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  • Source: Journal of Power Sources. Unidade: IQSC

    Subjects: ENZIMAS, ELETRODO

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      SEDENHO, Graziela Cristina et al. Stabilization of bilirubin oxidase in a biogel matrix for high-performance gas diffusion electrodes. Journal of Power Sources, v. 482, n. ja 2021, p. 229035, 2021Tradução . . Disponível em: https://doi.org/10.1016/j.jpowsour.2020.229035. Acesso em: 01 out. 2024.
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      Sedenho, G. C., Hassan, A., Macedo, L. J. A. de, & Crespilho, F. N. (2021). Stabilization of bilirubin oxidase in a biogel matrix for high-performance gas diffusion electrodes. Journal of Power Sources, 482(ja 2021), 229035. doi:10.1016/j.jpowsour.2020.229035
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      Sedenho GC, Hassan A, Macedo LJA de, Crespilho FN. Stabilization of bilirubin oxidase in a biogel matrix for high-performance gas diffusion electrodes [Internet]. Journal of Power Sources. 2021 ; 482(ja 2021): 229035.[citado 2024 out. 01 ] Available from: https://doi.org/10.1016/j.jpowsour.2020.229035
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      Sedenho GC, Hassan A, Macedo LJA de, Crespilho FN. Stabilization of bilirubin oxidase in a biogel matrix for high-performance gas diffusion electrodes [Internet]. Journal of Power Sources. 2021 ; 482(ja 2021): 229035.[citado 2024 out. 01 ] Available from: https://doi.org/10.1016/j.jpowsour.2020.229035
  • Source: Chemical Communications - ChemComm. Unidade: IQSC

    Subjects: ENZIMAS, ESPECTROMETRIA DE MASSAS, ELETROQUÍMICA

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      SOUZA, João Carlos Perbone de et al. Enzyme activity evaluation by differential electrochemical mass spectrometry. Chemical Communications - ChemComm, v. 53, n. 60, p. 8400-8402, 2017Tradução . . Disponível em: https://doi.org/10.1039/c7cc03963. Acesso em: 01 out. 2024.
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      Souza, J. C. P. de, Silva, W. O., Lima, F. H. B. de, & Crespilho, F. N. (2017). Enzyme activity evaluation by differential electrochemical mass spectrometry. Chemical Communications - ChemComm, 53( 60), 8400-8402. doi:10.1039/c7cc03963
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      Souza JCP de, Silva WO, Lima FHB de, Crespilho FN. Enzyme activity evaluation by differential electrochemical mass spectrometry [Internet]. Chemical Communications - ChemComm. 2017 ; 53( 60): 8400-8402.[citado 2024 out. 01 ] Available from: https://doi.org/10.1039/c7cc03963
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      Souza JCP de, Silva WO, Lima FHB de, Crespilho FN. Enzyme activity evaluation by differential electrochemical mass spectrometry [Internet]. Chemical Communications - ChemComm. 2017 ; 53( 60): 8400-8402.[citado 2024 out. 01 ] Available from: https://doi.org/10.1039/c7cc03963
  • Source: Molecular Biotechnology. Unidade: FCFRP

    Subjects: ETANOL, TRICHODERMA, BIOCOMBUSTÍVEIS, ENZIMAS, EXPRESSÃO GÊNICA

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      COLABARDINI, Ana C. et al. Expression of two novel β-glucosidases from Chaetomium atrobrunneum in Trichoderma reesei and characterization of the heterologous protein products. Molecular Biotechnology, v. 58, n. 12, p. 821-831, 2016Tradução . . Disponível em: https://doi.org/10.1007/s12033-016-9981-7. Acesso em: 01 out. 2024.
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      Colabardini, A. C., Valkonen, M., Huuskonen, A., Siika-aho, M., Koivula, A., Goldman, G. H., & Saloheimo, M. (2016). Expression of two novel β-glucosidases from Chaetomium atrobrunneum in Trichoderma reesei and characterization of the heterologous protein products. Molecular Biotechnology, 58( 12), 821-831. doi:10.1007/s12033-016-9981-7
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      Colabardini AC, Valkonen M, Huuskonen A, Siika-aho M, Koivula A, Goldman GH, Saloheimo M. Expression of two novel β-glucosidases from Chaetomium atrobrunneum in Trichoderma reesei and characterization of the heterologous protein products [Internet]. Molecular Biotechnology. 2016 ; 58( 12): 821-831.[citado 2024 out. 01 ] Available from: https://doi.org/10.1007/s12033-016-9981-7
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      Colabardini AC, Valkonen M, Huuskonen A, Siika-aho M, Koivula A, Goldman GH, Saloheimo M. Expression of two novel β-glucosidases from Chaetomium atrobrunneum in Trichoderma reesei and characterization of the heterologous protein products [Internet]. Molecular Biotechnology. 2016 ; 58( 12): 821-831.[citado 2024 out. 01 ] Available from: https://doi.org/10.1007/s12033-016-9981-7
  • Source: Preparative Biochemistry and Biotechnology. Unidade: FCFRP

