Filtros : "PROTEÍNAS" "Holanda" "IQ" Limpar

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  • Source: Journal of Proteomics. Unidades: ICB, IQ

    Subjects: PARASITOLOGIA, LEISHMANIA, LEISHMANIA BRASILIENSIS, LEISHMANIA INFANTUM, LEISHMANIOSE CUTÂNEA, PROTEÔMICA, ANIMAIS PARASITOS, PROTEÍNAS, TEMPERATURA, ESTRESSE

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      MULE, Simon Ngao et al. The protein map of the protozoan parasite Leishmania (Leishmania) amazonensis, Leishmania (Viannia) braziliensis and Leishmania (Leishmania) infantum during growth phase transition and temperature stress. Journal of Proteomics, v. 295, p. 17 , 2024Tradução . . Disponível em: https://doi.org/10.1016/j.jprot.2024.105088. Acesso em: 11 out. 2024.
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      Mule, S. N., Saad, J. S., Sauter, I. P., Fernandes, L. R., Oliveira, G. S. de, Quina, D. O., et al. (2024). The protein map of the protozoan parasite Leishmania (Leishmania) amazonensis, Leishmania (Viannia) braziliensis and Leishmania (Leishmania) infantum during growth phase transition and temperature stress. Journal of Proteomics, 295, 17 . doi:10.1016/j.jprot.2024.105088
    • NLM

      Mule SN, Saad JS, Sauter IP, Fernandes LR, Oliveira GS de, Quina DO, Tano FT, Brandt-Almeida D, Padrón G, Larsen MR, Stolf BS, Cortez M, Palmisano G. The protein map of the protozoan parasite Leishmania (Leishmania) amazonensis, Leishmania (Viannia) braziliensis and Leishmania (Leishmania) infantum during growth phase transition and temperature stress [Internet]. Journal of Proteomics. 2024 ; 295 17 .[citado 2024 out. 11 ] Available from: https://doi.org/10.1016/j.jprot.2024.105088
    • Vancouver

      Mule SN, Saad JS, Sauter IP, Fernandes LR, Oliveira GS de, Quina DO, Tano FT, Brandt-Almeida D, Padrón G, Larsen MR, Stolf BS, Cortez M, Palmisano G. The protein map of the protozoan parasite Leishmania (Leishmania) amazonensis, Leishmania (Viannia) braziliensis and Leishmania (Leishmania) infantum during growth phase transition and temperature stress [Internet]. Journal of Proteomics. 2024 ; 295 17 .[citado 2024 out. 11 ] Available from: https://doi.org/10.1016/j.jprot.2024.105088
  • 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: 11 out. 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 out. 11 ] Available from: https://doi.org/10.1016/j.sampre.2023.100069
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      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 out. 11 ] Available from: https://doi.org/10.1016/j.sampre.2023.100069
  • 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: 11 out. 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 out. 11 ] 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 out. 11 ] Available from: https://doi.org/10.1016/j.talanta.2022.123511
  • Source: Molecular Biology Reports. Unidade: IQ

