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  • Source: Journal of the Brazilian Chemical Society. Unidade: IQ

    Subjects: PROTEÍNAS, ANÁLISE EM FLUXO CONTÍNUO, CROMATOGRAFIA LÍQUIDA

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      VITEK, Renan e NASCIMENTO, Fernando Henrique do e MASINI, Jorge Cesar. Reversed-Phase liquid chromatography methods based on C18 polymer monoliths for the determination of urinary myoglobin. Journal of the Brazilian Chemical Society, v. 34, n. 11, p. 1601-1610, 2023Tradução . . Disponível em: https://doi.org/10.21577/0103-5053.20230084. Acesso em: 04 nov. 2024.
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      Vitek, R., Nascimento, F. H. do, & Masini, J. C. (2023). Reversed-Phase liquid chromatography methods based on C18 polymer monoliths for the determination of urinary myoglobin. Journal of the Brazilian Chemical Society, 34( 11), 1601-1610. doi:10.21577/0103-5053.20230084
    • NLM

      Vitek R, Nascimento FH do, Masini JC. Reversed-Phase liquid chromatography methods based on C18 polymer monoliths for the determination of urinary myoglobin [Internet]. Journal of the Brazilian Chemical Society. 2023 ; 34( 11): 1601-1610.[citado 2024 nov. 04 ] Available from: https://doi.org/10.21577/0103-5053.20230084
    • Vancouver

      Vitek R, Nascimento FH do, Masini JC. Reversed-Phase liquid chromatography methods based on C18 polymer monoliths for the determination of urinary myoglobin [Internet]. Journal of the Brazilian Chemical Society. 2023 ; 34( 11): 1601-1610.[citado 2024 nov. 04 ] Available from: https://doi.org/10.21577/0103-5053.20230084
  • Source: Advances in Sample Preparation. Unidade: IQ

    Subjects: CROMATOGRAFIA LÍQUIDA, OVO, PROTEÍNAS, TROCA IÔNICA

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      NASCIMENTO, Fernando Henrique do e VITEK, Renan e MASINI, Jorge Cesar. Porous polymer monoliths with complementary retention mechanisms for online solid-phase extraction liquid chromatography to determine lysozyme in egg white. Advances in Sample Preparation, v. 7, p. 1-7 art. 100069, 2023Tradução . . Disponível em: https://doi.org/10.1016/j.sampre.2023.100069. Acesso em: 04 nov. 2024.
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      Nascimento, F. H. do, Vitek, R., & Masini, J. C. (2023). Porous polymer monoliths with complementary retention mechanisms for online solid-phase extraction liquid chromatography to determine lysozyme in egg white. Advances in Sample Preparation, 7, 1-7 art. 100069. doi:10.1016/j.sampre.2023.100069
    • NLM

      Nascimento FH do, Vitek R, Masini JC. Porous polymer monoliths with complementary retention mechanisms for online solid-phase extraction liquid chromatography to determine lysozyme in egg white [Internet]. Advances in Sample Preparation. 2023 ; 7 1-7 art. 100069.[citado 2024 nov. 04 ] Available from: https://doi.org/10.1016/j.sampre.2023.100069
    • Vancouver

      Nascimento FH do, Vitek R, Masini JC. Porous polymer monoliths with complementary retention mechanisms for online solid-phase extraction liquid chromatography to determine lysozyme in egg white [Internet]. Advances in Sample Preparation. 2023 ; 7 1-7 art. 100069.[citado 2024 nov. 04 ] Available from: https://doi.org/10.1016/j.sampre.2023.100069
  • Source: Biosensors. Unidade: IQ

    Subjects: ELETROQUÍMICA, DOENÇA DE ALZHEIMER, PROTEÍNAS

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      SHARMA, Abhinav et al. Electrochemical immunosensors developed for amyloid-beta and Tau proteins, leading biomarkers of Alzheimer’s disease. Biosensors, v. 13, p. 1-28 art. 742, 2023Tradução . . Disponível em: https://doi.org/10.3390/bios13070742. Acesso em: 04 nov. 2024.
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      Sharma, A., Angnes, L., Sattarahmady, N., Heli, H., & Negahdary, M. (2023). Electrochemical immunosensors developed for amyloid-beta and Tau proteins, leading biomarkers of Alzheimer’s disease. Biosensors, 13, 1-28 art. 742. doi:10.3390/bios13070742
    • NLM