    Subjects: ASPERGILLUS, FÁRMACOS, FUNGOS, PROTEÍNAS, ENZIMAS

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      BIAGGIO, Rafael Tage et al. Purification and biochemical characterization of an extracellular serine peptidase from Aspergillus terreus. Preparative Biochemistry and Biotechnology, v. 46, n. 3, p. 298-304, 2016Tradução . . Disponível em: https://doi.org/10.1080/10826068.2015.1031387. Acesso em: 01 out. 2024.
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      Biaggio, R. T., Silva, R. R. da, Rosa, N. G. da, Leite, R. S. R., Arantes, E. C., Cabral, T. P. de F., et al. (2016). Purification and biochemical characterization of an extracellular serine peptidase from Aspergillus terreus. Preparative Biochemistry and Biotechnology, 46( 3), 298-304. doi:10.1080/10826068.2015.1031387
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      Biaggio RT, Silva RR da, Rosa NG da, Leite RSR, Arantes EC, Cabral TP de F, Juliano MA, Juliano L, Cabral H. Purification and biochemical characterization of an extracellular serine peptidase from Aspergillus terreus [Internet]. Preparative Biochemistry and Biotechnology. 2016 ; 46( 3): 298-304.[citado 2024 out. 01 ] Available from: https://doi.org/10.1080/10826068.2015.1031387
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      Biaggio RT, Silva RR da, Rosa NG da, Leite RSR, Arantes EC, Cabral TP de F, Juliano MA, Juliano L, Cabral H. Purification and biochemical characterization of an extracellular serine peptidase from Aspergillus terreus [Internet]. Preparative Biochemistry and Biotechnology. 2016 ; 46( 3): 298-304.[citado 2024 out. 01 ] Available from: https://doi.org/10.1080/10826068.2015.1031387
  • Source: Biotechnology Advances. Unidades: IQ, IQSC

    Subjects: QUÍMICA, ENZIMAS

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      BIROLLI, Willian Garcia et al. Biocatalysis and biotransformation in Brazil: an overview. Biotechnology Advances, v. 33, p. 481-510, 2015Tradução . . Disponível em: https://doi.org/10.1016/j.biotechadv.2015.02.001. Acesso em: 01 out. 2024.
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      Birolli, W. G., Ferreira , I. M., Alvarenga, N., Matos, I. L. de, Comasseto, J. V., & Porto, A. L. M. (2015). Biocatalysis and biotransformation in Brazil: an overview. Biotechnology Advances, 33, 481-510. doi:10.1016/j.biotechadv.2015.02.001
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      Birolli WG, Ferreira IM, Alvarenga N, Matos IL de, Comasseto JV, Porto ALM. Biocatalysis and biotransformation in Brazil: an overview [Internet]. Biotechnology Advances. 2015 ; 33 481-510.[citado 2024 out. 01 ] Available from: https://doi.org/10.1016/j.biotechadv.2015.02.001
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      Birolli WG, Ferreira IM, Alvarenga N, Matos IL de, Comasseto JV, Porto ALM. Biocatalysis and biotransformation in Brazil: an overview [Internet]. Biotechnology Advances. 2015 ; 33 481-510.[citado 2024 out. 01 ] Available from: https://doi.org/10.1016/j.biotechadv.2015.02.001
  • Source: The Journal of Physical Chemistry Part B. Unidade: FFCLRP

