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  • Source: European Journal of Biochemistry. Unidade: IQ

    Subjects: BIOQUÍMICA, POLIMERIZAÇÃO, PROTEÍNAS MUSCULARES

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      PAULUCCI, Adriana Aparecida et al. A specific C-terminal deletion in tropomyosin results in a stronger head-to-tail interaction and increased polymerization. European Journal of Biochemistry, v. 271, n. 3, p. 589-600, 2004Tradução . . Disponível em: https://doi.org/10.1111/j.1432-1033.2003.03961.x. Acesso em: 01 maio 2024.
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      Paulucci, A. A., Katsuyama, Â. M., Sousa, A. D. de, & Farah, C. S. (2004). A specific C-terminal deletion in tropomyosin results in a stronger head-to-tail interaction and increased polymerization. European Journal of Biochemistry, 271( 3), 589-600. doi:10.1111/j.1432-1033.2003.03961.x
    • NLM

      Paulucci AA, Katsuyama ÂM, Sousa AD de, Farah CS. A specific C-terminal deletion in tropomyosin results in a stronger head-to-tail interaction and increased polymerization [Internet]. European Journal of Biochemistry. 2004 ; 271( 3): 589-600.[citado 2024 maio 01 ] Available from: https://doi.org/10.1111/j.1432-1033.2003.03961.x
    • Vancouver

      Paulucci AA, Katsuyama ÂM, Sousa AD de, Farah CS. A specific C-terminal deletion in tropomyosin results in a stronger head-to-tail interaction and increased polymerization [Internet]. European Journal of Biochemistry. 2004 ; 271( 3): 589-600.[citado 2024 maio 01 ] Available from: https://doi.org/10.1111/j.1432-1033.2003.03961.x
  • Source: European Journal of Biochemistry. Unidade: IFSC

    Subjects: CRISTALOGRAFIA, ENZIMAS, LEISHMANIA MEXICANA, PROTEÍNAS

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      CORDEIRO, Artur T. et al. The crystal strucuture of glucose-6-phosphate isomerase from Leishmania mexicana reveals novel active site features. European Journal of Biochemistry, v. 271, n. 13, p. 2765-2772, 2004Tradução . . Disponível em: https://doi.org/10.1111/j.1432-1033.2004.04205.x. Acesso em: 01 maio 2024.
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      Cordeiro, A. T., Michels, P. A. M., Delboni, L. F., & Thiemann, O. H. (2004). The crystal strucuture of glucose-6-phosphate isomerase from Leishmania mexicana reveals novel active site features. European Journal of Biochemistry, 271( 13), 2765-2772. doi:10.1111/j.1432-1033.2004.04205.x
    • NLM

      Cordeiro AT, Michels PAM, Delboni LF, Thiemann OH. The crystal strucuture of glucose-6-phosphate isomerase from Leishmania mexicana reveals novel active site features [Internet]. European Journal of Biochemistry. 2004 ; 271( 13): 2765-2772.[citado 2024 maio 01 ] Available from: https://doi.org/10.1111/j.1432-1033.2004.04205.x
    • Vancouver

      Cordeiro AT, Michels PAM, Delboni LF, Thiemann OH. The crystal strucuture of glucose-6-phosphate isomerase from Leishmania mexicana reveals novel active site features [Internet]. European Journal of Biochemistry. 2004 ; 271( 13): 2765-2772.[citado 2024 maio 01 ] Available from: https://doi.org/10.1111/j.1432-1033.2004.04205.x
  • Source: European Journal of Biochemistry. Unidade: IQ

    Subjects: BIOQUÍMICA, ENZIMAS, BIOENERGÉTICA (ANÁLISE)

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      MARANA, Sandro Roberto et al. Investigation of the substrate specificity of a beta-glycosidase from Spodoptera frugiperda using site-directed mutagenesis and bioenergetics analysis. European Journal of Biochemistry, v. 271, n. 21, p. 4169-4177, 2004Tradução . . Disponível em: https://doi.org/10.1111/j.1432-1033.2004.04354.x. Acesso em: 01 maio 2024.
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      Marana, S. R., Andrade, E. H. P., Ferreira, C., & Terra, W. R. (2004). Investigation of the substrate specificity of a beta-glycosidase from Spodoptera frugiperda using site-directed mutagenesis and bioenergetics analysis. European Journal of Biochemistry, 271( 21), 4169-4177. doi:10.1111/j.1432-1033.2004.04354.x
    • NLM

