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

    Assunto: LEISHMANIA BRASILIENSIS

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      DORES-SILVA, Paulo Roberto das et al. Structural and functional studies of the Leishmania braziliensis mitochondrial Hsp70: similarities and dissimilarities to human orthologues. Archives of Biochemistry and Biophysics, v. 613, p. 43-52, 2017Tradução . . Disponível em: https://doi.org/10.1016/j.abb.2016.11.004. Acesso em: 09 out. 2024.
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      Dores-Silva, P. R. das, Nishimura, L. S., Kiraly, V. T. R., & Borges, J. C. (2017). Structural and functional studies of the Leishmania braziliensis mitochondrial Hsp70: similarities and dissimilarities to human orthologues. Archives of Biochemistry and Biophysics, 613, 43-52. doi:10.1016/j.abb.2016.11.004
    • NLM

      Dores-Silva PR das, Nishimura LS, Kiraly VTR, Borges JC. Structural and functional studies of the Leishmania braziliensis mitochondrial Hsp70: similarities and dissimilarities to human orthologues [Internet]. Archives of Biochemistry and Biophysics. 2017 ; 613 43-52.[citado 2024 out. 09 ] Available from: https://doi.org/10.1016/j.abb.2016.11.004
    • Vancouver

      Dores-Silva PR das, Nishimura LS, Kiraly VTR, Borges JC. Structural and functional studies of the Leishmania braziliensis mitochondrial Hsp70: similarities and dissimilarities to human orthologues [Internet]. Archives of Biochemistry and Biophysics. 2017 ; 613 43-52.[citado 2024 out. 09 ] Available from: https://doi.org/10.1016/j.abb.2016.11.004
  • Source: Archives of Biochemistry and Biophysics. Unidades: IQSC, IF

    Subjects: BIOFÍSICA, BIOLOGIA MOLECULAR

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      SERAPHIM, Thiago Vargas et al. The C-terminal region of the human p23 chaperone modulates its structure and function. Archives of Biochemistry and Biophysics, v. 565, p. 57-67, 2015Tradução . . Disponível em: https://doi.org/10.1016/j.abb.2014.10.015. Acesso em: 09 out. 2024.
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      Seraphim, T. V., Gava, L. M., Mokry, D. Z., Cagliari, T. D., Barbosa, L. R. S., Ramos, C. H. I., & Borges, J. C. (2015). The C-terminal region of the human p23 chaperone modulates its structure and function. Archives of Biochemistry and Biophysics, 565, 57-67. doi:10.1016/j.abb.2014.10.015
    • NLM

      Seraphim TV, Gava LM, Mokry DZ, Cagliari TD, Barbosa LRS, Ramos CHI, Borges JC. The C-terminal region of the human p23 chaperone modulates its structure and function [Internet]. Archives of Biochemistry and Biophysics. 2015 ; 565 57-67.[citado 2024 out. 09 ] Available from: https://doi.org/10.1016/j.abb.2014.10.015
    • Vancouver

      Seraphim TV, Gava LM, Mokry DZ, Cagliari TD, Barbosa LRS, Ramos CHI, Borges JC. The C-terminal region of the human p23 chaperone modulates its structure and function [Internet]. Archives of Biochemistry and Biophysics. 2015 ; 565 57-67.[citado 2024 out. 09 ] Available from: https://doi.org/10.1016/j.abb.2014.10.015
  • Source: Archives of Biochemistry and Biophysics. Unidades: IF, IQSC

    Subjects: BIOFÍSICA, BIOLOGIA MOLECULAR

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      DORES-SILVA, Paulo Roberto das et al. Low resolution structural characterization of the Hsp70-interacting protein – Hip – from Leishmania braziliensis emphasizes its high asymmetry. Archives of Biochemistry and Biophysics, v. 520, n. 2, p. 88-98, 2012Tradução . . Disponível em: https://doi.org/10.1016/j.abb.2012.02.009. Acesso em: 09 out. 2024.
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      Dores-Silva, P. R. das, Silva, E. R., Gomes, F. E. R., Silva, K. P., Barbosa, L. R. S., & Borges, J. C. (2012). Low resolution structural characterization of the Hsp70-interacting protein – Hip – from Leishmania braziliensis emphasizes its high asymmetry. Archives of Biochemistry and Biophysics, 520( 2), 88-98. doi:10.1016/j.abb.2012.02.009
    • NLM