    Subjects: FÁRMACOS, ANTINEOPLÁSICOS, ESPECTROSCOPIA, ENZIMAS

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      VICENTE, Eduardo F et al. Conformational changes of the HsDHODH N-terminal Microdomain via DEER Spectroscopy. The Journal of Physical Chemistry Part B, v. 119, n. 28, p. 8693-8697, 2015Tradução . . Disponível em: https://doi.org/10.1021/acs.jpcb.5b01706. Acesso em: 01 out. 2024.
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      Vicente, E. F., Sahu, I. D., Costa Filho, A. J. da, Cilli, E. M., & Lorigan, G. A. (2015). Conformational changes of the HsDHODH N-terminal Microdomain via DEER Spectroscopy. The Journal of Physical Chemistry Part B, 119( 28), 8693-8697. doi:10.1021/acs.jpcb.5b01706
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      Vicente EF, Sahu ID, Costa Filho AJ da, Cilli EM, Lorigan GA. Conformational changes of the HsDHODH N-terminal Microdomain via DEER Spectroscopy [Internet]. The Journal of Physical Chemistry Part B. 2015 ; 119( 28): 8693-8697.[citado 2024 out. 01 ] Available from: https://doi.org/10.1021/acs.jpcb.5b01706
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      Vicente EF, Sahu ID, Costa Filho AJ da, Cilli EM, Lorigan GA. Conformational changes of the HsDHODH N-terminal Microdomain via DEER Spectroscopy [Internet]. The Journal of Physical Chemistry Part B. 2015 ; 119( 28): 8693-8697.[citado 2024 out. 01 ] Available from: https://doi.org/10.1021/acs.jpcb.5b01706
  • Source: Journal of Molecular Catalysis B: Enzymatic. Unidade: IQSC

    Subjects: QUÍMICA, ENZIMAS

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      FERREIRA, Irlon Maciel et al. Chemoselective biohydrogenation of α,β- and α,β,γ,δ-unsaturated ketones by the marine-derived fungus Penicillium citrinum CBMAI 1186 in a biphasic system. Journal of Molecular Catalysis B: Enzymatic, v. 115, n. 1, p. 59-65, 2015Tradução . . Disponível em: https://doi.org/10.1016/j.molcatb.2015.01.017. Acesso em: 01 out. 2024.
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      Ferreira, I. M., Meira, E. B., Rosset, I. G., & Porto, A. L. M. (2015). Chemoselective biohydrogenation of α,β- and α,β,γ,δ-unsaturated ketones by the marine-derived fungus Penicillium citrinum CBMAI 1186 in a biphasic system. Journal of Molecular Catalysis B: Enzymatic, 115( 1), 59-65. doi:10.1016/j.molcatb.2015.01.017
    • NLM

      Ferreira IM, Meira EB, Rosset IG, Porto ALM. Chemoselective biohydrogenation of α,β- and α,β,γ,δ-unsaturated ketones by the marine-derived fungus Penicillium citrinum CBMAI 1186 in a biphasic system [Internet]. Journal of Molecular Catalysis B: Enzymatic. 2015 ; 115( 1): 59-65.[citado 2024 out. 01 ] Available from: https://doi.org/10.1016/j.molcatb.2015.01.017
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      Ferreira IM, Meira EB, Rosset IG, Porto ALM. Chemoselective biohydrogenation of α,β- and α,β,γ,δ-unsaturated ketones by the marine-derived fungus Penicillium citrinum CBMAI 1186 in a biphasic system [Internet]. Journal of Molecular Catalysis B: Enzymatic. 2015 ; 115( 1): 59-65.[citado 2024 out. 01 ] Available from: https://doi.org/10.1016/j.molcatb.2015.01.017
  • Source: European Journal Pharmacology. Unidades: FCFRP, FORP

    Subjects: ARTERIOSCLEROSE, ENZIMAS, RECEPTORES DE ANGIOTENSINA, FÁRMACOS

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      PERNOMIAN, Larissa et al. MAS receptors mediate vasoprotective and atheroprotective effects of candesartan upon the recovery of vascular angiotensin-converting enzyme 2–angiotensin-(1-7)–MAS axis functionality. European Journal Pharmacology, v. 764, p. 173-188, 2015Tradução . . Disponível em: https://doi.org/10.1016/j.ejphar.2015.07.007. Acesso em: 01 out. 2024.
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      Pernomian, L., Prado, A. F. do, Gomes, M. S., Pernomian, L., Silva, C. H. T. de P. da, Gerlach, R. F., & Oliveira, A. M. de. (2015). MAS receptors mediate vasoprotective and atheroprotective effects of candesartan upon the recovery of vascular angiotensin-converting enzyme 2–angiotensin-(1-7)–MAS axis functionality. European Journal Pharmacology, 764, 173-188. doi:10.1016/j.ejphar.2015.07.007
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      Pernomian L, Prado AF do, Gomes MS, Pernomian L, Silva CHT de P da, Gerlach RF, Oliveira AM de. MAS receptors mediate vasoprotective and atheroprotective effects of candesartan upon the recovery of vascular angiotensin-converting enzyme 2–angiotensin-(1-7)–MAS axis functionality [Internet]. European Journal Pharmacology. 2015 ; 764 173-188.[citado 2024 out. 01 ] Available from: https://doi.org/10.1016/j.ejphar.2015.07.007
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      Pernomian L, Prado AF do, Gomes MS, Pernomian L, Silva CHT de P da, Gerlach RF, Oliveira AM de. MAS receptors mediate vasoprotective and atheroprotective effects of candesartan upon the recovery of vascular angiotensin-converting enzyme 2–angiotensin-(1-7)–MAS axis functionality [Internet]. European Journal Pharmacology. 2015 ; 764 173-188.[citado 2024 out. 01 ] Available from: https://doi.org/10.1016/j.ejphar.2015.07.007
  • Source: Tetrahedron Letters. Unidades: FCFRP, IQSC