      Sharma A, Angnes L, Sattarahmady N, Heli H, Negahdary M. Electrochemical immunosensors developed for amyloid-beta and Tau proteins, leading biomarkers of Alzheimer’s disease [Internet]. Biosensors. 2023 ; 13 1-28 art. 742.[citado 2024 nov. 04 ] Available from: https://doi.org/10.3390/bios13070742
    • Vancouver

      Sharma A, Angnes L, Sattarahmady N, Heli H, Negahdary M. Electrochemical immunosensors developed for amyloid-beta and Tau proteins, leading biomarkers of Alzheimer’s disease [Internet]. Biosensors. 2023 ; 13 1-28 art. 742.[citado 2024 nov. 04 ] Available from: https://doi.org/10.3390/bios13070742
  • Source: Brazilian Journal of Analytical Chemistry. Unidade: IQ

    Subjects: COGUMELOS COMESTÍVEIS, PROTEÍNAS

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      DIAS, Saphire de Souza Lana et al. Optimization of the protein sequential extraction for quantitative determination of albumins, globulins, prolamins and glutelins in edible mushrooms. Brazilian Journal of Analytical Chemistry, v. 10, n. 40, p. 198-208, 2023Tradução . . Disponível em: https://doi.org/10.30744/brjac.2179-3425.TN-113-2022. Acesso em: 04 nov. 2024.
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      Dias, S. de S. L., Oliveira, A. P. de, Gaubeur, I., Nomura, C. S., & Naozuka, J. (2023). Optimization of the protein sequential extraction for quantitative determination of albumins, globulins, prolamins and glutelins in edible mushrooms. Brazilian Journal of Analytical Chemistry, 10( 40), 198-208. doi:10.30744/brjac.2179-3425.TN-113-2022
    • NLM

      Dias S de SL, Oliveira AP de, Gaubeur I, Nomura CS, Naozuka J. Optimization of the protein sequential extraction for quantitative determination of albumins, globulins, prolamins and glutelins in edible mushrooms [Internet]. Brazilian Journal of Analytical Chemistry. 2023 ; 10( 40): 198-208.[citado 2024 nov. 04 ] Available from: https://doi.org/10.30744/brjac.2179-3425.TN-113-2022
    • Vancouver

      Dias S de SL, Oliveira AP de, Gaubeur I, Nomura CS, Naozuka J. Optimization of the protein sequential extraction for quantitative determination of albumins, globulins, prolamins and glutelins in edible mushrooms [Internet]. Brazilian Journal of Analytical Chemistry. 2023 ; 10( 40): 198-208.[citado 2024 nov. 04 ] Available from: https://doi.org/10.30744/brjac.2179-3425.TN-113-2022
  • Source: Talanta. Unidade: IQ

    Subjects: NANOTECNOLOGIA, OURO, PROTEÍNAS, ELETROQUÍMICA

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      NEGAHDARY, Masoud e ANGNES, Lúcio. An aptasensing platform for detection of heat shock protein 70 kDa (HSP70) using a modified gold electrode with lady fern-like gold (LFG) nanostructure. Talanta, v. 246, p. 1-12 art. 123511, 2022Tradução . . Disponível em: https://doi.org/10.1016/j.talanta.2022.123511. Acesso em: 04 nov. 2024.
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      Negahdary, M., & Angnes, L. (2022). An aptasensing platform for detection of heat shock protein 70 kDa (HSP70) using a modified gold electrode with lady fern-like gold (LFG) nanostructure. Talanta, 246, 1-12 art. 123511. doi:10.1016/j.talanta.2022.123511
    • NLM

      Negahdary M, Angnes L. An aptasensing platform for detection of heat shock protein 70 kDa (HSP70) using a modified gold electrode with lady fern-like gold (LFG) nanostructure [Internet]. Talanta. 2022 ; 246 1-12 art. 123511.[citado 2024 nov. 04 ] Available from: https://doi.org/10.1016/j.talanta.2022.123511
    • Vancouver

