Filtros : "Archives of Biochemistry and Biophysics" "Indexado no Chemical Titles" Limpar

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  • Source: Archives of Biochemistry and Biophysics. Unidade: FCFRP

    Subjects: METABOLISMO, BIOENERGÉTICA

    Acesso à fonteDOIHow to cite
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    • ABNT

      ANDREU, Gilberto Lázaro Pardo et al. Mangiferin, a natural occurring glucosyl xanthone, increases susceptibility of rat liver mitochondria to calcium-induced permeability transition. Archives of Biochemistry and Biophysics, v. 439, p. 184-193, 2005Tradução . . Disponível em: https://doi.org/10.1016/j.abb.2005.05.015. Acesso em: 09 nov. 2025.
    • APA

      Andreu, G. L. P., Delgado, R., Velho, J. A., Curti, C., & Vercesi, A. E. (2005). Mangiferin, a natural occurring glucosyl xanthone, increases susceptibility of rat liver mitochondria to calcium-induced permeability transition. Archives of Biochemistry and Biophysics, 439, 184-193. doi:10.1016/j.abb.2005.05.015
    • NLM

      Andreu GLP, Delgado R, Velho JA, Curti C, Vercesi AE. Mangiferin, a natural occurring glucosyl xanthone, increases susceptibility of rat liver mitochondria to calcium-induced permeability transition [Internet]. Archives of Biochemistry and Biophysics. 2005 ; 439 184-193.[citado 2025 nov. 09 ] Available from: https://doi.org/10.1016/j.abb.2005.05.015
    • Vancouver

      Andreu GLP, Delgado R, Velho JA, Curti C, Vercesi AE. Mangiferin, a natural occurring glucosyl xanthone, increases susceptibility of rat liver mitochondria to calcium-induced permeability transition [Internet]. Archives of Biochemistry and Biophysics. 2005 ; 439 184-193.[citado 2025 nov. 09 ] Available from: https://doi.org/10.1016/j.abb.2005.05.015
  • Source: Archives of Biochemistry and Biophysics. Unidade: FZEA

    Subjects: MITOCÔNDRIAS, ANIMAIS DOMÉSTICOS, BIOQUÍMICA

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    • ABNT

      CÉSAR, Marcelo Cerqueira e WILSON, John E. All three isoforms of the voltage-dependent anion channel (VDAC1, VDAC2, and VDAC3) are present in mitochondria from bovine, rabbit, and rat brain. Archives of Biochemistry and Biophysics, v. 422, n. 2, p. 191-196, 2004Tradução . . Disponível em: https://doi.org/10.1016/j.abb.2003.12.030. Acesso em: 09 nov. 2025.
    • APA

      César, M. C., & Wilson, J. E. (2004). All three isoforms of the voltage-dependent anion channel (VDAC1, VDAC2, and VDAC3) are present in mitochondria from bovine, rabbit, and rat brain. Archives of Biochemistry and Biophysics, 422( 2), 191-196. doi:10.1016/j.abb.2003.12.030
    • NLM

      César MC, Wilson JE. All three isoforms of the voltage-dependent anion channel (VDAC1, VDAC2, and VDAC3) are present in mitochondria from bovine, rabbit, and rat brain [Internet]. Archives of Biochemistry and Biophysics. 2004 ; 422( 2): 191-196.[citado 2025 nov. 09 ] Available from: https://doi.org/10.1016/j.abb.2003.12.030
    • Vancouver

      César MC, Wilson JE. All three isoforms of the voltage-dependent anion channel (VDAC1, VDAC2, and VDAC3) are present in mitochondria from bovine, rabbit, and rat brain [Internet]. Archives of Biochemistry and Biophysics. 2004 ; 422( 2): 191-196.[citado 2025 nov. 09 ] Available from: https://doi.org/10.1016/j.abb.2003.12.030
  • Source: Archives of Biochemistry and Biophysics. Unidades: FMRP, FFCLRP

    Subjects: LECITINAS, LEGUMINOSAE

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    • ABNT

      KONOZY, Emadeldin H. E. et al. Isolation, purification, and physicochemical characterization of a D-galactose-binding lectin from seeds of Erythrina speciosa. Archives of Biochemistry and Biophysics, v. 410, p. 222-229, 2003Tradução . . Disponível em: https://doi.org/10.1016/s0003-9861(02)00695-1. Acesso em: 09 nov. 2025.
    • APA

      Konozy, E. H. E., Bernardes, E. S., Rosa, C., Faca, V., Greene, L. J., & Ward, R. J. (2003). Isolation, purification, and physicochemical characterization of a D-galactose-binding lectin from seeds of Erythrina speciosa. Archives of Biochemistry and Biophysics, 410, 222-229. doi:10.1016/s0003-9861(02)00695-1
    • NLM

      Konozy EHE, Bernardes ES, Rosa C, Faca V, Greene LJ, Ward RJ. Isolation, purification, and physicochemical characterization of a D-galactose-binding lectin from seeds of Erythrina speciosa [Internet]. Archives of Biochemistry and Biophysics. 2003 ; 410 222-229.[citado 2025 nov. 09 ] Available from: https://doi.org/10.1016/s0003-9861(02)00695-1
    • Vancouver

      Konozy EHE, Bernardes ES, Rosa C, Faca V, Greene LJ, Ward RJ. Isolation, purification, and physicochemical characterization of a D-galactose-binding lectin from seeds of Erythrina speciosa [Internet]. Archives of Biochemistry and Biophysics. 2003 ; 410 222-229.[citado 2025 nov. 09 ] Available from: https://doi.org/10.1016/s0003-9861(02)00695-1
  • Source: Archives of Biochemistry and Biophysics. Unidade: FFCLRP

    Subjects: FOSFOLIPASES A, VENENOS, COBRAS

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    • ABNT

      RULLER, Roberto et al. Chemical denaturation of a homodimeric lysine-49 phospholipase 'A IND 2': a stable dimer interface and a native monomeric intermediate. Archives of Biochemistry and Biophysics, 2003Tradução . . Disponível em: https://doi.org/10.1016/s0003-9861(02)00712-9. Acesso em: 09 nov. 2025.
    • APA

      Ruller, R., Ferreira, T. L., Olivira, A. H. C., & Ward, R. J. (2003). Chemical denaturation of a homodimeric lysine-49 phospholipase 'A IND 2': a stable dimer interface and a native monomeric intermediate. Archives of Biochemistry and Biophysics. doi:10.1016/s0003-9861(02)00712-9
    • NLM

      Ruller R, Ferreira TL, Olivira AHC, Ward RJ. Chemical denaturation of a homodimeric lysine-49 phospholipase 'A IND 2': a stable dimer interface and a native monomeric intermediate [Internet]. Archives of Biochemistry and Biophysics. 2003 ;[citado 2025 nov. 09 ] Available from: https://doi.org/10.1016/s0003-9861(02)00712-9
    • Vancouver

      Ruller R, Ferreira TL, Olivira AHC, Ward RJ. Chemical denaturation of a homodimeric lysine-49 phospholipase 'A IND 2': a stable dimer interface and a native monomeric intermediate [Internet]. Archives of Biochemistry and Biophysics. 2003 ;[citado 2025 nov. 09 ] Available from: https://doi.org/10.1016/s0003-9861(02)00712-9

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