      Marana SR, Andrade EHP, Ferreira C, Terra WR. Investigation of the substrate specificity of a beta-glycosidase from Spodoptera frugiperda using site-directed mutagenesis and bioenergetics analysis [Internet]. European Journal of Biochemistry. 2004 ; 271( 21): 4169-4177.[citado 2024 maio 01 ] Available from: https://doi.org/10.1111/j.1432-1033.2004.04354.x
    • Vancouver

      Marana SR, Andrade EHP, Ferreira C, Terra WR. Investigation of the substrate specificity of a beta-glycosidase from Spodoptera frugiperda using site-directed mutagenesis and bioenergetics analysis [Internet]. European Journal of Biochemistry. 2004 ; 271( 21): 4169-4177.[citado 2024 maio 01 ] Available from: https://doi.org/10.1111/j.1432-1033.2004.04354.x
  • Source: European Journal of Biochemistry. Unidade: IFSC

    Subjects: CRISTALOGRAFIA, TRYPANOSOMA CRUZI, ENZIMAS, PROTEÍNAS (MODELOS), LEISHMANIA

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      LADAME, Sylvain et al. Crystal structure Trypanosoma cruzi glyceraldehyde-3-phosphate dehydrogenase complexed with an analogue of 1,3-bisphospho-D-plyceric acid: selective inhibition by structure-based design. European Journal of Biochemistry, v. No 2003, n. 22, p. 4574-4586, 2003Tradução . . Disponível em: https://doi.org/10.1046/j.1432-1033.2003.03857.x. Acesso em: 01 maio 2024.
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      Ladame, S., Castilho, M. S., Silva, C. H. T. P., Denier, C., Hannaert, V., Périé Jacques,, et al. (2003). Crystal structure Trypanosoma cruzi glyceraldehyde-3-phosphate dehydrogenase complexed with an analogue of 1,3-bisphospho-D-plyceric acid: selective inhibition by structure-based design. European Journal of Biochemistry, No 2003( 22), 4574-4586. doi:10.1046/j.1432-1033.2003.03857.x
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      Ladame S, Castilho MS, Silva CHTP, Denier C, Hannaert V, Périé Jacques, Oliva G, Willson M. Crystal structure Trypanosoma cruzi glyceraldehyde-3-phosphate dehydrogenase complexed with an analogue of 1,3-bisphospho-D-plyceric acid: selective inhibition by structure-based design [Internet]. European Journal of Biochemistry. 2003 ; No 2003( 22): 4574-4586.[citado 2024 maio 01 ] Available from: https://doi.org/10.1046/j.1432-1033.2003.03857.x
    • Vancouver

      Ladame S, Castilho MS, Silva CHTP, Denier C, Hannaert V, Périé Jacques, Oliva G, Willson M. Crystal structure Trypanosoma cruzi glyceraldehyde-3-phosphate dehydrogenase complexed with an analogue of 1,3-bisphospho-D-plyceric acid: selective inhibition by structure-based design [Internet]. European Journal of Biochemistry. 2003 ; No 2003( 22): 4574-4586.[citado 2024 maio 01 ] Available from: https://doi.org/10.1046/j.1432-1033.2003.03857.x
  • Source: European Journal of Biochemistry. Unidade: ESALQ

    Subjects: MILHO, AMINOÁCIDOS, GENÉTICA VEGETAL, PROTEÍNAS DE PLANTAS

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      AZEVEDO, Ricardo Antunes de et al. Regulation of maize lysine metabolism and endosperm protein synthesis by opaque and floury mutations. European Journal of Biochemistry, v. 270, n. 24, p. 4898-4908, 2003Tradução . . Disponível em: https://doi.org/10.1111/j.1432-1033.2003.03890.x. Acesso em: 01 maio 2024.
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      Azevedo, R. A. de, Damerval, C., Landry, J., Lea, P. J., Bellato, C. M., Meinhardt, L. W., et al. (2003). Regulation of maize lysine metabolism and endosperm protein synthesis by opaque and floury mutations. European Journal of Biochemistry, 270( 24), 4898-4908. doi:10.1111/j.1432-1033.2003.03890.x
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      Azevedo RA de, Damerval C, Landry J, Lea PJ, Bellato CM, Meinhardt LW, Le Guilloux M, Delhaye S, Toro AA, Gaziola SA, Berdejo BDA. Regulation of maize lysine metabolism and endosperm protein synthesis by opaque and floury mutations [Internet]. European Journal of Biochemistry. 2003 ; 270( 24): 4898-4908.[citado 2024 maio 01 ] Available from: https://doi.org/10.1111/j.1432-1033.2003.03890.x
    • Vancouver