      Negahdary M, Angnes L. An aptasensing platform for detection of heat shock protein 70 kDa (HSP70) using a modified gold electrode with lady fern-like gold (LFG) nanostructure [Internet]. Talanta. 2022 ; 246 1-12 art. 123511.[citado 2024 nov. 04 ] Available from: https://doi.org/10.1016/j.talanta.2022.123511
  • Source: International Journal of Biological Macromolecules. Unidade: IQ

    Subjects: POLISSACARÍDEOS, PROTEÍNAS

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      ALAVARSE, Alex Carvalho et al. Crosslinkers for polysaccharides and proteins: synthesis conditions, mechanisms, and crosslinking efficiency, a review. International Journal of Biological Macromolecules, v. 202, p. 558-596, 2022Tradução . . Disponível em: https://doi.org/10.1016/j.ijbiomac.2022.01.029. Acesso em: 04 nov. 2024.
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      Alavarse, A. C., Frachini, E. C. G., Silva, R. L. C. G. da, Lima, V. H., Shavandi, A., & Petri, D. F. S. (2022). Crosslinkers for polysaccharides and proteins: synthesis conditions, mechanisms, and crosslinking efficiency, a review. International Journal of Biological Macromolecules, 202, 558-596. doi:10.1016/j.ijbiomac.2022.01.029
    • NLM

      Alavarse AC, Frachini ECG, Silva RLCG da, Lima VH, Shavandi A, Petri DFS. Crosslinkers for polysaccharides and proteins: synthesis conditions, mechanisms, and crosslinking efficiency, a review [Internet]. International Journal of Biological Macromolecules. 2022 ; 202 558-596.[citado 2024 nov. 04 ] Available from: https://doi.org/10.1016/j.ijbiomac.2022.01.029
    • Vancouver

      Alavarse AC, Frachini ECG, Silva RLCG da, Lima VH, Shavandi A, Petri DFS. Crosslinkers for polysaccharides and proteins: synthesis conditions, mechanisms, and crosslinking efficiency, a review [Internet]. International Journal of Biological Macromolecules. 2022 ; 202 558-596.[citado 2024 nov. 04 ] Available from: https://doi.org/10.1016/j.ijbiomac.2022.01.029
  • Source: Bioconjugate Chemistry. Unidade: IQ

    Subjects: NANOPARTÍCULAS, PEPTÍDEOS, PROTEÍNAS

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      SILVA, Rafael Trivella Pacheco da et al. Stimuli-responsive regulation of Biocatalysis through metallic nanoparticle interaction. Bioconjugate Chemistry, v. 33, n. 1, p. 53–66, 2022Tradução . . Disponível em: https://doi.org/10.1021/acs.bioconjchem.1c00515. Acesso em: 04 nov. 2024.
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      Silva, R. T. P. da, Barros, H. R. de, Sandrini, D. M. F., & Torresi, S. I. C. de. (2022). Stimuli-responsive regulation of Biocatalysis through metallic nanoparticle interaction. Bioconjugate Chemistry, 33( 1), 53–66. doi:10.1021/acs.bioconjchem.1c00515
    • NLM

      Silva RTP da, Barros HR de, Sandrini DMF, Torresi SIC de. Stimuli-responsive regulation of Biocatalysis through metallic nanoparticle interaction [Internet]. Bioconjugate Chemistry. 2022 ; 33( 1): 53–66.[citado 2024 nov. 04 ] Available from: https://doi.org/10.1021/acs.bioconjchem.1c00515
    • Vancouver

      Silva RTP da, Barros HR de, Sandrini DMF, Torresi SIC de. Stimuli-responsive regulation of Biocatalysis through metallic nanoparticle interaction [Internet]. Bioconjugate Chemistry. 2022 ; 33( 1): 53–66.[citado 2024 nov. 04 ] Available from: https://doi.org/10.1021/acs.bioconjchem.1c00515
  • Source: ACS Food Science and Technology. Unidade: IQ