    Subjects: CITOCINAS, PROTEÍNAS, APOPTOSE, MELANOMA, ALCALOIDES

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      PALMA, Tais Vidal et al. Berberine increases the expression of cytokines and proteins linked to apoptosis in human melanoma cells. Molecular Biology Reports, v. 49, p. 2037–2046, 2022Tradução . . Disponível em: https://doi.org/10.1007/s11033-021-07022-4. Acesso em: 11 out. 2024.
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      Palma, T. V., Bianchin, N. B., Oliveira, J. S. de, Assmann, C. E., Oliveira, M. das N., Schetinger, M. R. C., et al. (2022). Berberine increases the expression of cytokines and proteins linked to apoptosis in human melanoma cells. Molecular Biology Reports, 49, 2037–2046. doi:10.1007/s11033-021-07022-4
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      Palma TV, Bianchin NB, Oliveira JS de, Assmann CE, Oliveira M das N, Schetinger MRC, Morsch VM, Ulrich H, Pillat MM, Andrade CM de. Berberine increases the expression of cytokines and proteins linked to apoptosis in human melanoma cells [Internet]. Molecular Biology Reports. 2022 ; 49 2037–2046.[citado 2024 out. 11 ] Available from: https://doi.org/10.1007/s11033-021-07022-4
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      Palma TV, Bianchin NB, Oliveira JS de, Assmann CE, Oliveira M das N, Schetinger MRC, Morsch VM, Ulrich H, Pillat MM, Andrade CM de. Berberine increases the expression of cytokines and proteins linked to apoptosis in human melanoma cells [Internet]. Molecular Biology Reports. 2022 ; 49 2037–2046.[citado 2024 out. 11 ] Available from: https://doi.org/10.1007/s11033-021-07022-4
  • 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: 11 out. 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 out. 11 ] Available from: https://doi.org/10.1016/j.ijbiomac.2022.01.029
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      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 out. 11 ] Available from: https://doi.org/10.1016/j.ijbiomac.2022.01.029
  • Source: Fungal Biology. Unidade: IQ

    Subjects: GENES, PROTEÍNAS

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      GEORG, Raphaela de Castro et al. Small heat shock protein genes are developmentally regulated during stress and non-stress conditions in Blastocladiella emersonii. Fungal Biology, v. 124, n. 5, p. 482-489, 2020Tradução . . Disponível em: https://doi.org/10.1016/j.funbio.2020.02.009. Acesso em: 11 out. 2024.
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      Georg, R. de C., Oshiquiri, L. H., Barbosa-Filho, J. R., & Gomes, S. L. (2020). Small heat shock protein genes are developmentally regulated during stress and non-stress conditions in Blastocladiella emersonii. Fungal Biology, 124( 5), 482-489. doi:10.1016/j.funbio.2020.02.009
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      Georg R de C, Oshiquiri LH, Barbosa-Filho JR, Gomes SL. Small heat shock protein genes are developmentally regulated during stress and non-stress conditions in Blastocladiella emersonii [Internet]. Fungal Biology. 2020 ; 124( 5): 482-489.[citado 2024 out. 11 ] Available from: https://doi.org/10.1016/j.funbio.2020.02.009
    • Vancouver

      Georg R de C, Oshiquiri LH, Barbosa-Filho JR, Gomes SL. Small heat shock protein genes are developmentally regulated during stress and non-stress conditions in Blastocladiella emersonii [Internet]. Fungal Biology. 2020 ; 124( 5): 482-489.[citado 2024 out. 11 ] Available from: https://doi.org/10.1016/j.funbio.2020.02.009
  • 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: 11 out. 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 out. 11 ] 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 out. 11 ] Available from: https://doi.org/10.1016/j.talanta.2020.121063
  • Source: Biochimica et Biophysica Acta-Bioenergetics. Unidade: IQ

    Subjects: HIDRATAÇÃO, PROTEÍNAS, MOLÉCULA

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      TEIXEIRA, Murilo Hoias e ARANTES, Guilherme Menegon. Balanced internal hydration discriminates substrate binding to respiratory complex I. Biochimica et Biophysica Acta-Bioenergetics, v. 1860, n. 7, p. 541-548, 2019Tradução . . Disponível em: https://doi.org/10.1016/j.bbabio.2019.05.004. Acesso em: 11 out. 2024.
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      Teixeira, M. H., & Arantes, G. M. (2019). Balanced internal hydration discriminates substrate binding to respiratory complex I. Biochimica et Biophysica Acta-Bioenergetics, 1860( 7), 541-548. doi:10.1016/j.bbabio.2019.05.004
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      Teixeira MH, Arantes GM. Balanced internal hydration discriminates substrate binding to respiratory complex I [Internet]. Biochimica et Biophysica Acta-Bioenergetics. 2019 ; 1860( 7): 541-548.[citado 2024 out. 11 ] Available from: https://doi.org/10.1016/j.bbabio.2019.05.004
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      Teixeira MH, Arantes GM. Balanced internal hydration discriminates substrate binding to respiratory complex I [Internet]. Biochimica et Biophysica Acta-Bioenergetics. 2019 ; 1860( 7): 541-548.[citado 2024 out. 11 ] Available from: https://doi.org/10.1016/j.bbabio.2019.05.004
  • Source: Journal of Proteomics. Unidade: IQ

