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: 03 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. 03 ] 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. 03 ] 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.

    Source: Structure. Unidades: IQSC, IF

    Subjects: BIOQUÍMICA, BIOFÍSICA, MACROMOLÉCULA, PROTEÍNAS

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      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: 03 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. 03 ] 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. 03 ] Available from: https://doi.org/10.1016/j.str.2021.08.002

  • Artigo de periodico

    Compartmentalization of therapeutic proteins into semi-crystalline PEG-PCL polymersomes (2021)

    Vasconcelos, Juliana de Almeida Pachioni; Apolinário, Alexsandra Conceição ; Lopes, André Moreni; Pessoa Junior, Adalberto ; Barbosa, Leandro Ramos Souza ; Rangel-Yagui, Carlota de Oliveira

    Source: Soft Materials. Unidades: FCF, IF

    Subjects: DNA RECOMBINANTE, ENZIMAS, ANTICORPOS

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      VASCONCELOS, Juliana de Almeida Pachioni et al. Compartmentalization of therapeutic proteins into semi-crystalline PEG-PCL polymersomes. Soft Materials, v. 19, n. 2, p. 222-230, 2021Tradução . . Disponível em: https://doi.org/10.1080/1539445X.2020.1812643. Acesso em: 03 nov. 2025.

    • APA

      Vasconcelos, J. de A. P., Apolinário, A. C., Lopes, A. M., Pessoa Junior, A., Barbosa, L. R. S., & Rangel-Yagui, C. de O. (2021). Compartmentalization of therapeutic proteins into semi-crystalline PEG-PCL polymersomes. Soft Materials, 19( 2), 222-230. doi:10.1080/1539445X.2020.1812643

    • NLM

      Vasconcelos J de AP, Apolinário AC, Lopes AM, Pessoa Junior A, Barbosa LRS, Rangel-Yagui C de O. Compartmentalization of therapeutic proteins into semi-crystalline PEG-PCL polymersomes [Internet]. Soft Materials. 2021 ; 19( 2): 222-230.[citado 2025 nov. 03 ] Available from: https://doi.org/10.1080/1539445X.2020.1812643

    • Vancouver

      Vasconcelos J de AP, Apolinário AC, Lopes AM, Pessoa Junior A, Barbosa LRS, Rangel-Yagui C de O. Compartmentalization of therapeutic proteins into semi-crystalline PEG-PCL polymersomes [Internet]. Soft Materials. 2021 ; 19( 2): 222-230.[citado 2025 nov. 03 ] Available from: https://doi.org/10.1080/1539445X.2020.1812643

  • Artigo de periodico

    Fast Biofilm Penetration and Anti-PAO1 Activity of Nebulized Azithromycin in Nanoarchaeosomes (2020)

    Altube, Maria Julia; Martínez, Melina M B; Malheiros, Barbara ; Maffía, Paulo C; Barbosa, Leandro Ramos Souza ; Morilla, Maria Jose; Romero, Eder Lilia

    Source: Molecular Pharmaceutics. Unidades: IF, FCF

    Subjects: BIOFÍSICA, FÍSICA MOLECULAR

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      ALTUBE, Maria Julia et al. Fast Biofilm Penetration and Anti-PAO1 Activity of Nebulized Azithromycin in Nanoarchaeosomes. Molecular Pharmaceutics, v. 17, n. 1, p. 70-83, 2020Tradução . . Disponível em: https://doi.org/10.1021/acs.molpharmaceut.9b00721. Acesso em: 03 nov. 2025.