    Subjects: ENZIMAS, QUÍMICA ORGÂNICA

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      FERREIRA , Irlon Maciel et al. Highly enantioselective acylation of chlorohydrins using Amano AK lipase from P. fluorescens immobilized on silk fibroin–alginate spheres. Tetrahedron Letters, v. 55, n. 7, p. 5062-5065, 2014Tradução . . Disponível em: https://doi.org/10.1016/j.tetlet.2014.07.032. Acesso em: 01 out. 2024.
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      Ferreira , I. M., Nishimura, R. H. V., Souza, A. B. dos A., Clososki, G. C., Yoshioka, S. A., & Porto, A. L. M. (2014). Highly enantioselective acylation of chlorohydrins using Amano AK lipase from P. fluorescens immobilized on silk fibroin–alginate spheres. Tetrahedron Letters, 55( 7), 5062-5065. doi:10.1016/j.tetlet.2014.07.032
    • NLM

      Ferreira IM, Nishimura RHV, Souza AB dos A, Clososki GC, Yoshioka SA, Porto ALM. Highly enantioselective acylation of chlorohydrins using Amano AK lipase from P. fluorescens immobilized on silk fibroin–alginate spheres [Internet]. Tetrahedron Letters. 2014 ; 55( 7): 5062-5065.[citado 2024 out. 01 ] Available from: https://doi.org/10.1016/j.tetlet.2014.07.032
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      Ferreira IM, Nishimura RHV, Souza AB dos A, Clososki GC, Yoshioka SA, Porto ALM. Highly enantioselective acylation of chlorohydrins using Amano AK lipase from P. fluorescens immobilized on silk fibroin–alginate spheres [Internet]. Tetrahedron Letters. 2014 ; 55( 7): 5062-5065.[citado 2024 out. 01 ] Available from: https://doi.org/10.1016/j.tetlet.2014.07.032
  • Source: Electrochimica Acta. Unidade: FFCLRP

    Subjects: CÉLULAS A COMBUSTÍVEL, ENZIMAS, ELETROQUÍMICA

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      CREPALDI, L. B. et al. Ferrocene entrapped In polypyrrole film and PAMAM dendrimers as matrix for mediated glucose/O2 biofuel cell. Electrochimica Acta, v. 136, p. 52-58, 2014Tradução . . Disponível em: https://doi.org/10.1016/j.electacta.2014.05.049. Acesso em: 01 out. 2024.
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      Crepaldi, L. B., Aquino Neto, S., Cardoso, F. P., Ciancaglini, P., & Andrade, A. R. de. (2014). Ferrocene entrapped In polypyrrole film and PAMAM dendrimers as matrix for mediated glucose/O2 biofuel cell. Electrochimica Acta, 136, 52-58. doi:10.1016/j.electacta.2014.05.049
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      Crepaldi LB, Aquino Neto S, Cardoso FP, Ciancaglini P, Andrade AR de. Ferrocene entrapped In polypyrrole film and PAMAM dendrimers as matrix for mediated glucose/O2 biofuel cell [Internet]. Electrochimica Acta. 2014 ; 136 52-58.[citado 2024 out. 01 ] Available from: https://doi.org/10.1016/j.electacta.2014.05.049
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      Crepaldi LB, Aquino Neto S, Cardoso FP, Ciancaglini P, Andrade AR de. Ferrocene entrapped In polypyrrole film and PAMAM dendrimers as matrix for mediated glucose/O2 biofuel cell [Internet]. Electrochimica Acta. 2014 ; 136 52-58.[citado 2024 out. 01 ] Available from: https://doi.org/10.1016/j.electacta.2014.05.049
  • Source: Brazilian Archives of Biology and Technology. Unidade: FFCLRP