    Subjects: PROTEÍNAS, PROTEÔMICA

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      MONTEIRO, Lucas Falcão e FORTI, Fabio Luis. Network analysis of DUSP12 partners in the nucleus under genotoxic stress. Journal of Proteomics, v. 197, p. 42-52, 2019Tradução . . Disponível em: https://doi.org/10.1016/j.jprot.2019.02.008. Acesso em: 11 out. 2024.
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      Monteiro, L. F., & Forti, F. L. (2019). Network analysis of DUSP12 partners in the nucleus under genotoxic stress. Journal of Proteomics, 197, 42-52. doi:10.1016/j.jprot.2019.02.008
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      Monteiro LF, Forti FL. Network analysis of DUSP12 partners in the nucleus under genotoxic stress [Internet]. Journal of Proteomics. 2019 ; 197 42-52.[citado 2024 out. 11 ] Available from: https://doi.org/10.1016/j.jprot.2019.02.008
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      Monteiro LF, Forti FL. Network analysis of DUSP12 partners in the nucleus under genotoxic stress [Internet]. Journal of Proteomics. 2019 ; 197 42-52.[citado 2024 out. 11 ] Available from: https://doi.org/10.1016/j.jprot.2019.02.008
  • Source: Acta Tropica. Unidades: ICB, IQ, FCF

    Subjects: PARASITOLOGIA, DOENÇA DE CHAGAS, TRYPANOSOMA CRUZI, TRYPANOSOMATIDAE, SEQUENCIAMENTO GENÉTICO, PROTEÍNAS

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      PETRAVICIUS, Pamela Omena et al. Mapping benznidazole resistance in trypanosomatids and exploring evolutionary histories of nitroreductases and ABCG transporter protein sequences. Acta Tropica, v. 200, p. 1-10, 2019Tradução . . Disponível em: https://doi.org/10.1016/j.actatropica.2019.105161. Acesso em: 11 out. 2024.
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      Petravicius, P. O., Martins, A. G. da C., Silva, M. N., Cunha, J. L. R., Bartholomeu, D. C., Teixeira, M. M. G., & Zingales, B. (2019). Mapping benznidazole resistance in trypanosomatids and exploring evolutionary histories of nitroreductases and ABCG transporter protein sequences. Acta Tropica, 200, 1-10. doi:10.1016/j.actatropica.2019.105161
    • NLM

      Petravicius PO, Martins AG da C, Silva MN, Cunha JLR, Bartholomeu DC, Teixeira MMG, Zingales B. Mapping benznidazole resistance in trypanosomatids and exploring evolutionary histories of nitroreductases and ABCG transporter protein sequences [Internet]. Acta Tropica. 2019 ; 200 1-10.[citado 2024 out. 11 ] Available from: https://doi.org/10.1016/j.actatropica.2019.105161
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      Petravicius PO, Martins AG da C, Silva MN, Cunha JLR, Bartholomeu DC, Teixeira MMG, Zingales B. Mapping benznidazole resistance in trypanosomatids and exploring evolutionary histories of nitroreductases and ABCG transporter protein sequences [Internet]. Acta Tropica. 2019 ; 200 1-10.[citado 2024 out. 11 ] Available from: https://doi.org/10.1016/j.actatropica.2019.105161
  • Source: Biochimica et Biophysica Acta: General Subjects. Unidades: IF, IQ, IFSC

