Filtros : "BARBOSA, LEANDRO RAMOS SOUZA" "Estados Unidos" Removido: "Financiamento FAPESP" Limpar

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  • 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: 04 nov. 2025.
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      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. 04 ] 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. 04 ] Available from: https://doi.org/10.1021/acsomega.3c04188
  • 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: 04 nov. 2025.
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      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. 04 ] 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. 04 ] Available from: https://doi.org/10.1080/1539445X.2020.1812643
  • 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: 04 nov. 2025.
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      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. 04 ] 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. 04 ] Available from: https://doi.org/10.1021/acs.molpharmaceut.9b00721
  • 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: 04 nov. 2025.
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      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. 04 ] 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. 04 ] Available from: https://doi.org/10.2174/1381612825666190709210211
  • 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: 04 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. 04 ] 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. 04 ] Available from: https://doi.org/10.1128/AAC.02297-16
  • 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: 04 nov. 2025.
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      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. 04 ] 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. 04 ] Available from: http://pubs.acs.org/doi/abs/10.1021/acs.langmuir.5b03507
  • 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: 04 nov. 2025.
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      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. 04 ] 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. 04 ] Available from: https://doi.org/10.1021/acs.iecr.5b04103
  • 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: 04 nov. 2025.
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      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. 04 ] 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. 04 ] Available from: https://doi.org/10.1016/j.abb.2016.04.008
  • 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: 04 nov. 2025.
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      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. 04 ] 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. 04 ] Available from: http://www.jbc.org/content/291/36/18620
  • Source: PLoS ONE. Unidades: IF, IQSC

    Assunto: PROTEÍNAS

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      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: 04 nov. 2025.
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      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. 04 ] 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. 04 ] Available from: https://doi.org/10.1371/journal.pone.0117170
  • Source: Archives of Biochemistry and Biophysics. Unidades: IQSC, IF

    Subjects: BIOFÍSICA, BIOLOGIA MOLECULAR

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      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: 04 nov. 2025.
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      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. 04 ] 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. 04 ] Available from: https://doi.org/10.1016/j.abb.2014.10.015
  • Source: JOURNAL OF BIOLOGICAL CHEMISTRY. Unidade: IF

    Subjects: RADIOGRAFIA, PROTEÍNAS

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      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: 04 nov. 2025.
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      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. 04 ] 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. 04 ] Available from: https://doi.org/10.1074/jbc.M113.544288
  • Source: Biophysical Journal. Conference titles: Annual Meeting of the Biophysical Society. Unidade: IF

    Subjects: PEPTÍDEOS, PROTEÍNAS (ESTUDO)

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      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: 04 nov. 2025. , 2014
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      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. 04 ] 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. 04 ] Available from: http://www.cell.com/biophysj/comments/S0006-3495(13)03434-6
  • Source: Biophysical Journal. Conference titles: Annual Meeting of the Biophysical Society. Unidade: IF

    Subjects: PEPTÍDEOS, PROTEÍNAS (ESTUDO)

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      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: 04 nov. 2025. , 2014
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      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. 04 ] 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. 04 ] Available from: http://www.cell.com/biophysj/pdf/S0006-3495(13)05028-5.pdf
  • Source: LANGMUIR. Unidade: IF

    Subjects: RAIOS X, POLÍMEROS (MATERIAIS)

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      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: 04 nov. 2025.
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      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. 04 ] 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. 04 ] Available from: https://doi.org/10.1021/la5019604
  • Source: Applied Microbiology and Biotechnology. Unidades: IF, FCF

    Subjects: PROTEÍNAS DE FLUORESCÊNCIA VERDE, ENDOTOXINAS

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      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: 04 nov. 2025.
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      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. 04 ] 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. 04 ] Available from: https://doi.org/10.1007/s00253-013-4922-x
  • Source: CELL PRESS. Conference titles: Annual Meeting of the Biophysical-Society LVII. Unidade: IF

    Subjects: ESPECTROSCOPIA, FLUORESCÊNCIA

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      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: 04 nov. 2025. , 2013
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      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
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      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. 04 ] 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. 04 ] Available from: http://www.sciencedirect.com/science/article/pii/S0006349512034030
  • Source: PLoS ONE. Unidades: IF, IQSC