    Subjects: SOLOS (COLETA), PLANTAS (COLETA), RESÍDUOS AGRÍCOLAS, FUNGOS, ENZIMAS

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      DAMÁSIO, André Ricardo de Lima et al. Biotechnological potential of alternative carbon sources for production of pectinases by Rhizopus microsporus var. rhizopodiformis. Brazilian Archives of Biology and Technology, v. 54, n. 1, p. 141-148, 2011Tradução . . Disponível em: https://doi.org/10.1590/s1516-89132011000100019. Acesso em: 01 out. 2024.
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      Damásio, A. R. de L., Maller, A., Silva, T. M. da, Jorge, J. A., Terenzi, H. F., & Polizeli, M. de L. T. de M. (2011). Biotechnological potential of alternative carbon sources for production of pectinases by Rhizopus microsporus var. rhizopodiformis. Brazilian Archives of Biology and Technology, 54( 1), 141-148. doi:10.1590/s1516-89132011000100019
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      Damásio AR de L, Maller A, Silva TM da, Jorge JA, Terenzi HF, Polizeli M de LT de M. Biotechnological potential of alternative carbon sources for production of pectinases by Rhizopus microsporus var. rhizopodiformis [Internet]. Brazilian Archives of Biology and Technology. 2011 ; 54( 1): 141-148.[citado 2024 out. 01 ] Available from: https://doi.org/10.1590/s1516-89132011000100019
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      Damásio AR de L, Maller A, Silva TM da, Jorge JA, Terenzi HF, Polizeli M de LT de M. Biotechnological potential of alternative carbon sources for production of pectinases by Rhizopus microsporus var. rhizopodiformis [Internet]. Brazilian Archives of Biology and Technology. 2011 ; 54( 1): 141-148.[citado 2024 out. 01 ] Available from: https://doi.org/10.1590/s1516-89132011000100019
  • Source: Biophysical Chemistry. Unidade: FFCLRP

    Subjects: ENZIMAS, PROTEÍNAS, ESPECTROSCOPIA

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      RIGOS, Carolina Fortes et al. Cytoplasmatic domain of Na,K-ATPase 'alfa'-subunit is responsible for the aggregation of the enzyme in proteoliposomes. Biophysical Chemistry, v. 146, n. 1, p. 36-41, 2010Tradução . . Disponível em: https://doi.org/10.1016/j.bpc.2009.10.002. Acesso em: 01 out. 2024.
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      Rigos, C. F., Santos, H. de L., Yoneda, J. S., Montich, G., Maggio, B., & Ciancaglini, P. (2010). Cytoplasmatic domain of Na,K-ATPase 'alfa'-subunit is responsible for the aggregation of the enzyme in proteoliposomes. Biophysical Chemistry, 146( 1), 36-41. doi:10.1016/j.bpc.2009.10.002
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      Rigos CF, Santos H de L, Yoneda JS, Montich G, Maggio B, Ciancaglini P. Cytoplasmatic domain of Na,K-ATPase 'alfa'-subunit is responsible for the aggregation of the enzyme in proteoliposomes [Internet]. Biophysical Chemistry. 2010 ; 146( 1): 36-41.[citado 2024 out. 01 ] Available from: https://doi.org/10.1016/j.bpc.2009.10.002
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      Rigos CF, Santos H de L, Yoneda JS, Montich G, Maggio B, Ciancaglini P. Cytoplasmatic domain of Na,K-ATPase 'alfa'-subunit is responsible for the aggregation of the enzyme in proteoliposomes [Internet]. Biophysical Chemistry. 2010 ; 146( 1): 36-41.[citado 2024 out. 01 ] Available from: https://doi.org/10.1016/j.bpc.2009.10.002
  • Source: Journal of the Iranian Chemical Society. Unidade: IQSC