    Subjects: RADIAÇÃO SINCROTRON, PROTEÍNAS

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      ORCIA, Débora et al. Interaction of an esophageal MEG protein from schistosomes with a human S100 protein involved in inflammatory response. Biochimica et Biophysica Acta: General Subjects, v. 1861, n. Ja 2017, p. 3490-3497, 2017Tradução . . Disponível em: https://doi.org/10.1016/j.bbagen.2016.09.015. Acesso em: 11 out. 2024.
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      Orcia, D., Zeraik, A. E., Lopes, J. L. de S., Macêdo, J. N. A., Santos, C. R. dos, Oliveira, K. C. de, et al. (2017). Interaction of an esophageal MEG protein from schistosomes with a human S100 protein involved in inflammatory response. Biochimica et Biophysica Acta: General Subjects, 1861( Ja 2017), 3490-3497. doi:10.1016/j.bbagen.2016.09.015
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      Orcia D, Zeraik AE, Lopes JL de S, Macêdo JNA, Santos CR dos, Oliveira KC de, Anderson L, Wallace BA, Verjovski-Almeida S, Araújo APU de, De Marco R. Interaction of an esophageal MEG protein from schistosomes with a human S100 protein involved in inflammatory response [Internet]. Biochimica et Biophysica Acta: General Subjects. 2017 ; 1861( Ja 2017): 3490-3497.[citado 2024 out. 11 ] Available from: https://doi.org/10.1016/j.bbagen.2016.09.015
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      Orcia D, Zeraik AE, Lopes JL de S, Macêdo JNA, Santos CR dos, Oliveira KC de, Anderson L, Wallace BA, Verjovski-Almeida S, Araújo APU de, De Marco R. Interaction of an esophageal MEG protein from schistosomes with a human S100 protein involved in inflammatory response [Internet]. Biochimica et Biophysica Acta: General Subjects. 2017 ; 1861( Ja 2017): 3490-3497.[citado 2024 out. 11 ] Available from: https://doi.org/10.1016/j.bbagen.2016.09.015
  • Source: Emerging trends in applications and infrastructures for computational biology, bioinformatics, and systems biology. Unidade: IQ

    Subjects: ESTRESSE OXIDATIVO, PROTEÍNAS

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      MIOTTO, Ronei et al. Biomembranes under oxidative stress: insights from molecular dynamics simulations. Emerging trends in applications and infrastructures for computational biology, bioinformatics, and systems biology. Tradução . Amsterdam: Elsevier, 2016. . Disponível em: https://doi.org/10.1016/B978-0-12-804203-8.00014-6. Acesso em: 11 out. 2024.
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      Miotto, R., Costa, E. B., Trellese, G. G., Neto, A. J. P., Baptista, M. da S., Ferraz, A. C., & Cordeiro, R. M. (2016). Biomembranes under oxidative stress: insights from molecular dynamics simulations. In Emerging trends in applications and infrastructures for computational biology, bioinformatics, and systems biology. Amsterdam: Elsevier. doi:10.1016/B978-0-12-804203-8.00014-6
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      Miotto R, Costa EB, Trellese GG, Neto AJP, Baptista M da S, Ferraz AC, Cordeiro RM. Biomembranes under oxidative stress: insights from molecular dynamics simulations [Internet]. In: Emerging trends in applications and infrastructures for computational biology, bioinformatics, and systems biology. Amsterdam: Elsevier; 2016. [citado 2024 out. 11 ] Available from: https://doi.org/10.1016/B978-0-12-804203-8.00014-6
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      Miotto R, Costa EB, Trellese GG, Neto AJP, Baptista M da S, Ferraz AC, Cordeiro RM. Biomembranes under oxidative stress: insights from molecular dynamics simulations [Internet]. In: Emerging trends in applications and infrastructures for computational biology, bioinformatics, and systems biology. Amsterdam: Elsevier; 2016. [citado 2024 out. 11 ] Available from: https://doi.org/10.1016/B978-0-12-804203-8.00014-6
  • Source: Journal of Advanced Research. Unidade: IQ