      Dores-Silva PR das, Silva ER, Gomes FER, Silva KP, Barbosa LRS, Borges JC. Low resolution structural characterization of the Hsp70-interacting protein – Hip – from Leishmania braziliensis emphasizes its high asymmetry [Internet]. Archives of Biochemistry and Biophysics. 2012 ; 520( 2): 88-98.[citado 2024 out. 09 ] Available from: https://doi.org/10.1016/j.abb.2012.02.009
    • Vancouver

      Dores-Silva PR das, Silva ER, Gomes FER, Silva KP, Barbosa LRS, Borges JC. Low resolution structural characterization of the Hsp70-interacting protein – Hip – from Leishmania braziliensis emphasizes its high asymmetry [Internet]. Archives of Biochemistry and Biophysics. 2012 ; 520( 2): 88-98.[citado 2024 out. 09 ] Available from: https://doi.org/10.1016/j.abb.2012.02.009
  • Source: Archives of Biochemistry and Biophysics. Unidade: IQSC

    Subjects: BIOFÍSICA, BIOLOGIA MOLECULAR

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      CARVALHO, Francisco Adriano O e SANTIAGO, Patricia Soares e TABAK, Marcel. On the stability of the extracellular hemoglobin of glossoscolex paulistus, in two iron oxidation sates, in the presence of urea. Archives of Biochemistry and Biophysics, v. 519, n. 1, p. 46-58, 2012Tradução . . Disponível em: https://doi.org/10.1016/j.abb.2012.01.007. Acesso em: 09 out. 2024.
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      Carvalho, F. A. O., Santiago, P. S., & Tabak, M. (2012). On the stability of the extracellular hemoglobin of glossoscolex paulistus, in two iron oxidation sates, in the presence of urea. Archives of Biochemistry and Biophysics, 519( 1), 46-58. doi:10.1016/j.abb.2012.01.007
    • NLM

      Carvalho FAO, Santiago PS, Tabak M. On the stability of the extracellular hemoglobin of glossoscolex paulistus, in two iron oxidation sates, in the presence of urea [Internet]. Archives of Biochemistry and Biophysics. 2012 ; 519( 1): 46-58.[citado 2024 out. 09 ] Available from: https://doi.org/10.1016/j.abb.2012.01.007
    • Vancouver

      Carvalho FAO, Santiago PS, Tabak M. On the stability of the extracellular hemoglobin of glossoscolex paulistus, in two iron oxidation sates, in the presence of urea [Internet]. Archives of Biochemistry and Biophysics. 2012 ; 519( 1): 46-58.[citado 2024 out. 09 ] Available from: https://doi.org/10.1016/j.abb.2012.01.007
  • Source: Archives of Biochemistry and Biophysics. Unidade: IQSC

    Subjects: BIOFÍSICA, BIOLOGIA MOLECULAR

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      GAVA, Lisandra M et al. Stoichiometry and thermodynamics of the interaction between the C-terminus of human 90KDa heat schock protein Hsp90 and the mitochondrial translocase of outer membrane Tom70. Archives of Biochemistry and Biophysics, v. 513, n. 2, p. 119-125, 2011Tradução . . Disponível em: https://doi.org/10.1016/j.abb.2011.06.015. Acesso em: 09 out. 2024.
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      Gava, L. M., Gonçalves, D. C., Borges, J. C., & Ramos, C. H. I. (2011). Stoichiometry and thermodynamics of the interaction between the C-terminus of human 90KDa heat schock protein Hsp90 and the mitochondrial translocase of outer membrane Tom70. Archives of Biochemistry and Biophysics, 513( 2), 119-125. doi:10.1016/j.abb.2011.06.015
    • NLM

      Gava LM, Gonçalves DC, Borges JC, Ramos CHI. Stoichiometry and thermodynamics of the interaction between the C-terminus of human 90KDa heat schock protein Hsp90 and the mitochondrial translocase of outer membrane Tom70 [Internet]. Archives of Biochemistry and Biophysics. 2011 ; 513( 2): 119-125.[citado 2024 out. 09 ] Available from: https://doi.org/10.1016/j.abb.2011.06.015
    • Vancouver