    Subjects: LIPASE, ENZIMAS

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      FERREIRA, H V et al. Enzymatic resolution of racemic sulcatol by lipase from candida antarctica in a large scale. Journal of the Iranian Chemical Society, v. 7, n. 4, p. 883-889, 2010Tradução . . Disponível em: https://doi.org/10.1007/bf03246083. Acesso em: 01 out. 2024.
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      Ferreira, H. V., Rocha, L. C., Severino, R. P., Silva, A. B. F. da, & Porto, A. L. M. (2010). Enzymatic resolution of racemic sulcatol by lipase from candida antarctica in a large scale. Journal of the Iranian Chemical Society, 7( 4), 883-889. doi:10.1007/bf03246083
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      Ferreira HV, Rocha LC, Severino RP, Silva ABF da, Porto ALM. Enzymatic resolution of racemic sulcatol by lipase from candida antarctica in a large scale [Internet]. Journal of the Iranian Chemical Society. 2010 ; 7( 4): 883-889.[citado 2024 out. 01 ] Available from: https://doi.org/10.1007/bf03246083
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      Ferreira HV, Rocha LC, Severino RP, Silva ABF da, Porto ALM. Enzymatic resolution of racemic sulcatol by lipase from candida antarctica in a large scale [Internet]. Journal of the Iranian Chemical Society. 2010 ; 7( 4): 883-889.[citado 2024 out. 01 ] Available from: https://doi.org/10.1007/bf03246083
  • Source: Journal of Physical Chemistry Part B. Unidades: FFCLRP, IF

    Assunto: ENZIMAS

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      BARBOSA, Leandro Ramos Souza et al. Unraveling the NA,K-ATPase ‘alpha’4 subunit assembling induced by large amounts of 'C IND.12' 'E IND.8' by means of small-angle X-ray scattering. Journal of Physical Chemistry Part B, v. 114, n. 35, p. 11371-11376, 2010Tradução . . Disponível em: http://pubs.acs.org/doi/pdf/10.1021/jp1013829. Acesso em: 01 out. 2024.
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      Barbosa, L. R. S., Rigos, C. F., Yoneda, J. S., Itri, R., & Ciancaglini, P. (2010). Unraveling the NA,K-ATPase ‘alpha’4 subunit assembling induced by large amounts of 'C IND.12' 'E IND.8' by means of small-angle X-ray scattering. Journal of Physical Chemistry Part B, 114( 35), 11371-11376. Recuperado de http://pubs.acs.org/doi/pdf/10.1021/jp1013829
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      Barbosa LRS, Rigos CF, Yoneda JS, Itri R, Ciancaglini P. Unraveling the NA,K-ATPase ‘alpha’4 subunit assembling induced by large amounts of 'C IND.12' 'E IND.8' by means of small-angle X-ray scattering [Internet]. Journal of Physical Chemistry Part B. 2010 ; 114( 35): 11371-11376.[citado 2024 out. 01 ] Available from: http://pubs.acs.org/doi/pdf/10.1021/jp1013829
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      Barbosa LRS, Rigos CF, Yoneda JS, Itri R, Ciancaglini P. Unraveling the NA,K-ATPase ‘alpha’4 subunit assembling induced by large amounts of 'C IND.12' 'E IND.8' by means of small-angle X-ray scattering [Internet]. Journal of Physical Chemistry Part B. 2010 ; 114( 35): 11371-11376.[citado 2024 out. 01 ] Available from: http://pubs.acs.org/doi/pdf/10.1021/jp1013829
  • Source: European Journal of Inorganic Chemistry. Unidades: IQSC, IF, IQ

    Subjects: RESSONÂNCIA PARAMAGNÉTICA DE SPIN, HIDROGÊNIO, ENZIMAS, FÍSICA DA MATÉRIA CONDENSADA, ELETROQUÍMICA, SENSOR

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      ALVES, Wendel A. et al. A chloro-bridged linear chain imine-copper(II) complex and its application as an enzyme-free amperometric biosensor for hydrogen peroxide. European Journal of Inorganic Chemistry, v. 15, p. 2219-2228, 2009Tradução . . Acesso em: 01 out. 2024.
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      Alves, W. A., Matos, I. O., Takahashi, P. M., Bastos, E. L., Martinho, H., Ferreira, J. G., et al. (2009). A chloro-bridged linear chain imine-copper(II) complex and its application as an enzyme-free amperometric biosensor for hydrogen peroxide. European Journal of Inorganic Chemistry, 15, 2219-2228.
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      Alves WA, Matos IO, Takahashi PM, Bastos EL, Martinho H, Ferreira JG, Silva CC, Santos RH de A, Paduan-Filho A, Ferreira AM da C. A chloro-bridged linear chain imine-copper(II) complex and its application as an enzyme-free amperometric biosensor for hydrogen peroxide. European Journal of Inorganic Chemistry. 2009 ; 15 2219-2228.[citado 2024 out. 01 ]
    • Vancouver