    Subjects: NANOPARTÍCULAS, PROTEÍNAS

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      TERBORG, Lydia et al. Porous polymer monolithic columns with gold nanoparticles as an intermediate ligand for the separation of proteins in reverse phase-ion exchange mixed mode. Journal of Advanced Research, v. 6, n. 3, p. 441-448, 2015Tradução . . Disponível em: https://doi.org/10.1016/j.jare.2014.10.004. Acesso em: 11 out. 2024.
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      Terborg, L., Masini, J. C., Lin, M., Lipponen, K., Riekolla, M. L., & Svec, F. (2015). Porous polymer monolithic columns with gold nanoparticles as an intermediate ligand for the separation of proteins in reverse phase-ion exchange mixed mode. Journal of Advanced Research, 6( 3), 441-448. doi:10.1016/j.jare.2014.10.004
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      Terborg L, Masini JC, Lin M, Lipponen K, Riekolla ML, Svec F. Porous polymer monolithic columns with gold nanoparticles as an intermediate ligand for the separation of proteins in reverse phase-ion exchange mixed mode [Internet]. Journal of Advanced Research. 2015 ; 6( 3): 441-448.[citado 2024 out. 11 ] Available from: https://doi.org/10.1016/j.jare.2014.10.004
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      Terborg L, Masini JC, Lin M, Lipponen K, Riekolla ML, Svec F. Porous polymer monolithic columns with gold nanoparticles as an intermediate ligand for the separation of proteins in reverse phase-ion exchange mixed mode [Internet]. Journal of Advanced Research. 2015 ; 6( 3): 441-448.[citado 2024 out. 11 ] Available from: https://doi.org/10.1016/j.jare.2014.10.004
  • Source: Journal of Proteomics. Unidades: IQ, IFSC

    Subjects: SCHISTOSOMA MANSONI, PROTEÍNAS, GENES (ESTUDO)

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      VERJOVSKI-ALMEIDA, Sergio e DE MARCO, Ricardo. Gene structure and splicing in schistosomes. Journal of Proteomics, v. 74, n. 9, p. 1515-1518, 2011Tradução . . Disponível em: https://doi.org/10.1016/j.jprot.2011.03.022. Acesso em: 11 out. 2024.
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      Verjovski-Almeida, S., & De Marco, R. (2011). Gene structure and splicing in schistosomes. Journal of Proteomics, 74( 9), 1515-1518. doi:10.1016/j.jprot.2011.03.022
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      Verjovski-Almeida S, De Marco R. Gene structure and splicing in schistosomes [Internet]. Journal of Proteomics. 2011 ; 74( 9): 1515-1518.[citado 2024 out. 11 ] Available from: https://doi.org/10.1016/j.jprot.2011.03.022
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      Verjovski-Almeida S, De Marco R. Gene structure and splicing in schistosomes [Internet]. Journal of Proteomics. 2011 ; 74( 9): 1515-1518.[citado 2024 out. 11 ] Available from: https://doi.org/10.1016/j.jprot.2011.03.022
  • Source: Food Chemistry. Unidades: IQ, FCF

    Subjects: PROTEÍNAS, ALGAS MARINHAS, ÁCIDOS GRAXOS, AMINOÁCIDOS

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      GRESSLER, Vanessa et al. Lipid, fatty acid, protein, amino acid and ash contents in four Brazilian red algae species. Food Chemistry, v. 120, n. 2, p. 585-590, 2010Tradução . . Disponível em: https://doi.org/10.1016/j.foodchem.2009.10.028. Acesso em: 11 out. 2024.
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      Gressler, V., Yokoya, N. S., Fujii, M. T., Colepicolo, P., Mancini-Filho, J., Torres, R. P., & Pinto, E. (2010). Lipid, fatty acid, protein, amino acid and ash contents in four Brazilian red algae species. Food Chemistry, 120( 2), 585-590. doi:10.1016/j.foodchem.2009.10.028
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      Gressler V, Yokoya NS, Fujii MT, Colepicolo P, Mancini-Filho J, Torres RP, Pinto E. Lipid, fatty acid, protein, amino acid and ash contents in four Brazilian red algae species [Internet]. Food Chemistry. 2010 ; 120( 2): 585-590.[citado 2024 out. 11 ] Available from: https://doi.org/10.1016/j.foodchem.2009.10.028
    • Vancouver

      Gressler V, Yokoya NS, Fujii MT, Colepicolo P, Mancini-Filho J, Torres RP, Pinto E. Lipid, fatty acid, protein, amino acid and ash contents in four Brazilian red algae species [Internet]. Food Chemistry. 2010 ; 120( 2): 585-590.[citado 2024 out. 11 ] Available from: https://doi.org/10.1016/j.foodchem.2009.10.028
  • Source: Regulatory Peptides. Unidades: FM, IQ