      Gava LM, Gonçalves DC, Borges JC, Ramos CHI. Stoichiometry and thermodynamics of the interaction between the C-terminus of human 90KDa heat schock protein Hsp90 and the mitochondrial translocase of outer membrane Tom70 [Internet]. Archives of Biochemistry and Biophysics. 2011 ; 513( 2): 119-125.[citado 2024 out. 09 ] Available from: https://doi.org/10.1016/j.abb.2011.06.015
  • Source: Archives of Biochemistry and Biophysics. Unidade: IQ

    Subjects: ZINCO, COBRE, SUPERÓXIDO DISMUTASE, ÓXIDO NÍTRICO, PROTEÍNAS

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      VAZ, Sandra Muntz et al. Oxidation and nitration of ribonuclease and lysozyme by peroxynitrite and myeloperoxidase. Archives of Biochemistry and Biophysics, v. 484, n. 2, p. 127-133, 2009Tradução . . Disponível em: https://doi.org/10.1016/j.abb.2008.12.017. Acesso em: 09 out. 2024.
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      Vaz, S. M., Prado, F. M., Di Mascio, P., & Augusto, O. (2009). Oxidation and nitration of ribonuclease and lysozyme by peroxynitrite and myeloperoxidase. Archives of Biochemistry and Biophysics, 484( 2), 127-133. doi:10.1016/j.abb.2008.12.017
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      Vaz SM, Prado FM, Di Mascio P, Augusto O. Oxidation and nitration of ribonuclease and lysozyme by peroxynitrite and myeloperoxidase [Internet]. Archives of Biochemistry and Biophysics. 2009 ; 484( 2): 127-133.[citado 2024 out. 09 ] Available from: https://doi.org/10.1016/j.abb.2008.12.017
    • Vancouver

      Vaz SM, Prado FM, Di Mascio P, Augusto O. Oxidation and nitration of ribonuclease and lysozyme by peroxynitrite and myeloperoxidase [Internet]. Archives of Biochemistry and Biophysics. 2009 ; 484( 2): 127-133.[citado 2024 out. 09 ] Available from: https://doi.org/10.1016/j.abb.2008.12.017
  • Source: Archives of Biochemistry and Biophysics. Unidade: FFCLRP

    Subjects: CRUSTACEA, SÓDIO, POTÁSSIO, BIOQUÍMICA

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      MASUI, D. C. et al. The crustacean gill (Na+,K+)-ATPAse: allosteric modulation of high- and low-affinity ATP-binding sites by sodium and potassium. Archives of Biochemistry and Biophysics, v. 479, n. 2, p. 139-144, 2008Tradução . . Disponível em: https://doi.org/10.1016/j.abb.2008.08.018. Acesso em: 09 out. 2024.
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      Masui, D. C., Silva, E. C. C., Mantelatto, F. L. M., McNamara, J. C., Barrabin, H., Scofano, H. M., et al. (2008). The crustacean gill (Na+,K+)-ATPAse: allosteric modulation of high- and low-affinity ATP-binding sites by sodium and potassium. Archives of Biochemistry and Biophysics, 479( 2), 139-144. doi:10.1016/j.abb.2008.08.018
    • NLM

      Masui DC, Silva ECC, Mantelatto FLM, McNamara JC, Barrabin H, Scofano HM, Fontes CFL, Furriel RPM, Leone F de A. The crustacean gill (Na+,K+)-ATPAse: allosteric modulation of high- and low-affinity ATP-binding sites by sodium and potassium [Internet]. Archives of Biochemistry and Biophysics. 2008 ; 479( 2): 139-144.[citado 2024 out. 09 ] Available from: https://doi.org/10.1016/j.abb.2008.08.018
    • Vancouver

      Masui DC, Silva ECC, Mantelatto FLM, McNamara JC, Barrabin H, Scofano HM, Fontes CFL, Furriel RPM, Leone F de A. The crustacean gill (Na+,K+)-ATPAse: allosteric modulation of high- and low-affinity ATP-binding sites by sodium and potassium [Internet]. Archives of Biochemistry and Biophysics. 2008 ; 479( 2): 139-144.[citado 2024 out. 09 ] Available from: https://doi.org/10.1016/j.abb.2008.08.018
  • Source: Archives of Biochemistry and Biophysics. Unidade: FCFRP

    Subjects: METABOLISMO, BIOENERGÉTICA

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      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 out. 2024.
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      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 2024 out. 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 2024 out. 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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      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 out. 2024.
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      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 2024 out. 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 2024 out. 09 ] Available from: https://doi.org/10.1016/j.abb.2003.12.030
  • Source: Archives of Biochemistry and Biophysics. Unidade: IQ