      Alves WA, Matos IO, Takahashi PM, Bastos EL, Martinho H, Ferreira JG, Silva CC, Santos RH de A, Paduan-Filho A, Ferreira AM da C. A chloro-bridged linear chain imine-copper(II) complex and its application as an enzyme-free amperometric biosensor for hydrogen peroxide. European Journal of Inorganic Chemistry. 2009 ; 15 2219-2228.[citado 2024 out. 01 ]
  • Source: Insect Biochemistry and Molecular Biology. Unidade: IQ

    Subjects: COLEOPTERA, DIGESTÃO ANIMAL, ENZIMAS

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      GENTA, Fernando Ariel et al. Purification, characterization and sequencing of the major 'beta'-1,3-glucanase from the midgut of Tenebrio molitor larvae. Insect Biochemistry and Molecular Biology, v. 39, n. 12, p. 861-874, 2009Tradução . . Disponível em: https://doi.org/10.1016/j.ibmb.2009.10.003. Acesso em: 01 out. 2024.
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      Genta, F. A., Bragatto, I., Terra, W. R., & Ferreira, C. (2009). Purification, characterization and sequencing of the major 'beta'-1,3-glucanase from the midgut of Tenebrio molitor larvae. Insect Biochemistry and Molecular Biology, 39( 12), 861-874. doi:10.1016/j.ibmb.2009.10.003
    • NLM

      Genta FA, Bragatto I, Terra WR, Ferreira C. Purification, characterization and sequencing of the major 'beta'-1,3-glucanase from the midgut of Tenebrio molitor larvae [Internet]. Insect Biochemistry and Molecular Biology. 2009 ; 39( 12): 861-874.[citado 2024 out. 01 ] Available from: https://doi.org/10.1016/j.ibmb.2009.10.003
    • Vancouver

      Genta FA, Bragatto I, Terra WR, Ferreira C. Purification, characterization and sequencing of the major 'beta'-1,3-glucanase from the midgut of Tenebrio molitor larvae [Internet]. Insect Biochemistry and Molecular Biology. 2009 ; 39( 12): 861-874.[citado 2024 out. 01 ] Available from: https://doi.org/10.1016/j.ibmb.2009.10.003
  • Source: Protein Expression and Purification. Unidades: FFCLRP, IQ

    Subjects: ESCHERICHIA COLI, ENZIMAS

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      ALMEIDA, Fabiana Maria de et al. Heterologous expression in Escherichia coli of Neurospora crassa neutral trehalase as an active enzyme. Protein Expression and Purification, v. 65, n. 2, p. 185-189, 2009Tradução . . Disponível em: https://doi.org/10.1016/j.pep.2008.11.010. Acesso em: 01 out. 2024.
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      Almeida, F. M. de, Bonini, B. M., Beton, D., Jorge, J. A., Terenzi, H. F., & Da Silva, A. M. (2009). Heterologous expression in Escherichia coli of Neurospora crassa neutral trehalase as an active enzyme. Protein Expression and Purification, 65( 2), 185-189. doi:10.1016/j.pep.2008.11.010
    • NLM

      Almeida FM de, Bonini BM, Beton D, Jorge JA, Terenzi HF, Da Silva AM. Heterologous expression in Escherichia coli of Neurospora crassa neutral trehalase as an active enzyme [Internet]. Protein Expression and Purification. 2009 ; 65( 2): 185-189.[citado 2024 out. 01 ] Available from: https://doi.org/10.1016/j.pep.2008.11.010
    • Vancouver

      Almeida FM de, Bonini BM, Beton D, Jorge JA, Terenzi HF, Da Silva AM. Heterologous expression in Escherichia coli of Neurospora crassa neutral trehalase as an active enzyme [Internet]. Protein Expression and Purification. 2009 ; 65( 2): 185-189.[citado 2024 out. 01 ] Available from: https://doi.org/10.1016/j.pep.2008.11.010
  • Source: Molecular Physics. Unidade: FFCLRP

    Subjects: ENZIMAS, BIOFÍSICA

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      VIEIRA, Davi Serradella e DEGRÈVE, Léo. An insight into the thermostability of a pair of xylanases: the role of hydrogen bonds. Molecular Physics, v. 107, n. 1, p. 59-69, 2009Tradução . . Disponível em: https://doi.org/10.1080/00268970902717959. Acesso em: 01 out. 2024.
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      Vieira, D. S., & Degrève, L. (2009). An insight into the thermostability of a pair of xylanases: the role of hydrogen bonds. Molecular Physics, 107( 1), 59-69. doi:10.1080/00268970902717959
    • NLM