      Azevedo RA de, Damerval C, Landry J, Lea PJ, Bellato CM, Meinhardt LW, Le Guilloux M, Delhaye S, Toro AA, Gaziola SA, Berdejo BDA. Regulation of maize lysine metabolism and endosperm protein synthesis by opaque and floury mutations [Internet]. European Journal of Biochemistry. 2003 ; 270( 24): 4898-4908.[citado 2024 maio 01 ] Available from: https://doi.org/10.1111/j.1432-1033.2003.03890.x
  • Source: European Journal of Biochemistry. Unidade: IFSC

    Assunto: CRISTALOGRAFIA

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      HANNAERT, Véronique et al. Kinetic characterization, structure modelling studies and crystallization of Trypanosoma brucei enolase. European Journal of Biochemistry, v. 270, n. 15, p. 3205-3213, 2003Tradução . . Disponível em: https://doi.org/10.1046/j.1432-1033.2003.03692.x. Acesso em: 01 maio 2024.
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      Hannaert, V., Marie-Astrid, A., Rigden, D. J., Giotto, M. T. da S. [M. T. da S. G. - erro de impressão], Thiemann, O. H., Garratt, R. C., et al. (2003). Kinetic characterization, structure modelling studies and crystallization of Trypanosoma brucei enolase. European Journal of Biochemistry, 270( 15), 3205-3213. doi:10.1046/j.1432-1033.2003.03692.x
    • NLM

      Hannaert V, Marie-Astrid A, Rigden DJ, Giotto MT da S [MT da SG- erro de impressão], Thiemann OH, Garratt RC, Van Roy J, Opperdoes FR, Michels PAM. Kinetic characterization, structure modelling studies and crystallization of Trypanosoma brucei enolase [Internet]. European Journal of Biochemistry. 2003 ; 270( 15): 3205-3213.[citado 2024 maio 01 ] Available from: https://doi.org/10.1046/j.1432-1033.2003.03692.x
    • Vancouver

      Hannaert V, Marie-Astrid A, Rigden DJ, Giotto MT da S [MT da SG- erro de impressão], Thiemann OH, Garratt RC, Van Roy J, Opperdoes FR, Michels PAM. Kinetic characterization, structure modelling studies and crystallization of Trypanosoma brucei enolase [Internet]. European Journal of Biochemistry. 2003 ; 270( 15): 3205-3213.[citado 2024 maio 01 ] Available from: https://doi.org/10.1046/j.1432-1033.2003.03692.x
  • Source: European Journal of Biochemistry. Unidade: IQ

    Subjects: BIOQUÍMICA, ENZIMAS

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      MARANA, Sandro Roberto et al. The role of residues R97 and Y331 in modulating the pH optimum of an insect 'beta'-glycosidase of family 1. European Journal of Biochemistry, v. 270, n. 24, p. 4866-4875, 2003Tradução . . Acesso em: 01 maio 2024.
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      Marana, S. R., Mendonça, L. M. F. de, Andrade, E. H. P., Terra, W. R., & Ferreira, C. (2003). The role of residues R97 and Y331 in modulating the pH optimum of an insect 'beta'-glycosidase of family 1. European Journal of Biochemistry, 270( 24), 4866-4875.
    • NLM

      Marana SR, Mendonça LMF de, Andrade EHP, Terra WR, Ferreira C. The role of residues R97 and Y331 in modulating the pH optimum of an insect 'beta'-glycosidase of family 1. European Journal of Biochemistry. 2003 ; 270( 24): 4866-4875.[citado 2024 maio 01 ]
    • Vancouver

      Marana SR, Mendonça LMF de, Andrade EHP, Terra WR, Ferreira C. The role of residues R97 and Y331 in modulating the pH optimum of an insect 'beta'-glycosidase of family 1. European Journal of Biochemistry. 2003 ; 270( 24): 4866-4875.[citado 2024 maio 01 ]
  • Source: European Journal of Biochemistry. Unidade: FMRP