    • APA

      Altube, M. J., Martínez, M. M. B., Malheiros, B., Maffía, P. C., Barbosa, L. R. S., Morilla, M. J., & Romero, E. L. (2020). Fast Biofilm Penetration and Anti-PAO1 Activity of Nebulized Azithromycin in Nanoarchaeosomes. Molecular Pharmaceutics, 17( 1), 70-83. doi:10.1021/acs.molpharmaceut.9b00721

    • NLM

      Altube MJ, Martínez MMB, Malheiros B, Maffía PC, Barbosa LRS, Morilla MJ, Romero EL. Fast Biofilm Penetration and Anti-PAO1 Activity of Nebulized Azithromycin in Nanoarchaeosomes [Internet]. Molecular Pharmaceutics. 2020 ; 17( 1): 70-83.[citado 2025 nov. 03 ] Available from: https://doi.org/10.1021/acs.molpharmaceut.9b00721

    • Vancouver

      Altube MJ, Martínez MMB, Malheiros B, Maffía PC, Barbosa LRS, Morilla MJ, Romero EL. Fast Biofilm Penetration and Anti-PAO1 Activity of Nebulized Azithromycin in Nanoarchaeosomes [Internet]. Molecular Pharmaceutics. 2020 ; 17( 1): 70-83.[citado 2025 nov. 03 ] Available from: https://doi.org/10.1021/acs.molpharmaceut.9b00721

  • Artigo de periodico

    X-Ray Characterization of Pharmaceutical and Cosmetic Lipidic Nanoparticles for Cutaneous Application (2019)

    Carducci, Federica; Casadei, Bruna Renata ; Mariani, Paolo ; Barbosa, Leandro Ramos Souza

    Source: Current Pharmaceutical Design. Unidade: IF

    Subjects: BIOFÍSICA, LIPÍDEOS, ESPALHAMENTO, RAIOS X

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      CARDUCCI, Federica et al. X-Ray Characterization of Pharmaceutical and Cosmetic Lipidic Nanoparticles for Cutaneous Application. Current Pharmaceutical Design, v. 25 , n. 214, p. 2364-2374, 2019Tradução . . Disponível em: https://doi.org/10.2174/1381612825666190709210211. Acesso em: 03 nov. 2025.

    • APA

      Carducci, F., Casadei, B. R., Mariani, P., & Barbosa, L. R. S. (2019). X-Ray Characterization of Pharmaceutical and Cosmetic Lipidic Nanoparticles for Cutaneous Application. Current Pharmaceutical Design, 25 ( 214), 2364-2374. doi:10.2174/1381612825666190709210211

    • NLM

      Carducci F, Casadei BR, Mariani P, Barbosa LRS. X-Ray Characterization of Pharmaceutical and Cosmetic Lipidic Nanoparticles for Cutaneous Application [Internet]. Current Pharmaceutical Design. 2019 ; 25 ( 214): 2364-2374.[citado 2025 nov. 03 ] Available from: https://doi.org/10.2174/1381612825666190709210211

    • Vancouver

      Carducci F, Casadei BR, Mariani P, Barbosa LRS. X-Ray Characterization of Pharmaceutical and Cosmetic Lipidic Nanoparticles for Cutaneous Application [Internet]. Current Pharmaceutical Design. 2019 ; 25 ( 214): 2364-2374.[citado 2025 nov. 03 ] Available from: https://doi.org/10.2174/1381612825666190709210211

  • Artigo de periodico

    Nanoliposomal Buparvaquone Immunomodulates Leishmania (L.) infantum-infected Macrophages and is Highly Effective in Murine Model (2017)

    Costa-Silva, Thais Alves da; Galisteo Junior, Andrés Jimenez; Lindoso, José Angelo Lauletta; Barbosa, Leandro Ramos Souza ; Tempone, Andre Gustavo

    Source: Antimicrobial Agents Chemother. Unidade: IF

    Subjects: BIOFÍSICA, LEISHMANIOSE VISCERAL, ESPALHAMENTO DE RAIOS X A BAIXOS ÂNGULOS, DOENÇAS INFECCIOSAS

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      COSTA-SILVA, Thais Alves da et al. Nanoliposomal Buparvaquone Immunomodulates Leishmania (L.) infantum-infected Macrophages and is Highly Effective in Murine Model. Antimicrobial Agents Chemother, v. 61, n. 9, p. 1-45, 2017Tradução . . Disponível em: https://doi.org/10.1128/AAC.02297-16. Acesso em: 03 nov. 2025.