    Subjects: PROTEÍNAS, PEPTÍDEOS

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      COSTA-JUNIOR, Helio Miranda et al. Specific modulation of protein kinase activity via small peptides. Regulatory Peptides, v. 153, n. 1-3, p. 11-18, 2009Tradução . . Disponível em: https://doi.org/10.1016/j.regpep.2008.12.002. Acesso em: 11 out. 2024.
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      Costa-Junior, H. M., Suetsugu, M. J., Krieger, J. E., & Schechtman, D. (2009). Specific modulation of protein kinase activity via small peptides. Regulatory Peptides, 153( 1-3), 11-18. doi:10.1016/j.regpep.2008.12.002
    • NLM

      Costa-Junior HM, Suetsugu MJ, Krieger JE, Schechtman D. Specific modulation of protein kinase activity via small peptides [Internet]. Regulatory Peptides. 2009 ; 153( 1-3): 11-18.[citado 2024 out. 11 ] Available from: https://doi.org/10.1016/j.regpep.2008.12.002
    • Vancouver

      Costa-Junior HM, Suetsugu MJ, Krieger JE, Schechtman D. Specific modulation of protein kinase activity via small peptides [Internet]. Regulatory Peptides. 2009 ; 153( 1-3): 11-18.[citado 2024 out. 11 ] Available from: https://doi.org/10.1016/j.regpep.2008.12.002
  • Source: International Journal of Pharmaceutics. Unidade: IQ

    Subjects: BIOQUÍMICA, PROTEÍNAS

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      NAMUR, Jocimara Ambrosio de Moraes et al. Lactic acid triggers, in vitro, thiomersal to degrade protein in the presence of PLGA microspheres. International Journal of Pharmaceutics, v. 273, n. 1-2, p. 1-8, 2004Tradução . . Disponível em: https://doi.org/10.1016/j.ijpharm.2003.12.003. Acesso em: 11 out. 2024.
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      Namur, J. A. de M., Takata, C. S., Moro, A. M., Politi, M. J., De Araujo, P. S., Cuccovia, I. M., & Bueno da Costa, M. H. (2004). Lactic acid triggers, in vitro, thiomersal to degrade protein in the presence of PLGA microspheres. International Journal of Pharmaceutics, 273( 1-2), 1-8. doi:10.1016/j.ijpharm.2003.12.003
    • NLM

      Namur JA de M, Takata CS, Moro AM, Politi MJ, De Araujo PS, Cuccovia IM, Bueno da Costa MH. Lactic acid triggers, in vitro, thiomersal to degrade protein in the presence of PLGA microspheres [Internet]. International Journal of Pharmaceutics. 2004 ; 273( 1-2): 1-8.[citado 2024 out. 11 ] Available from: https://doi.org/10.1016/j.ijpharm.2003.12.003
    • Vancouver

      Namur JA de M, Takata CS, Moro AM, Politi MJ, De Araujo PS, Cuccovia IM, Bueno da Costa MH. Lactic acid triggers, in vitro, thiomersal to degrade protein in the presence of PLGA microspheres [Internet]. International Journal of Pharmaceutics. 2004 ; 273( 1-2): 1-8.[citado 2024 out. 11 ] Available from: https://doi.org/10.1016/j.ijpharm.2003.12.003
  • Source: Biochimica et Biophysica Acta. Conference titles: European Bioenergetics Conference. Unidade: IQ

    Subjects: MITOCÔNDRIAS, PROTEÍNAS, BIOQUÍMICA

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      JEZEK, Petr et al. Feedback regulation of oxidative stress: fatty acid hydroperoxides are cycling substrates of mitochondrial uncoupling protein UCP2. Biochimica et Biophysica Acta. Amsterdam: Instituto de Química, Universidade de São Paulo. . Acesso em: 11 out. 2024. , 2004
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      Jezek, P., Miyamoto, S., Di Mascio, P., Garlid, K. D., & Jaburek, M. (2004). Feedback regulation of oxidative stress: fatty acid hydroperoxides are cycling substrates of mitochondrial uncoupling protein UCP2. Biochimica et Biophysica Acta. Amsterdam: Instituto de Química, Universidade de São Paulo.
    • NLM