    Subjects: AÇAÍ, POLPA, PEPTÍDEOS, PROTEÍNAS, ELEMENTOS DE TRANSIÇÃO

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      SANTOS, Giselaine Alves dos et al. Bioaccessibility of essential elements in açaí (Euterpe oleracea Mart.) pulp. ACS Food Science and Technology, v. 1, p. 874−883, 2021Tradução . . Disponível em: https://doi.org/10.1021/acsfoodscitech.1c00070. Acesso em: 04 nov. 2024.
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      Santos, G. A. dos, Carvalho, A. A. C., Oliveira, A. P., Naozuka, J., Matta, F. V., Felipe-Sotelo, M., et al. (2021). Bioaccessibility of essential elements in açaí (Euterpe oleracea Mart.) pulp. ACS Food Science and Technology, 1, 874−883. doi:10.1021/acsfoodscitech.1c00070
    • NLM

      Santos GA dos, Carvalho AAC, Oliveira AP, Naozuka J, Matta FV, Felipe-Sotelo M, Ward NI, Correa NCF, Nomura CS. Bioaccessibility of essential elements in açaí (Euterpe oleracea Mart.) pulp [Internet]. ACS Food Science and Technology. 2021 ; 1 874−883.[citado 2024 nov. 04 ] Available from: https://doi.org/10.1021/acsfoodscitech.1c00070
    • Vancouver

      Santos GA dos, Carvalho AAC, Oliveira AP, Naozuka J, Matta FV, Felipe-Sotelo M, Ward NI, Correa NCF, Nomura CS. Bioaccessibility of essential elements in açaí (Euterpe oleracea Mart.) pulp [Internet]. ACS Food Science and Technology. 2021 ; 1 874−883.[citado 2024 nov. 04 ] Available from: https://doi.org/10.1021/acsfoodscitech.1c00070
  • Source: Bioengineering. Unidade: IQ

    Subjects: PROTEÍNAS, BIOMATERIAIS, PEPTÍDEOS

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      MIRZAEI, Mahta et al. Protein-based 3D biofabrication of biomaterials. Bioengineering, v. 8, p. 1-26 art. 48, 2021Tradução . . Disponível em: https://doi.org/10.3390/bioengineering8040048. Acesso em: 04 nov. 2024.
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      Mirzaei, M., Okoro, O. V., Nie, L., Petri, D. F. S., & Shavandi, A. (2021). Protein-based 3D biofabrication of biomaterials. Bioengineering, 8, 1-26 art. 48. doi:10.3390/bioengineering8040048
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      Mirzaei M, Okoro OV, Nie L, Petri DFS, Shavandi A. Protein-based 3D biofabrication of biomaterials [Internet]. Bioengineering. 2021 ; 8 1-26 art. 48.[citado 2024 nov. 04 ] Available from: https://doi.org/10.3390/bioengineering8040048
    • Vancouver

      Mirzaei M, Okoro OV, Nie L, Petri DFS, Shavandi A. Protein-based 3D biofabrication of biomaterials [Internet]. Bioengineering. 2021 ; 8 1-26 art. 48.[citado 2024 nov. 04 ] Available from: https://doi.org/10.3390/bioengineering8040048
  • Source: RSC Advances. Unidade: IQ

    Subjects: PROTEÍNAS, ENZIMAS, ELETROQUÍMICA, BIOMARCADORES, MALÁRIA

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      GANDARILLA, Ariamna María Dip et al. One-step enzyme-free dual electrochemical immunosensor for histidine-rich protein 2 determination. RSC Advances, v. 11, p. 408–415, 2021Tradução . . Disponível em: https://doi.org/10.1039/d0ra08729g. Acesso em: 04 nov. 2024.
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      Gandarilla, A. M. D., Regiart, D. M. G., Bertotti, M., Glória, J. C., Mariuba, L. A. M., & Brito, W. R. (2021). One-step enzyme-free dual electrochemical immunosensor for histidine-rich protein 2 determination. RSC Advances, 11, 408–415. doi:10.1039/d0ra08729g
    • NLM

      Gandarilla AMD, Regiart DMG, Bertotti M, Glória JC, Mariuba LAM, Brito WR. One-step enzyme-free dual electrochemical immunosensor for histidine-rich protein 2 determination [Internet]. RSC Advances. 2021 ; 11 408–415.[citado 2024 nov. 04 ] Available from: https://doi.org/10.1039/d0ra08729g
    • Vancouver

      Gandarilla AMD, Regiart DMG, Bertotti M, Glória JC, Mariuba LAM, Brito WR. One-step enzyme-free dual electrochemical immunosensor for histidine-rich protein 2 determination [Internet]. RSC Advances. 2021 ; 11 408–415.[citado 2024 nov. 04 ] Available from: https://doi.org/10.1039/d0ra08729g
  • Source: Journal of Separation Science. Unidade: IQ