    • APA

      Costa-Silva, T. A. da, Galisteo Junior, A. J., Lindoso, J. A. L., Barbosa, L. R. S., & Tempone, A. G. (2017). Nanoliposomal Buparvaquone Immunomodulates Leishmania (L.) infantum-infected Macrophages and is Highly Effective in Murine Model. Antimicrobial Agents Chemother, 61( 9), 1-45. doi:10.1128/AAC.02297-16

    • NLM

      Costa-Silva TA da, Galisteo Junior AJ, Lindoso JAL, Barbosa LRS, Tempone AG. Nanoliposomal Buparvaquone Immunomodulates Leishmania (L.) infantum-infected Macrophages and is Highly Effective in Murine Model [Internet]. Antimicrobial Agents Chemother. 2017 ; 61( 9): 1-45.[citado 2025 nov. 03 ] Available from: https://doi.org/10.1128/AAC.02297-16

    • Vancouver

      Costa-Silva TA da, Galisteo Junior AJ, Lindoso JAL, Barbosa LRS, Tempone AG. Nanoliposomal Buparvaquone Immunomodulates Leishmania (L.) infantum-infected Macrophages and is Highly Effective in Murine Model [Internet]. Antimicrobial Agents Chemother. 2017 ; 61( 9): 1-45.[citado 2025 nov. 03 ] Available from: https://doi.org/10.1128/AAC.02297-16

  • Artigo de periodico

    Cytochrome-c affects the monoolein polymorphism: Consequences for stability and loading efficiency of drug delivery systems (2016)

    Mazzoni, Serena; Funari, Sergio S.; Mariani, Paolo; Barbosa, Leandro Ramos Souza ; Itri, Rosangela

    Source: LANGMUIR. Unidade: IF

    Subjects: CRISTALIZAÇÃO, NANOPARTÍCULAS

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      MAZZONI, Serena et al. Cytochrome-c affects the monoolein polymorphism: Consequences for stability and loading efficiency of drug delivery systems. LANGMUIR, v. 32, n. ja 2016, p. 873-881, 2016Tradução . . Disponível em: http://pubs.acs.org/doi/abs/10.1021/acs.langmuir.5b03507. Acesso em: 03 nov. 2025.

    • APA

      Mazzoni, S., Funari, S. S., Mariani, P., Barbosa, L. R. S., & Itri, R. (2016). Cytochrome-c affects the monoolein polymorphism: Consequences for stability and loading efficiency of drug delivery systems. LANGMUIR, 32( ja 2016), 873-881. doi:10.1021/acs.langmuir.5b03507

    • NLM

      Mazzoni S, Funari SS, Mariani P, Barbosa LRS, Itri R. Cytochrome-c affects the monoolein polymorphism: Consequences for stability and loading efficiency of drug delivery systems [Internet]. LANGMUIR. 2016 ; 32( ja 2016): 873-881.[citado 2025 nov. 03 ] Available from: http://pubs.acs.org/doi/abs/10.1021/acs.langmuir.5b03507

    • Vancouver

      Mazzoni S, Funari SS, Mariani P, Barbosa LRS, Itri R. Cytochrome-c affects the monoolein polymorphism: Consequences for stability and loading efficiency of drug delivery systems [Internet]. LANGMUIR. 2016 ; 32( ja 2016): 873-881.[citado 2025 nov. 03 ] Available from: http://pubs.acs.org/doi/abs/10.1021/acs.langmuir.5b03507

  • Artigo de periodico

    Impact of monovalent and divalent cations on the colloidal stability of negatively charged latex particles decorated with Poly(ethylene glycol) (2016)

    Nukui, Larissa H. N; Barbosa, Leandro Ramos Souza ; Petri, Denise Freitas Siqueira

    Source: Industrial & Engineering Chemistry Research. Unidades: IF, IQ

    Assunto: QUÍMICA COLOIDAL

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      NUKUI, Larissa H. N e BARBOSA, Leandro Ramos Souza e PETRI, Denise Freitas Siqueira. Impact of monovalent and divalent cations on the colloidal stability of negatively charged latex particles decorated with Poly(ethylene glycol). Industrial & Engineering Chemistry Research, v. 55, n. 3, p. 606-614, 2016Tradução . . Disponível em: https://doi.org/10.1021/acs.iecr.5b04103. Acesso em: 03 nov. 2025.