      Vieira DS, Degrève L. An insight into the thermostability of a pair of xylanases: the role of hydrogen bonds [Internet]. Molecular Physics. 2009 ; 107( 1): 59-69.[citado 2024 out. 01 ] Available from: https://doi.org/10.1080/00268970902717959
    • Vancouver

      Vieira DS, Degrève L. An insight into the thermostability of a pair of xylanases: the role of hydrogen bonds [Internet]. Molecular Physics. 2009 ; 107( 1): 59-69.[citado 2024 out. 01 ] Available from: https://doi.org/10.1080/00268970902717959
  • Source: Journal of Colloid and Interface Science. Unidade: FFCLRP

    Subjects: ENZIMAS, DETERGENTES, ELASTICIDADE

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      RIGOS, Carolina Fortes et al. The association of Na,K-ATPase subunits studied by circular dichroism, surface tension and dilatational elasticity. Journal of Colloid and Interface Science, v. 325, n. 2, p. 478-484, 2008Tradução . . Disponível em: https://doi.org/10.1016/j.jcis.2008.06.011. Acesso em: 01 out. 2024.
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      Rigos, C. F., Nobre, T. M., Zaniquelli, M. E. D., Ward, R. J., & Ciancaglini, P. (2008). The association of Na,K-ATPase subunits studied by circular dichroism, surface tension and dilatational elasticity. Journal of Colloid and Interface Science, 325( 2), 478-484. doi:10.1016/j.jcis.2008.06.011
    • NLM

      Rigos CF, Nobre TM, Zaniquelli MED, Ward RJ, Ciancaglini P. The association of Na,K-ATPase subunits studied by circular dichroism, surface tension and dilatational elasticity [Internet]. Journal of Colloid and Interface Science. 2008 ; 325( 2): 478-484.[citado 2024 out. 01 ] Available from: https://doi.org/10.1016/j.jcis.2008.06.011
    • Vancouver

      Rigos CF, Nobre TM, Zaniquelli MED, Ward RJ, Ciancaglini P. The association of Na,K-ATPase subunits studied by circular dichroism, surface tension and dilatational elasticity [Internet]. Journal of Colloid and Interface Science. 2008 ; 325( 2): 478-484.[citado 2024 out. 01 ] Available from: https://doi.org/10.1016/j.jcis.2008.06.011
  • Source: Comparative Biochemistry and Physiology, Part A. Unidades: FCFRP, FMRP

    Subjects: ENZIMAS, APOPTOSE, VENENOS DE ORIGEM ANIMAL

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      ALVES, Raquel Melo et al. Evidence of caspase-mediated apoptosis induced by L-amino acid oxidase isolated from Bothrops atrox snake venom. Comparative Biochemistry and Physiology, Part A, v. 151, n. 4, p. 542-550, 2008Tradução . . Disponível em: https://doi.org/10.1016/j.cbpa.2008.07.007. Acesso em: 01 out. 2024.
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      Alves, R. M., Antonucci, G. A., Paiva, H. H., Cintra, A. C. O., Franco, J. J., Franqueiro, E. de P. M., et al. (2008). Evidence of caspase-mediated apoptosis induced by L-amino acid oxidase isolated from Bothrops atrox snake venom. Comparative Biochemistry and Physiology, Part A, 151( 4), 542-550. doi:10.1016/j.cbpa.2008.07.007
    • NLM

      Alves RM, Antonucci GA, Paiva HH, Cintra ACO, Franco JJ, Franqueiro E de PM, Dorta DJ, Giglio JR, Rosa JC, Fuly AL, Baruffi MD, Soares AM, Sampaio SV. Evidence of caspase-mediated apoptosis induced by L-amino acid oxidase isolated from Bothrops atrox snake venom [Internet]. Comparative Biochemistry and Physiology, Part A. 2008 ; 151( 4): 542-550.[citado 2024 out. 01 ] Available from: https://doi.org/10.1016/j.cbpa.2008.07.007
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      Alves RM, Antonucci GA, Paiva HH, Cintra ACO, Franco JJ, Franqueiro E de PM, Dorta DJ, Giglio JR, Rosa JC, Fuly AL, Baruffi MD, Soares AM, Sampaio SV. Evidence of caspase-mediated apoptosis induced by L-amino acid oxidase isolated from Bothrops atrox snake venom [Internet]. Comparative Biochemistry and Physiology, Part A. 2008 ; 151( 4): 542-550.[citado 2024 out. 01 ] Available from: https://doi.org/10.1016/j.cbpa.2008.07.007

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