    Subjects: VENENOS DE ORIGEM ANIMAL (ESTRUTURA), TOXINAS, BIOQUÍMICA

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      NICASTRO, Giuseppe et al. Solution structure of crotamine, a Na+ channel affecting toxin from Crotalus durissus terrificus venom. European Journal of Biochemistry, v. 270, p. 1969-1979, 2003Tradução . . Disponível em: https://doi.org/10.1046/j.1432-1033.2003.03563.x. Acesso em: 01 maio 2024.
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      Nicastro, G., Franzoni, L., Chiara, C., Mancin, A. C., Giglio, J. R., & Spisni, A. (2003). Solution structure of crotamine, a Na+ channel affecting toxin from Crotalus durissus terrificus venom. European Journal of Biochemistry, 270, 1969-1979. doi:10.1046/j.1432-1033.2003.03563.x
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      Nicastro G, Franzoni L, Chiara C, Mancin AC, Giglio JR, Spisni A. Solution structure of crotamine, a Na+ channel affecting toxin from Crotalus durissus terrificus venom [Internet]. European Journal of Biochemistry. 2003 ; 270 1969-1979.[citado 2024 maio 01 ] Available from: https://doi.org/10.1046/j.1432-1033.2003.03563.x
    • Vancouver

      Nicastro G, Franzoni L, Chiara C, Mancin AC, Giglio JR, Spisni A. Solution structure of crotamine, a Na+ channel affecting toxin from Crotalus durissus terrificus venom [Internet]. European Journal of Biochemistry. 2003 ; 270 1969-1979.[citado 2024 maio 01 ] Available from: https://doi.org/10.1046/j.1432-1033.2003.03563.x
  • Source: European Journal of Biochemistry. Unidade: IQ

    Subjects: BIOQUÍMICA, ESCHERICHIA COLI, MÚSCULO ESQUELÉTICO

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      OLIVEIRA, Deodoro Camargo Silva Gonçalves de e REINACH, Fernando de Castro. The calcium-induced switch in the troponin complex probed by fluorescent mutants of troponin I. European Journal of Biochemistry, v. 270, n. 14, p. 2937-2944, 2003Tradução . . Disponível em: https://doi.org/10.1046/j.1432-1033.2003.03659.x. Acesso em: 01 maio 2024.
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      Oliveira, D. C. S. G. de, & Reinach, F. de C. (2003). The calcium-induced switch in the troponin complex probed by fluorescent mutants of troponin I. European Journal of Biochemistry, 270( 14), 2937-2944. doi:10.1046/j.1432-1033.2003.03659.x
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      Oliveira DCSG de, Reinach F de C. The calcium-induced switch in the troponin complex probed by fluorescent mutants of troponin I [Internet]. European Journal of Biochemistry. 2003 ; 270( 14): 2937-2944.[citado 2024 maio 01 ] Available from: https://doi.org/10.1046/j.1432-1033.2003.03659.x
    • Vancouver

      Oliveira DCSG de, Reinach F de C. The calcium-induced switch in the troponin complex probed by fluorescent mutants of troponin I [Internet]. European Journal of Biochemistry. 2003 ; 270( 14): 2937-2944.[citado 2024 maio 01 ] Available from: https://doi.org/10.1046/j.1432-1033.2003.03659.x
  • Source: European Journal of Biochemistry. Unidade: IFSC

    Subjects: CRISTALOGRAFIA, PROTEÍNAS

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      BENELLI, Elaine Machado et al. Herbaspirillum seropedicae signal transduction protein PII is structurally similar to the enteric GlnK. European Journal of Biochemistry, v. 269, n. 13, p. 3296-3303, 2002Tradução . . Disponível em: https://doi.org/10.1046/j.1432-1033.2002.03011.x. Acesso em: 01 maio 2024.
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      Benelli, E. M., Buck, M., Polikarpov, I., Souza, E. M., Cruz, L. M., & Pedrosa, F. O. (2002). Herbaspirillum seropedicae signal transduction protein PII is structurally similar to the enteric GlnK. European Journal of Biochemistry, 269( 13), 3296-3303. doi:10.1046/j.1432-1033.2002.03011.x
    • NLM

      Benelli EM, Buck M, Polikarpov I, Souza EM, Cruz LM, Pedrosa FO. Herbaspirillum seropedicae signal transduction protein PII is structurally similar to the enteric GlnK [Internet]. European Journal of Biochemistry. 2002 ; 269( 13): 3296-3303.[citado 2024 maio 01 ] Available from: https://doi.org/10.1046/j.1432-1033.2002.03011.x
    • Vancouver