    Subjects: CROMATOGRAFIA, PROTEÍNAS

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      NASCIMENTO, Fernando Henrique do et al. Construction of polymer monolithic columns in polypropylene ink-pen tubes for separation of proteins by cation-exchange chromatography. Journal of Separation Science, v. 43, n. 22, p. 4123-4130, 2020Tradução . . Disponível em: https://doi.org/10.1002/jssc.202000803. Acesso em: 04 nov. 2024.
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      Nascimento, F. H. do, Trazzi, C. R. L., Moraes, A. H., Velasques, C. M., Costa, D. M. de S., & Masini, J. C. (2020). Construction of polymer monolithic columns in polypropylene ink-pen tubes for separation of proteins by cation-exchange chromatography. Journal of Separation Science, 43( 22), 4123-4130. doi:10.1002/jssc.202000803
    • NLM

      Nascimento FH do, Trazzi CRL, Moraes AH, Velasques CM, Costa DM de S, Masini JC. Construction of polymer monolithic columns in polypropylene ink-pen tubes for separation of proteins by cation-exchange chromatography [Internet]. Journal of Separation Science. 2020 ; 43( 22): 4123-4130.[citado 2024 nov. 04 ] Available from: https://doi.org/10.1002/jssc.202000803
    • Vancouver

      Nascimento FH do, Trazzi CRL, Moraes AH, Velasques CM, Costa DM de S, Masini JC. Construction of polymer monolithic columns in polypropylene ink-pen tubes for separation of proteins by cation-exchange chromatography [Internet]. Journal of Separation Science. 2020 ; 43( 22): 4123-4130.[citado 2024 nov. 04 ] Available from: https://doi.org/10.1002/jssc.202000803
  • Source: Materials Advances. Unidade: IQ

    Subjects: PROTEÍNAS, ENGENHARIA TECIDUAL

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      DELECHIAVE, Giovanne et al. Tuning protein delivery from different architectures of layer-by-layer assemblies on polymer films. Materials Advances, v. 1, p. 2043-2056, 2020Tradução . . Disponível em: https://doi.org/10.1039/d0ma00432d. Acesso em: 04 nov. 2024.
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      Delechiave, G., Naves, A. F., Kolanthai, E., Silva, R. A. da, Vlasman, R. C., Petri, D. F. S., et al. (2020). Tuning protein delivery from different architectures of layer-by-layer assemblies on polymer films. Materials Advances, 1, 2043-2056. doi:10.1039/d0ma00432d
    • NLM

      Delechiave G, Naves AF, Kolanthai E, Silva RA da, Vlasman RC, Petri DFS, Torresi RM, Catalani LH. Tuning protein delivery from different architectures of layer-by-layer assemblies on polymer films [Internet]. Materials Advances. 2020 ; 1 2043-2056.[citado 2024 nov. 04 ] Available from: https://doi.org/10.1039/d0ma00432d
    • Vancouver

      Delechiave G, Naves AF, Kolanthai E, Silva RA da, Vlasman RC, Petri DFS, Torresi RM, Catalani LH. Tuning protein delivery from different architectures of layer-by-layer assemblies on polymer films [Internet]. Materials Advances. 2020 ; 1 2043-2056.[citado 2024 nov. 04 ] Available from: https://doi.org/10.1039/d0ma00432d
  • Source: Talanta. Unidade: IQ

    Subjects: CROMATOGRAFIA LÍQUIDA, PROTEÍNAS, URINA, OVO

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      NASCIMENTO, Fernando Henrique do et al. Fast construction of polymer monolithic columns inside fluorinated ethylene propylene (FEP) tubes for separation of proteins by reversed-phase liquid chromatography. Talanta, v. 217, p. 1-7 art. 121063, 2020Tradução . . Disponível em: https://doi.org/10.1016/j.talanta.2020.121063. Acesso em: 04 nov. 2024.
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      Nascimento, F. H. do, Moraes, A. H., Trazzi, C. R. L., Velasques, C. M., & Masini, J. C. (2020). Fast construction of polymer monolithic columns inside fluorinated ethylene propylene (FEP) tubes for separation of proteins by reversed-phase liquid chromatography. Talanta, 217, 1-7 art. 121063. doi:10.1016/j.talanta.2020.121063
    • NLM