      Jezek P, Miyamoto S, Di Mascio P, Garlid KD, Jaburek M. Feedback regulation of oxidative stress: fatty acid hydroperoxides are cycling substrates of mitochondrial uncoupling protein UCP2. Biochimica et Biophysica Acta. 2004 ; 1658 56.[citado 2024 out. 11 ]
    • Vancouver

      Jezek P, Miyamoto S, Di Mascio P, Garlid KD, Jaburek M. Feedback regulation of oxidative stress: fatty acid hydroperoxides are cycling substrates of mitochondrial uncoupling protein UCP2. Biochimica et Biophysica Acta. 2004 ; 1658 56.[citado 2024 out. 11 ]
  • Source: Current Cancer Drug Targets. Unidade: IQ

    Subjects: OLIGONUCLEOTÍDEOS, PEPTÍDEOS, PROTEÍNAS, BIOQUÍMICA

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      FARIA, M. e ULRICH, Henning. The use of synthetic oligonucleotides as protein inhibitors and anticode drugs in cancer therapy: accomplishments and limitations. Current Cancer Drug Targets, v. 2, n. 4, p. 355-368, 2002Tradução . . Acesso em: 11 out. 2024.
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      Faria, M., & Ulrich, H. (2002). The use of synthetic oligonucleotides as protein inhibitors and anticode drugs in cancer therapy: accomplishments and limitations. Current Cancer Drug Targets, 2( 4), 355-368.
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      Faria M, Ulrich H. The use of synthetic oligonucleotides as protein inhibitors and anticode drugs in cancer therapy: accomplishments and limitations. Current Cancer Drug Targets. 2002 ; 2( 4): 355-368.[citado 2024 out. 11 ]
    • Vancouver

      Faria M, Ulrich H. The use of synthetic oligonucleotides as protein inhibitors and anticode drugs in cancer therapy: accomplishments and limitations. Current Cancer Drug Targets. 2002 ; 2( 4): 355-368.[citado 2024 out. 11 ]
  • Source: Journal of Molecular Structure. Unidade: IQ

    Subjects: PROTEÍNAS, ENZIMAS, DIFRAÇÃO POR RAIOS X

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      DELBONI, Luis Fernando et al. Applications of thermal-gradients method for the optimization of alpha-amylase crystallization conditions based on dynamic and static light scattering data. Journal of Molecular Structure, v. 604, n. 2-3, p. 87-99, 2002Tradução . . Disponível em: https://doi.org/10.1016/s0022-2860(01)00663-9. Acesso em: 11 out. 2024.
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      Delboni, L. F., Iulek, J., Burger, R., Silva, A. C. R. da, & Moreno, A. (2002). Applications of thermal-gradients method for the optimization of alpha-amylase crystallization conditions based on dynamic and static light scattering data. Journal of Molecular Structure, 604( 2-3), 87-99. doi:10.1016/s0022-2860(01)00663-9
    • NLM

      Delboni LF, Iulek J, Burger R, Silva ACR da, Moreno A. Applications of thermal-gradients method for the optimization of alpha-amylase crystallization conditions based on dynamic and static light scattering data [Internet]. Journal of Molecular Structure. 2002 ; 604( 2-3): 87-99.[citado 2024 out. 11 ] Available from: https://doi.org/10.1016/s0022-2860(01)00663-9
    • Vancouver

      Delboni LF, Iulek J, Burger R, Silva ACR da, Moreno A. Applications of thermal-gradients method for the optimization of alpha-amylase crystallization conditions based on dynamic and static light scattering data [Internet]. Journal of Molecular Structure. 2002 ; 604( 2-3): 87-99.[citado 2024 out. 11 ] Available from: https://doi.org/10.1016/s0022-2860(01)00663-9

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