      Benelli EM, Buck M, Polikarpov I, Souza EM, Cruz LM, Pedrosa FO. Herbaspirillum seropedicae signal transduction protein PII is structurally similar to the enteric GlnK [Internet]. European Journal of Biochemistry. 2002 ; 269( 13): 3296-3303.[citado 2024 maio 01 ] Available from: https://doi.org/10.1046/j.1432-1033.2002.03011.x
  • Source: European Journal of Biochemistry. Unidade: IQ

    Subjects: BIOQUÍMICA, ENZIMAS, LEPIDOPTERA

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      MARANA, Sandro Roberto e TERRA, Walter Ribeiro e FERREIRA, Clélia. The role of amino-acid residues Q39 and E451 in the determination of substrate specificity of the Spodoptera frugiperda 'beta'-glycosidase. European Journal of Biochemistry, v. 269, n. 15, p. 3705-3714, 2002Tradução . . Disponível em: https://doi.org/10.1046/j.1432-1033.2002.03061.x. Acesso em: 01 maio 2024.
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      Marana, S. R., Terra, W. R., & Ferreira, C. (2002). The role of amino-acid residues Q39 and E451 in the determination of substrate specificity of the Spodoptera frugiperda 'beta'-glycosidase. European Journal of Biochemistry, 269( 15), 3705-3714. doi:10.1046/j.1432-1033.2002.03061.x
    • NLM

      Marana SR, Terra WR, Ferreira C. The role of amino-acid residues Q39 and E451 in the determination of substrate specificity of the Spodoptera frugiperda 'beta'-glycosidase [Internet]. European Journal of Biochemistry. 2002 ; 269( 15): 3705-3714.[citado 2024 maio 01 ] Available from: https://doi.org/10.1046/j.1432-1033.2002.03061.x
    • Vancouver

      Marana SR, Terra WR, Ferreira C. The role of amino-acid residues Q39 and E451 in the determination of substrate specificity of the Spodoptera frugiperda 'beta'-glycosidase [Internet]. European Journal of Biochemistry. 2002 ; 269( 15): 3705-3714.[citado 2024 maio 01 ] Available from: https://doi.org/10.1046/j.1432-1033.2002.03061.x
  • Source: European Journal of Biochemistry. Unidade: EP

    Subjects: ESPECTROMETRIA DE MASSAS, METABOLISMO, SACCHAROMYCES, MODELOS MATEMÁTICOS

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      CHRISTENSEN, Bjarke e GOMBERT, Andreas Karoly e NIELSEN, Jens. Analysis of flux estimates based on C-13-labelling experiments. European Journal of Biochemistry, v. 269, n. 11, p. 2795.2800, 2002Tradução . . Disponível em: https://doi.org/10.1046/j.1432-1033.2002.02959.x. Acesso em: 01 maio 2024.
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      Christensen, B., Gombert, A. K., & Nielsen, J. (2002). Analysis of flux estimates based on C-13-labelling experiments. European Journal of Biochemistry, 269( 11), 2795.2800. doi:10.1046/j.1432-1033.2002.02959.x
    • NLM

      Christensen B, Gombert AK, Nielsen J. Analysis of flux estimates based on C-13-labelling experiments [Internet]. European Journal of Biochemistry. 2002 ; 269( 11): 2795.2800.[citado 2024 maio 01 ] Available from: https://doi.org/10.1046/j.1432-1033.2002.02959.x
    • Vancouver

      Christensen B, Gombert AK, Nielsen J. Analysis of flux estimates based on C-13-labelling experiments [Internet]. European Journal of Biochemistry. 2002 ; 269( 11): 2795.2800.[citado 2024 maio 01 ] Available from: https://doi.org/10.1046/j.1432-1033.2002.02959.x
  • Source: European Journal of Biochemistry. Unidade: IFSC

    Subjects: BIOQUÍMICA, BIOFÍSICA, PROTEÍNAS

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      CAMPANA, Patrícia Targon et al. Unfonding and refolding studies of frutalin, a tetrametric D-galactose binding lectin. European Journal of Biochemistry, v. 269, p. 753-758, 2002Tradução . . Disponível em: https://doi.org/10.1046/j.0014-2956.2001.02502.x. Acesso em: 01 maio 2024.
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      Campana, P. T., Moraes, D. I. de, Monteiro-Moreira, A. C. O., & Beltramini, L. M. (2002). Unfonding and refolding studies of frutalin, a tetrametric D-galactose binding lectin. European Journal of Biochemistry, 269, 753-758. doi:10.1046/j.0014-2956.2001.02502.x
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      Campana PT, Moraes DI de, Monteiro-Moreira ACO, Beltramini LM. Unfonding and refolding studies of frutalin, a tetrametric D-galactose binding lectin [Internet]. European Journal of Biochemistry. 2002 ;269 753-758.[citado 2024 maio 01 ] Available from: https://doi.org/10.1046/j.0014-2956.2001.02502.x
    • Vancouver