      Nascimento FH do, Moraes AH, Trazzi CRL, Velasques CM, Masini JC. Fast construction of polymer monolithic columns inside fluorinated ethylene propylene (FEP) tubes for separation of proteins by reversed-phase liquid chromatography [Internet]. Talanta. 2020 ; 217 1-7 art. 121063.[citado 2024 nov. 04 ] Available from: https://doi.org/10.1016/j.talanta.2020.121063
    • Vancouver

      Nascimento FH do, Moraes AH, Trazzi CRL, Velasques CM, Masini JC. Fast construction of polymer monolithic columns inside fluorinated ethylene propylene (FEP) tubes for separation of proteins by reversed-phase liquid chromatography [Internet]. Talanta. 2020 ; 217 1-7 art. 121063.[citado 2024 nov. 04 ] Available from: https://doi.org/10.1016/j.talanta.2020.121063
  • Source: Journal of Inorganic Biochemistry. Unidades: IQ, IF

    Subjects: PROTEÍNAS, ANTINEOPLÁSICOS, COBRE, ZINCO

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      CASTELLI, Silvia et al. Comparative studies of oxindolimine-metal complexes as inhibitors of human DNA topoisomerase IB. Journal of Inorganic Biochemistry, v. 186, p. 85-94, 2018Tradução . . Disponível em: https://doi.org/10.1016/j.jinorgbio.2018.05.012. Acesso em: 04 nov. 2024.
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      Castelli, S., Gonçalves, M. B., Katkar, P., Stuchi, G. C., Couto, R. A. A. de, Petrilli, H. M., & Ferreira, A. M. da C. (2018). Comparative studies of oxindolimine-metal complexes as inhibitors of human DNA topoisomerase IB. Journal of Inorganic Biochemistry, 186, 85-94. doi:10.1016/j.jinorgbio.2018.05.012
    • NLM

      Castelli S, Gonçalves MB, Katkar P, Stuchi GC, Couto RAA de, Petrilli HM, Ferreira AM da C. Comparative studies of oxindolimine-metal complexes as inhibitors of human DNA topoisomerase IB [Internet]. Journal of Inorganic Biochemistry. 2018 ;186 85-94.[citado 2024 nov. 04 ] Available from: https://doi.org/10.1016/j.jinorgbio.2018.05.012
    • Vancouver

      Castelli S, Gonçalves MB, Katkar P, Stuchi GC, Couto RAA de, Petrilli HM, Ferreira AM da C. Comparative studies of oxindolimine-metal complexes as inhibitors of human DNA topoisomerase IB [Internet]. Journal of Inorganic Biochemistry. 2018 ;186 85-94.[citado 2024 nov. 04 ] Available from: https://doi.org/10.1016/j.jinorgbio.2018.05.012
  • Source: PLOS ONE. Unidades: IB, IQ

    Subjects: PROTEÍNAS, ANTIOXIDANTES, OXIDAÇÃO, BACTÉRIAS ANAERÓBICAS GRAM-NEGATIVAS, ENZIMAS, DOENÇAS DE PLANTAS

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      PICCIRILLO, Erika et al. Structural insights on the efficient catalysis of hydroperoxide reduction by Ohr: crystallographic and molecular dynamics approaches. PLOS ONE, v. 13, n. 5, p. 1-23, 2018Tradução . . Disponível em: https://doi.org/10.1371/journal.pone.0196918. Acesso em: 04 nov. 2024.
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      Piccirillo, E., Alegria, T. G. P., Discola, K. F., Cussiol, J. R. R., Domingos, R. M., Oliveira, M. A. de, et al. (2018). Structural insights on the efficient catalysis of hydroperoxide reduction by Ohr: crystallographic and molecular dynamics approaches. PLOS ONE, 13( 5), 1-23. doi:10.1371/journal.pone.0196918
    • NLM