    • APA

      Nukui, L. H. N., Barbosa, L. R. S., & Petri, D. F. S. (2016). Impact of monovalent and divalent cations on the colloidal stability of negatively charged latex particles decorated with Poly(ethylene glycol). Industrial & Engineering Chemistry Research, 55( 3), 606-614. doi:10.1021/acs.iecr.5b04103

    • NLM

      Nukui LHN, Barbosa LRS, Petri DFS. Impact of monovalent and divalent cations on the colloidal stability of negatively charged latex particles decorated with Poly(ethylene glycol) [Internet]. Industrial & Engineering Chemistry Research. 2016 ; 55( 3): 606-614.[citado 2025 nov. 03 ] Available from: https://doi.org/10.1021/acs.iecr.5b04103

    • Vancouver

      Nukui LHN, Barbosa LRS, Petri DFS. Impact of monovalent and divalent cations on the colloidal stability of negatively charged latex particles decorated with Poly(ethylene glycol) [Internet]. Industrial & Engineering Chemistry Research. 2016 ; 55( 3): 606-614.[citado 2025 nov. 03 ] Available from: https://doi.org/10.1021/acs.iecr.5b04103

  • Artigo de periodico

    Low sequence identity but high structural and functional conservation: The case of Hsp70/Hsp90 organizing protein (Hop/Sti1) of Leishmania braziliensis (2016)

    Batista, Fernanda Aparecida Heleno; Seraphim, Thiago V.; Santos, Clelton Aparecido dos; Gonzaga, Marisvanda R; Barbosa, Leandro Ramos Souza ; Ramos, Carlos Henrique Inacio; Borges, Julio Cesar

    Source: Archives Biochemistry and Biophysics. Unidades: IF, IQSC

    Assunto: LEISHMANIA BRASILIENSIS

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      BATISTA, Fernanda Aparecida Heleno et al. Low sequence identity but high structural and functional conservation: The case of Hsp70/Hsp90 organizing protein (Hop/Sti1) of Leishmania braziliensis. Archives Biochemistry and Biophysics, v. 600, p. 12-22, 2016Tradução . . Disponível em: https://doi.org/10.1016/j.abb.2016.04.008. Acesso em: 03 nov. 2025.

    • APA

      Batista, F. A. H., Seraphim, T. V., Santos, C. A. dos, Gonzaga, M. R., Barbosa, L. R. S., Ramos, C. H. I., & Borges, J. C. (2016). Low sequence identity but high structural and functional conservation: The case of Hsp70/Hsp90 organizing protein (Hop/Sti1) of Leishmania braziliensis. Archives Biochemistry and Biophysics, 600, 12-22. doi:10.1016/j.abb.2016.04.008

    • NLM

      Batista FAH, Seraphim TV, Santos CA dos, Gonzaga MR, Barbosa LRS, Ramos CHI, Borges JC. Low sequence identity but high structural and functional conservation: The case of Hsp70/Hsp90 organizing protein (Hop/Sti1) of Leishmania braziliensis [Internet]. Archives Biochemistry and Biophysics. 2016 ; 600 12-22.[citado 2025 nov. 03 ] Available from: https://doi.org/10.1016/j.abb.2016.04.008

    • Vancouver

      Batista FAH, Seraphim TV, Santos CA dos, Gonzaga MR, Barbosa LRS, Ramos CHI, Borges JC. Low sequence identity but high structural and functional conservation: The case of Hsp70/Hsp90 organizing protein (Hop/Sti1) of Leishmania braziliensis [Internet]. Archives Biochemistry and Biophysics. 2016 ; 600 12-22.[citado 2025 nov. 03 ] Available from: https://doi.org/10.1016/j.abb.2016.04.008