      Campana PT, Moraes DI de, Monteiro-Moreira ACO, Beltramini LM. Unfonding and refolding studies of frutalin, a tetrametric D-galactose binding lectin [Internet]. European Journal of Biochemistry. 2002 ;269 753-758.[citado 2024 maio 01 ] Available from: https://doi.org/10.1046/j.0014-2956.2001.02502.x
  • Source: European Journal of Biochemistry. Unidade: IFSC

    Subjects: BIOQUÍMICA, BIOFÍSICA, PROTEÍNAS

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      CAMPANA, Patrícia Targon et al. Ulfonding and refolding studies of frutalin, a tetrametric D-galactose binding lectin. European Journal of Biochemistry, v. 268, n. 21, p. 5647-5652, 2001Tradução . . Disponível em: https://doi.org/10.1046/j.0014-2956.2001.02502.x. Acesso em: 01 maio 2024.
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      Campana, P. T., Moraes, D. I. de, Monteiro-Moreira, A. C. O., & Beltramini, L. M. (2001). Ulfonding and refolding studies of frutalin, a tetrametric D-galactose binding lectin. European Journal of Biochemistry, 268( 21), 5647-5652. doi:10.1046/j.0014-2956.2001.02502.x
    • NLM

      Campana PT, Moraes DI de, Monteiro-Moreira ACO, Beltramini LM. Ulfonding and refolding studies of frutalin, a tetrametric D-galactose binding lectin [Internet]. European Journal of Biochemistry. 2001 ;268( 21): 5647-5652.[citado 2024 maio 01 ] Available from: https://doi.org/10.1046/j.0014-2956.2001.02502.x
    • Vancouver

      Campana PT, Moraes DI de, Monteiro-Moreira ACO, Beltramini LM. Ulfonding and refolding studies of frutalin, a tetrametric D-galactose binding lectin [Internet]. European Journal of Biochemistry. 2001 ;268( 21): 5647-5652.[citado 2024 maio 01 ] Available from: https://doi.org/10.1046/j.0014-2956.2001.02502.x
  • Source: European Journal of Biochemistry. Unidade: FMRP

    Subjects: PEPTÍDEOS, ENZIMAS

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      PORTARO, Fernanda C. V. et al. Free ATP inhibits thimet oligopeptidase (EC 3.4.24.15) activity, induces autophosphorylation in vitro, and oligopeptide degradation in macrophage. European Journal of Biochemistry, v. 268, p. 887-894, 2001Tradução . . Disponível em: https://doi.org/10.1046/j.1432-1327.2001.01978.x. Acesso em: 01 maio 2024.
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      Portaro, F. C. V., Hayashi, M. A. F., Silva, C. L., & Camargo, A. C. M. de. (2001). Free ATP inhibits thimet oligopeptidase (EC 3.4.24.15) activity, induces autophosphorylation in vitro, and oligopeptide degradation in macrophage. European Journal of Biochemistry, 268, 887-894. doi:10.1046/j.1432-1327.2001.01978.x
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      Portaro FCV, Hayashi MAF, Silva CL, Camargo ACM de. Free ATP inhibits thimet oligopeptidase (EC 3.4.24.15) activity, induces autophosphorylation in vitro, and oligopeptide degradation in macrophage [Internet]. European Journal of Biochemistry. 2001 ; 268 887-894.[citado 2024 maio 01 ] Available from: https://doi.org/10.1046/j.1432-1327.2001.01978.x
    • Vancouver

      Portaro FCV, Hayashi MAF, Silva CL, Camargo ACM de. Free ATP inhibits thimet oligopeptidase (EC 3.4.24.15) activity, induces autophosphorylation in vitro, and oligopeptide degradation in macrophage [Internet]. European Journal of Biochemistry. 2001 ; 268 887-894.[citado 2024 maio 01 ] Available from: https://doi.org/10.1046/j.1432-1327.2001.01978.x
  • Source: European Journal of Biochemistry. Unidade: ICB