    Subjects: DANO AO DNA, BIOQUÍMICA, ESCHERICHIA COLI

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      RAVANAT, Jean-Luc et al. Mechanistic aspects of the oxidation of DNA constituents mediated by singlet molecular oxygen. Archives of Biochemistry and Biophysics, v. 423, n. 1, p. 23-30, 2004Tradução . . Disponível em: https://doi.org/10.1016/j.abb.2003.10.018. Acesso em: 09 out. 2024.
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      Ravanat, J. -L., Martinez, G. R., Medeiros, M. H. G. de, Di Mascio, P., & Cadet, J. (2004). Mechanistic aspects of the oxidation of DNA constituents mediated by singlet molecular oxygen. Archives of Biochemistry and Biophysics, 423( 1), 23-30. doi:10.1016/j.abb.2003.10.018
    • NLM

      Ravanat J-L, Martinez GR, Medeiros MHG de, Di Mascio P, Cadet J. Mechanistic aspects of the oxidation of DNA constituents mediated by singlet molecular oxygen [Internet]. Archives of Biochemistry and Biophysics. 2004 ; 423( 1): 23-30.[citado 2024 out. 09 ] Available from: https://doi.org/10.1016/j.abb.2003.10.018
    • Vancouver

      Ravanat J-L, Martinez GR, Medeiros MHG de, Di Mascio P, Cadet J. Mechanistic aspects of the oxidation of DNA constituents mediated by singlet molecular oxygen [Internet]. Archives of Biochemistry and Biophysics. 2004 ; 423( 1): 23-30.[citado 2024 out. 09 ] Available from: https://doi.org/10.1016/j.abb.2003.10.018
  • Source: Archives of Biochemistry and Biophysics. Unidades: IQ, IB

    Subjects: CÁLCIO, MITOCÔNDRIAS, PEROXIDASE, OXIDAÇÃO

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      MONTEIRO, Gisele et al. Glutathione and thioredoxin peroxidase mediate susceptibility of yeast mitochondria to 'CA IND.2+'-induced damage. Archives of Biochemistry and Biophysics, v. 425, n. 1, p. 14-24, 2004Tradução . . Disponível em: https://doi.org/10.1016/j.abb.2004.03.005. Acesso em: 09 out. 2024.
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      Monteiro, G., Kowaltowski, A. J., Barros, M. H. de, & Netto, L. E. S. (2004). Glutathione and thioredoxin peroxidase mediate susceptibility of yeast mitochondria to 'CA IND.2+'-induced damage. Archives of Biochemistry and Biophysics, 425( 1), 14-24. doi:10.1016/j.abb.2004.03.005
    • NLM

      Monteiro G, Kowaltowski AJ, Barros MH de, Netto LES. Glutathione and thioredoxin peroxidase mediate susceptibility of yeast mitochondria to 'CA IND.2+'-induced damage [Internet]. Archives of Biochemistry and Biophysics. 2004 ; 425( 1): 14-24.[citado 2024 out. 09 ] Available from: https://doi.org/10.1016/j.abb.2004.03.005
    • Vancouver

      Monteiro G, Kowaltowski AJ, Barros MH de, Netto LES. Glutathione and thioredoxin peroxidase mediate susceptibility of yeast mitochondria to 'CA IND.2+'-induced damage [Internet]. Archives of Biochemistry and Biophysics. 2004 ; 425( 1): 14-24.[citado 2024 out. 09 ] Available from: https://doi.org/10.1016/j.abb.2004.03.005
  • Source: Archives of Biochemistry and Biophysics. Unidade: IQ

    Subjects: BIOQUÍMICA, DIABETES MELLITUS

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      DUTRA, Fernando e BECHARA, Etelvino José Henriques. Aminoacetone induces iron-mediated oxidative damage to isolated rat liver mitochondria. Archives of Biochemistry and Biophysics, v. 430, n. 2, p. 284-289, 2004Tradução . . Disponível em: https://doi.org/10.1016/j.abb.2004.06.029. Acesso em: 09 out. 2024.
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      Dutra, F., & Bechara, E. J. H. (2004). Aminoacetone induces iron-mediated oxidative damage to isolated rat liver mitochondria. Archives of Biochemistry and Biophysics, 430( 2), 284-289. doi:10.1016/j.abb.2004.06.029
    • NLM