  • Artigo de periodico

    Heat Shock Protein 90 'K''DA' (Hsp90) Has a Second Functional Interaction Site with the Mitochondrial Import Receptor Tom70 (2016)

    Zanphorlin, Leticia M.; Lima, Tatiani B.; Gozzo, Fabio C.; Ramos, Carlos H. I.; Costa, Juliana Souza Ribeiro; Nascimento, Laura de Oliveira; Wong, Michael J.; Young, Jason C.; Minetti, Conceicao A. S. A; Remeta, David P.; Balbuena, Tiago S.; Barbosa, Leandro Ramos Souza

    Source: JOURNAL OF BIOLOGICAL CHEMISTRY. Unidade: IF

    Subjects: MATERIAIS NANOESTRUTURADOS, ESPECTROMETRIA

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      ZANPHORLIN, Leticia M. et al. Heat Shock Protein 90 'K''DA' (Hsp90) Has a Second Functional Interaction Site with the Mitochondrial Import Receptor Tom70. JOURNAL OF BIOLOGICAL CHEMISTRY, v. 291, n. 36, p. 18620-18631, 2016Tradução . . Disponível em: http://www.jbc.org/content/291/36/18620. Acesso em: 03 nov. 2025.

    • APA

      Zanphorlin, L. M., Lima, T. B., Gozzo, F. C., Ramos, C. H. I., Costa, J. S. R., Nascimento, L. de O., et al. (2016). Heat Shock Protein 90 'K''DA' (Hsp90) Has a Second Functional Interaction Site with the Mitochondrial Import Receptor Tom70. JOURNAL OF BIOLOGICAL CHEMISTRY, 291( 36), 18620-18631. doi:10.1074/jbc.M115.710137

    • NLM

      Zanphorlin LM, Lima TB, Gozzo FC, Ramos CHI, Costa JSR, Nascimento L de O, Wong MJ, Young JC, Minetti CASA, Remeta DP, Balbuena TS, Barbosa LRS. Heat Shock Protein 90 'K''DA' (Hsp90) Has a Second Functional Interaction Site with the Mitochondrial Import Receptor Tom70 [Internet]. JOURNAL OF BIOLOGICAL CHEMISTRY. 2016 ; 291( 36): 18620-18631.[citado 2025 nov. 03 ] Available from: http://www.jbc.org/content/291/36/18620

    • Vancouver

      Zanphorlin LM, Lima TB, Gozzo FC, Ramos CHI, Costa JSR, Nascimento L de O, Wong MJ, Young JC, Minetti CASA, Remeta DP, Balbuena TS, Barbosa LRS. Heat Shock Protein 90 'K''DA' (Hsp90) Has a Second Functional Interaction Site with the Mitochondrial Import Receptor Tom70 [Internet]. JOURNAL OF BIOLOGICAL CHEMISTRY. 2016 ; 291( 36): 18620-18631.[citado 2025 nov. 03 ] Available from: http://www.jbc.org/content/291/36/18620

  • 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

    Source: 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: 03 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. 03 ] 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. 03 ] Available from: https://doi.org/10.1371/journal.pone.0117170

  • Artigo de periodico

    The C-terminal region of the human p23 chaperone modulates its structure and function (2015)

    Seraphim, Thiago Vargas ; Gava, Lisandra M; Mokry, David Z.; Cagliari, Thiago D; Barbosa, Leandro Ramos Souza ; Ramos, Carlos Henrique Inacio ; Borges, Julio Cesar

    Source: Archives of Biochemistry and Biophysics. Unidades: IQSC, IF

    Subjects: BIOFÍSICA, BIOLOGIA MOLECULAR

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    • ABNT

      SERAPHIM, Thiago Vargas et al. The C-terminal region of the human p23 chaperone modulates its structure and function. Archives of Biochemistry and Biophysics, v. 565, p. 57-67, 2015Tradução . . Disponível em: https://doi.org/10.1016/j.abb.2014.10.015. Acesso em: 03 nov. 2025.