    Assunto: FISIOLOGIA

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      CEDDIA, Rolando B et al. Leptin stimulates uncoupling protein-2 mRNA expression and Krebs cycle activity and inhibts lipid synthesis in isolated rat white adipocytes. European Journal of Biochemistry, v. 267, p. 5952-8, 2000Tradução . . Disponível em: https://doi.org/10.1046/j.1432-1327.2000.01664.x. Acesso em: 01 maio 2024.
    • APA

      Ceddia, R. B., William Jr, W. N., Lima, F. B., Flandin, P., Curi, R., & Giacobino, J. -P. (2000). Leptin stimulates uncoupling protein-2 mRNA expression and Krebs cycle activity and inhibts lipid synthesis in isolated rat white adipocytes. European Journal of Biochemistry, 267, 5952-8. doi:10.1046/j.1432-1327.2000.01664.x
    • NLM

      Ceddia RB, William Jr WN, Lima FB, Flandin P, Curi R, Giacobino J-P. Leptin stimulates uncoupling protein-2 mRNA expression and Krebs cycle activity and inhibts lipid synthesis in isolated rat white adipocytes [Internet]. European Journal of Biochemistry. 2000 ; 267 5952-8.[citado 2024 maio 01 ] Available from: https://doi.org/10.1046/j.1432-1327.2000.01664.x
    • Vancouver

      Ceddia RB, William Jr WN, Lima FB, Flandin P, Curi R, Giacobino J-P. Leptin stimulates uncoupling protein-2 mRNA expression and Krebs cycle activity and inhibts lipid synthesis in isolated rat white adipocytes [Internet]. European Journal of Biochemistry. 2000 ; 267 5952-8.[citado 2024 maio 01 ] Available from: https://doi.org/10.1046/j.1432-1327.2000.01664.x
  • Source: European Journal of Biochemistry. Unidade: ESALQ

    Subjects: MILHO, BIOQUÍMICA

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      KEMPER, E L et al. Structure and regulation of the bifunctional enzyme lysine-ketoglutarate reductase-saccaropine dehydrogenase in maize. European Journal of Biochemistry, v. 253, p. 720-729, 1998Tradução . . Disponível em: https://doi.org/10.1046/j.1432-1327.1998.2530720.x. Acesso em: 01 maio 2024.
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      Kemper, E. L., Cord Neto, G., Capella, A. N., Gonçalves-Butruille, M., Azevedo, R. A. de, & Arruda, P. (1998). Structure and regulation of the bifunctional enzyme lysine-ketoglutarate reductase-saccaropine dehydrogenase in maize. European Journal of Biochemistry, 253, 720-729. doi:10.1046/j.1432-1327.1998.2530720.x
    • NLM

      Kemper EL, Cord Neto G, Capella AN, Gonçalves-Butruille M, Azevedo RA de, Arruda P. Structure and regulation of the bifunctional enzyme lysine-ketoglutarate reductase-saccaropine dehydrogenase in maize [Internet]. European Journal of Biochemistry. 1998 ; 253 720-729.[citado 2024 maio 01 ] Available from: https://doi.org/10.1046/j.1432-1327.1998.2530720.x
    • Vancouver

      Kemper EL, Cord Neto G, Capella AN, Gonçalves-Butruille M, Azevedo RA de, Arruda P. Structure and regulation of the bifunctional enzyme lysine-ketoglutarate reductase-saccaropine dehydrogenase in maize [Internet]. European Journal of Biochemistry. 1998 ; 253 720-729.[citado 2024 maio 01 ] Available from: https://doi.org/10.1046/j.1432-1327.1998.2530720.x
  • Source: European Journal of Biochemistry. Unidade: IQ

    Assunto: BIOQUÍMICA

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      ZELADA, A et al. Isolation and characterization of cyclic AMP-dependent protein kinase from Candida albicans: purification of the regulatory and catalytic subunits. European Journal of Biochemistry, v. 252, p. 245-52, 1998Tradução . . Disponível em: https://doi.org/10.1046/j.1432-1327.1998.2520245.x. Acesso em: 01 maio 2024.
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      Zelada, A., Passeron, S., Gomes, S. L., & Cantore, M. L. (1998). Isolation and characterization of cyclic AMP-dependent protein kinase from Candida albicans: purification of the regulatory and catalytic subunits. European Journal of Biochemistry, 252, 245-52. doi:10.1046/j.1432-1327.1998.2520245.x
    • NLM

      Zelada A, Passeron S, Gomes SL, Cantore ML. Isolation and characterization of cyclic AMP-dependent protein kinase from Candida albicans: purification of the regulatory and catalytic subunits [Internet]. European Journal of Biochemistry. 1998 ; 252 245-52.[citado 2024 maio 01 ] Available from: https://doi.org/10.1046/j.1432-1327.1998.2520245.x
    • Vancouver