      Piccirillo E, Alegria TGP, Discola KF, Cussiol JRR, Domingos RM, Oliveira MA de, Rezende L de, Netto LES, Amaral AT do. Structural insights on the efficient catalysis of hydroperoxide reduction by Ohr: crystallographic and molecular dynamics approaches [Internet]. PLOS ONE. 2018 ; 13( 5): 1-23.[citado 2024 nov. 04 ] Available from: https://doi.org/10.1371/journal.pone.0196918
    • Vancouver

      Piccirillo E, Alegria TGP, Discola KF, Cussiol JRR, Domingos RM, Oliveira MA de, Rezende L de, Netto LES, Amaral AT do. Structural insights on the efficient catalysis of hydroperoxide reduction by Ohr: crystallographic and molecular dynamics approaches [Internet]. PLOS ONE. 2018 ; 13( 5): 1-23.[citado 2024 nov. 04 ] Available from: https://doi.org/10.1371/journal.pone.0196918
  • Source: Proceedings. Conference titles: World Chemistry Congress. Unidade: IQ

    Subjects: PROTEÍNAS, BIOMATERIAIS

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      KOLANTHAI, Elayaraja e CATALANI, Luiz Henrique. Study of model proteins with graphene oxide self assembled on electrospun polycaprolactone fiber by layer-by-layer technique. 2017, Anais.. Durham: International Union of Pure and Applied Chemistry (IUPAC), 2017. Disponível em: http://www.neopixdmi.com.br/@mci/iupac2017/. Acesso em: 04 nov. 2024.
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      Kolanthai, E., & Catalani, L. H. (2017). Study of model proteins with graphene oxide self assembled on electrospun polycaprolactone fiber by layer-by-layer technique. In Proceedings. Durham: International Union of Pure and Applied Chemistry (IUPAC). Recuperado de http://www.neopixdmi.com.br/@mci/iupac2017/
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      Kolanthai E, Catalani LH. Study of model proteins with graphene oxide self assembled on electrospun polycaprolactone fiber by layer-by-layer technique [Internet]. Proceedings. 2017 ;[citado 2024 nov. 04 ] Available from: http://www.neopixdmi.com.br/@mci/iupac2017/
    • Vancouver

      Kolanthai E, Catalani LH. Study of model proteins with graphene oxide self assembled on electrospun polycaprolactone fiber by layer-by-layer technique [Internet]. Proceedings. 2017 ;[citado 2024 nov. 04 ] Available from: http://www.neopixdmi.com.br/@mci/iupac2017/
  • Source: Journal of Separation Science. Unidade: IQ

    Subjects: PROTEÍNAS, CROMATOGRAFIA LÍQUIDA

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      MASINI, Jorge Cesar. Semi-micro reversed-phase liquid chromatography for the separation of alkylbenzenes and proteins exploiting methacrylate and polystyrene-basedmonolithic columns. Journal of Separation Science, v. 39, n. 9, p. 1648-1655, 2016Tradução . . Disponível em: https://doi.org/10.1002/jssc.201600049. Acesso em: 04 nov. 2024.
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      Masini, J. C. (2016). Semi-micro reversed-phase liquid chromatography for the separation of alkylbenzenes and proteins exploiting methacrylate and polystyrene-basedmonolithic columns. Journal of Separation Science, 39( 9), 1648-1655. doi:10.1002/jssc.201600049
    • NLM

      Masini JC. Semi-micro reversed-phase liquid chromatography for the separation of alkylbenzenes and proteins exploiting methacrylate and polystyrene-basedmonolithic columns [Internet]. Journal of Separation Science. 2016 ; 39( 9): 1648-1655.[citado 2024 nov. 04 ] Available from: https://doi.org/10.1002/jssc.201600049
    • Vancouver

      Masini JC. Semi-micro reversed-phase liquid chromatography for the separation of alkylbenzenes and proteins exploiting methacrylate and polystyrene-basedmonolithic columns [Internet]. Journal of Separation Science. 2016 ; 39( 9): 1648-1655.[citado 2024 nov. 04 ] Available from: https://doi.org/10.1002/jssc.201600049
  • Source: Analytical and Bioanalytical Chemistry. Unidade: IQ