    • APA

      Seraphim, T. V., Gava, L. M., Mokry, D. Z., Cagliari, T. D., Barbosa, L. R. S., Ramos, C. H. I., & Borges, J. C. (2015). The C-terminal region of the human p23 chaperone modulates its structure and function. Archives of Biochemistry and Biophysics, 565, 57-67. doi:10.1016/j.abb.2014.10.015

    • NLM

      Seraphim TV, Gava LM, Mokry DZ, Cagliari TD, Barbosa LRS, Ramos CHI, Borges JC. The C-terminal region of the human p23 chaperone modulates its structure and function [Internet]. Archives of Biochemistry and Biophysics. 2015 ; 565 57-67.[citado 2025 nov. 03 ] Available from: https://doi.org/10.1016/j.abb.2014.10.015

    • Vancouver

      Seraphim TV, Gava LM, Mokry DZ, Cagliari TD, Barbosa LRS, Ramos CHI, Borges JC. The C-terminal region of the human p23 chaperone modulates its structure and function [Internet]. Archives of Biochemistry and Biophysics. 2015 ; 565 57-67.[citado 2025 nov. 03 ] Available from: https://doi.org/10.1016/j.abb.2014.10.015

  • 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

    Source: JOURNAL OF BIOLOGICAL CHEMISTRY. Unidade: IF

    Subjects: 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: 03 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. 03 ] 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. 03 ] Available from: https://doi.org/10.1074/jbc.M113.544288

  • 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: 03 nov. 2025. , 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 2025 nov. 03 ] 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 2025 nov. 03 ] Available from: http://www.cell.com/biophysj/comments/S0006-3495(13)03434-6

  • 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)

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    • 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: 03 nov. 2025. , 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 2025 nov. 03 ] 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 2025 nov. 03 ] Available from: http://www.cell.com/biophysj/pdf/S0006-3495(13)05028-5.pdf

  • Artigo de periodico

    How does the ethoxylated grafting of polyelectrolytes affect the self-assembly of polyanion–cationic surfactant complex salts? (2014)

    Percebom, Ana Maria; Loh, Watson; Barbosa, Leandro Ramos Souza ; Itri, Rosangela

    Source: LANGMUIR. Unidade: IF

    Subjects: RAIOS X, POLÍMEROS (MATERIAIS)

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    • ABNT

      PERCEBOM, Ana Maria et al. How does the ethoxylated grafting of polyelectrolytes affect the self-assembly of polyanion–cationic surfactant complex salts?. LANGMUIR, v. 30, n. 39, p. 11493-11503, 2014Tradução . . Disponível em: https://doi.org/10.1021/la5019604. Acesso em: 03 nov. 2025.

    • APA

      Percebom, A. M., Loh, W., Barbosa, L. R. S., & Itri, R. (2014). How does the ethoxylated grafting of polyelectrolytes affect the self-assembly of polyanion–cationic surfactant complex salts? LANGMUIR, 30( 39), 11493-11503. doi:10.1021/la5019604

    • NLM

      Percebom AM, Loh W, Barbosa LRS, Itri R. How does the ethoxylated grafting of polyelectrolytes affect the self-assembly of polyanion–cationic surfactant complex salts? [Internet]. LANGMUIR. 2014 ; 30( 39): 11493-11503.[citado 2025 nov. 03 ] Available from: https://doi.org/10.1021/la5019604

    • Vancouver

      Percebom AM, Loh W, Barbosa LRS, Itri R. How does the ethoxylated grafting of polyelectrolytes affect the self-assembly of polyanion–cationic surfactant complex salts? [Internet]. LANGMUIR. 2014 ; 30( 39): 11493-11503.[citado 2025 nov. 03 ] Available from: https://doi.org/10.1021/la5019604

  • 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

    Source: Applied Microbiology and Biotechnology. Unidades: IF, FCF

    Subjects: 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: 03 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. 03 ] 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. 03 ] Available from: https://doi.org/10.1007/s00253-013-4922-x

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