      Zelada A, Passeron S, Gomes SL, Cantore ML. Isolation and characterization of cyclic AMP-dependent protein kinase from Candida albicans: purification of the regulatory and catalytic subunits [Internet]. European Journal of Biochemistry. 1998 ; 252 245-52.[citado 2024 maio 01 ] Available from: https://doi.org/10.1046/j.1432-1327.1998.2520245.x
  • Source: European Journal of Biochemistry. Unidade: IQ

    Subjects: BIOQUÍMICA, SCHISTOSOMA

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      TORRES, C R et al. Divalent cation dependence and inhibition of Schistosoma mansoni ATP diphosphohydrolase by fluorosulfonylbenzoyladenosine. European Journal of Biochemistry, v. 251, n. 1/2, p. 516-521, 1998Tradução . . Disponível em: https://doi.org/10.1046/j.1432-1327.1998.2510516.x. Acesso em: 01 maio 2024.
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      Torres, C. R., Vasconcelos, E. G., Ferreira, S. T., & Verjovski-Almeida, S. (1998). Divalent cation dependence and inhibition of Schistosoma mansoni ATP diphosphohydrolase by fluorosulfonylbenzoyladenosine. European Journal of Biochemistry, 251( 1/2), 516-521. doi:10.1046/j.1432-1327.1998.2510516.x
    • NLM

      Torres CR, Vasconcelos EG, Ferreira ST, Verjovski-Almeida S. Divalent cation dependence and inhibition of Schistosoma mansoni ATP diphosphohydrolase by fluorosulfonylbenzoyladenosine [Internet]. European Journal of Biochemistry. 1998 ; 251( 1/2): 516-521.[citado 2024 maio 01 ] Available from: https://doi.org/10.1046/j.1432-1327.1998.2510516.x
    • Vancouver

      Torres CR, Vasconcelos EG, Ferreira ST, Verjovski-Almeida S. Divalent cation dependence and inhibition of Schistosoma mansoni ATP diphosphohydrolase by fluorosulfonylbenzoyladenosine [Internet]. European Journal of Biochemistry. 1998 ; 251( 1/2): 516-521.[citado 2024 maio 01 ] Available from: https://doi.org/10.1046/j.1432-1327.1998.2510516.x
  • Source: European Journal of Biochemistry. Unidade: ESALQ

    Subjects: ENZIMAS, BIOQUÍMICA

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      GAZIOLA, Salete Aparecida et al. The enzymology of lysine catabolism in rice seeds isolation, characterization, and regulatory properties of a lysine 2-oxoglutarate reductase/saccharopine dehydrogenase bifunctional polypetide. European Journal of Biochemistry, v. 247, p. 364-371, 1997Tradução . . Disponível em: https://doi.org/10.1111/j.1432-1033.1997.00364.x. Acesso em: 01 maio 2024.
    • APA

      Gaziola, S. A., Teixeira, C. M. G., Lugli, J., Sodek, L., & Azevedo, R. A. de. (1997). The enzymology of lysine catabolism in rice seeds isolation, characterization, and regulatory properties of a lysine 2-oxoglutarate reductase/saccharopine dehydrogenase bifunctional polypetide. European Journal of Biochemistry, 247, 364-371. doi:10.1111/j.1432-1033.1997.00364.x
    • NLM

      Gaziola SA, Teixeira CMG, Lugli J, Sodek L, Azevedo RA de. The enzymology of lysine catabolism in rice seeds isolation, characterization, and regulatory properties of a lysine 2-oxoglutarate reductase/saccharopine dehydrogenase bifunctional polypetide [Internet]. European Journal of Biochemistry. 1997 ; 247 364-371.[citado 2024 maio 01 ] Available from: https://doi.org/10.1111/j.1432-1033.1997.00364.x
    • Vancouver

      Gaziola SA, Teixeira CMG, Lugli J, Sodek L, Azevedo RA de. The enzymology of lysine catabolism in rice seeds isolation, characterization, and regulatory properties of a lysine 2-oxoglutarate reductase/saccharopine dehydrogenase bifunctional polypetide [Internet]. European Journal of Biochemistry. 1997 ; 247 364-371.[citado 2024 maio 01 ] Available from: https://doi.org/10.1111/j.1432-1033.1997.00364.x

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