    Subjects: PROTEÍNAS, LEISHMANIA BRASILIENSIS

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      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: 04 nov. 2025.
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      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. 04 ] 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. 04 ] Available from: https://doi.org/10.1371/journal.pone.0066822
  • Source: Archives of Biochemistry and Biophysics. Unidades: IF, IQSC

    Subjects: BIOFÍSICA, BIOLOGIA MOLECULAR

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      DORES-SILVA, Paulo Roberto das et al. Low resolution structural characterization of the Hsp70-interacting protein – Hip – from Leishmania braziliensis emphasizes its high asymmetry. Archives of Biochemistry and Biophysics, v. 520, n. 2, p. 88-98, 2012Tradução . . Disponível em: https://doi.org/10.1016/j.abb.2012.02.009. Acesso em: 04 nov. 2025.
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      Dores-Silva, P. R. das, Silva, E. R., Gomes, F. E. R., Silva, K. P., Barbosa, L. R. S., & Borges, J. C. (2012). Low resolution structural characterization of the Hsp70-interacting protein – Hip – from Leishmania braziliensis emphasizes its high asymmetry. Archives of Biochemistry and Biophysics, 520( 2), 88-98. doi:10.1016/j.abb.2012.02.009
    • NLM

      Dores-Silva PR das, Silva ER, Gomes FER, Silva KP, Barbosa LRS, Borges JC. Low resolution structural characterization of the Hsp70-interacting protein – Hip – from Leishmania braziliensis emphasizes its high asymmetry [Internet]. Archives of Biochemistry and Biophysics. 2012 ; 520( 2): 88-98.[citado 2025 nov. 04 ] Available from: https://doi.org/10.1016/j.abb.2012.02.009
    • Vancouver

      Dores-Silva PR das, Silva ER, Gomes FER, Silva KP, Barbosa LRS, Borges JC. Low resolution structural characterization of the Hsp70-interacting protein – Hip – from Leishmania braziliensis emphasizes its high asymmetry [Internet]. Archives of Biochemistry and Biophysics. 2012 ; 520( 2): 88-98.[citado 2025 nov. 04 ] Available from: https://doi.org/10.1016/j.abb.2012.02.009
  • Source: Journal of Biological Chemistry. Unidade: IF

    Assunto: BIOQUÍMICA

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      TORRES-BUGEAU, Clarisa M et al. Characterization of heparin-induced glyceraldehyde 3-phosphate dehydrogenase early amyloid-like oligomers and their implication in `alfa´-synuclein aggregation. Journal of Biological Chemistry, v. 287, n. 4, p. 2398–2409, 2012Tradução . . Disponível em: https://doi.org/10.1074/jbc.M111.303503. Acesso em: 04 nov. 2025.
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      Torres-Bugeau, C. M., Ávila, C. L., Raisman-Vozzari, R., Papy-Garcia, D., Itri, R., Barbosa, L. R. S., et al. (2012). Characterization of heparin-induced glyceraldehyde 3-phosphate dehydrogenase early amyloid-like oligomers and their implication in `alfa´-synuclein aggregation. Journal of Biological Chemistry, 287( 4), 2398–2409. doi:10.1074/jbc.M111.303503
    • NLM

      Torres-Bugeau CM, Ávila CL, Raisman-Vozzari R, Papy-Garcia D, Itri R, Barbosa LRS, Cortez LM, Chehín RN. Characterization of heparin-induced glyceraldehyde 3-phosphate dehydrogenase early amyloid-like oligomers and their implication in `alfa´-synuclein aggregation [Internet]. Journal of Biological Chemistry. 2012 ; 287( 4): 2398–2409.[citado 2025 nov. 04 ] Available from: https://doi.org/10.1074/jbc.M111.303503
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      Torres-Bugeau CM, Ávila CL, Raisman-Vozzari R, Papy-Garcia D, Itri R, Barbosa LRS, Cortez LM, Chehín RN. Characterization of heparin-induced glyceraldehyde 3-phosphate dehydrogenase early amyloid-like oligomers and their implication in `alfa´-synuclein aggregation [Internet]. Journal of Biological Chemistry. 2012 ; 287( 4): 2398–2409.[citado 2025 nov. 04 ] Available from: https://doi.org/10.1074/jbc.M111.303503

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