    Subjects: ANÁLISE POR INJEÇÃO SEQUENCIAL, PROTEÍNAS, TROCA IÔNICA

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      MASINI, Jorge Cesar. Separation of proteins by cation exchange sequential injection chromatography using a polymeric monolithic column. Analytical and Bioanalytical Chemistry, v. 408, n. 5, p. 1445-1452, 2016Tradução . . Disponível em: https://doi.org/10.1007/s00216-015-9242-9. Acesso em: 04 nov. 2024.
    • APA

      Masini, J. C. (2016). Separation of proteins by cation exchange sequential injection chromatography using a polymeric monolithic column. Analytical and Bioanalytical Chemistry, 408( 5), 1445-1452. doi:10.1007/s00216-015-9242-9
    • NLM

      Masini JC. Separation of proteins by cation exchange sequential injection chromatography using a polymeric monolithic column [Internet]. Analytical and Bioanalytical Chemistry. 2016 ; 408( 5): 1445-1452.[citado 2024 nov. 04 ] Available from: https://doi.org/10.1007/s00216-015-9242-9
    • Vancouver

      Masini JC. Separation of proteins by cation exchange sequential injection chromatography using a polymeric monolithic column [Internet]. Analytical and Bioanalytical Chemistry. 2016 ; 408( 5): 1445-1452.[citado 2024 nov. 04 ] Available from: https://doi.org/10.1007/s00216-015-9242-9
  • Source: Resumos. Conference titles: Reunião Anual da Sociedade Brasileira de Química/SBQ. Unidade: IQ

    Subjects: FILMES FINOS, PROTEÍNAS

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      DELECHIAVE, Giovanne e NAVES, Alliny Ferreira e CATALANI, Luiz Henrique. Reservatórios proteicos a partir de multicamadas automontadas via LbL depositadas em filmes de PLLA e PCL. 2016, Anais.. São Paulo: Sociedade Brasileira de Química/SBQ, 2016. . Acesso em: 04 nov. 2024.
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      Delechiave, G., Naves, A. F., & Catalani, L. H. (2016). Reservatórios proteicos a partir de multicamadas automontadas via LbL depositadas em filmes de PLLA e PCL. In Resumos. São Paulo: Sociedade Brasileira de Química/SBQ.
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      Delechiave G, Naves AF, Catalani LH. Reservatórios proteicos a partir de multicamadas automontadas via LbL depositadas em filmes de PLLA e PCL. Resumos. 2016 ;[citado 2024 nov. 04 ]
    • Vancouver

      Delechiave G, Naves AF, Catalani LH. Reservatórios proteicos a partir de multicamadas automontadas via LbL depositadas em filmes de PLLA e PCL. Resumos. 2016 ;[citado 2024 nov. 04 ]
  • Source: Nanoscale Research Letters. Unidade: IQ

    Subjects: NANOPARTÍCULAS, ASPERGILLUS, PROTEÍNAS

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      BALLOTTIN, Daniela et al. Elucidating protein involvement in the stabilization of the biogenic silver nanoparticles. Nanoscale Research Letters, v. 11, p. 1-9 art. 313, 2016Tradução . . Disponível em: https://doi.org/10.1186/s11671-016-1538-y. Acesso em: 04 nov. 2024.
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      Ballottin, D., Fulaz, S., Souza, M. L., Corio, P., Rodrigues, A. G., Souza, A. O., et al. (2016). Elucidating protein involvement in the stabilization of the biogenic silver nanoparticles. Nanoscale Research Letters, 11, 1-9 art. 313. doi:10.1186/s11671-016-1538-y
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      Ballottin D, Fulaz S, Souza ML, Corio P, Rodrigues AG, Souza AO, Gaspari PM, Gomes AF, Gozzo F, Tasic L. Elucidating protein involvement in the stabilization of the biogenic silver nanoparticles [Internet]. Nanoscale Research Letters. 2016 ; 11 1-9 art. 313.[citado 2024 nov. 04 ] Available from: https://doi.org/10.1186/s11671-016-1538-y
    • Vancouver

      Ballottin D, Fulaz S, Souza ML, Corio P, Rodrigues AG, Souza AO, Gaspari PM, Gomes AF, Gozzo F, Tasic L. Elucidating protein involvement in the stabilization of the biogenic silver nanoparticles [Internet]. Nanoscale Research Letters. 2016 ; 11 1-9 art. 313.[citado 2024 nov. 04 ] Available from: https://doi.org/10.1186/s11671-016-1538-y

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