      Dutra F, Bechara EJH. Aminoacetone induces iron-mediated oxidative damage to isolated rat liver mitochondria [Internet]. Archives of Biochemistry and Biophysics. 2004 ; 430( 2): 284-289.[citado 2024 out. 09 ] Available from: https://doi.org/10.1016/j.abb.2004.06.029
    • Vancouver

      Dutra F, Bechara EJH. Aminoacetone induces iron-mediated oxidative damage to isolated rat liver mitochondria [Internet]. Archives of Biochemistry and Biophysics. 2004 ; 430( 2): 284-289.[citado 2024 out. 09 ] Available from: https://doi.org/10.1016/j.abb.2004.06.029
  • Source: Archives of Biochemistry and Biophysics. Unidades: FMRP, FFCLRP

    Subjects: LECITINAS, LEGUMINOSAE

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      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 out. 2024.
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      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 2024 out. 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 2024 out. 09 ] Available from: https://doi.org/10.1016/s0003-9861(02)00695-1
  • Source: Archives of Biochemistry and Biophysics. Unidade: IQ

    Subjects: SUPERÓXIDO DISMUTASE, ALGAE, BIOQUÍMICA

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      BARROS, Marcelo Paes de et al. Temporal mismatch between induction of superoxide dismutase and ascorbate peroxidase correlates with high H2O2 concentration in seawater from clofibrate-treated red algae Kappaphyeus alvarezii. Archives of Biochemistry and Biophysics, v. 420, n. 1, p. 161-168, 2003Tradução . . Disponível em: https://doi.org/10.1016/j.abb.2003.09.014. Acesso em: 09 out. 2024.
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      Barros, M. P. de, Granbom, M., Colepicolo, P., & Pedersén, M. (2003). Temporal mismatch between induction of superoxide dismutase and ascorbate peroxidase correlates with high H2O2 concentration in seawater from clofibrate-treated red algae Kappaphyeus alvarezii. Archives of Biochemistry and Biophysics, 420( 1), 161-168. doi:10.1016/j.abb.2003.09.014
    • NLM

      Barros MP de, Granbom M, Colepicolo P, Pedersén M. Temporal mismatch between induction of superoxide dismutase and ascorbate peroxidase correlates with high H2O2 concentration in seawater from clofibrate-treated red algae Kappaphyeus alvarezii [Internet]. Archives of Biochemistry and Biophysics. 2003 ; 420( 1): 161-168.[citado 2024 out. 09 ] Available from: https://doi.org/10.1016/j.abb.2003.09.014
    • Vancouver

      Barros MP de, Granbom M, Colepicolo P, Pedersén M. Temporal mismatch between induction of superoxide dismutase and ascorbate peroxidase correlates with high H2O2 concentration in seawater from clofibrate-treated red algae Kappaphyeus alvarezii [Internet]. Archives of Biochemistry and Biophysics. 2003 ; 420( 1): 161-168.[citado 2024 out. 09 ] Available from: https://doi.org/10.1016/j.abb.2003.09.014
  • Source: Archives of Biochemistry and Biophysics. Unidade: IQ

    Subjects: BIOQUÍMICA, MEMBRANAS (BIOLOGIA), RELAÇÕES QUANTITATIVAS ENTRE ESTRUTURA QUÍMICA E ATIVIDADE BIOLÓGICA

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      NANTES, Iseli Lourenço et al. Nucleotide conformational change induced by cationic bilayers. Archives of Biochemistry and Biophysics, v. 416, n. 1, p. 25-30, 2003Tradução . . Disponível em: https://doi.org/10.1016/s0003-9861(03)00280-7. Acesso em: 09 out. 2024.
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      Nantes, I. L., Correia, F. M., Faljoni-Alario, A., Kawanani, A. E., Ishiki, H. M., Amaral, A. T. do, & Carmona-Ribeiro, A. M. (2003). Nucleotide conformational change induced by cationic bilayers. Archives of Biochemistry and Biophysics, 416( 1), 25-30. doi:10.1016/s0003-9861(03)00280-7
    • NLM

      Nantes IL, Correia FM, Faljoni-Alario A, Kawanani AE, Ishiki HM, Amaral AT do, Carmona-Ribeiro AM. Nucleotide conformational change induced by cationic bilayers [Internet]. Archives of Biochemistry and Biophysics. 2003 ; 416( 1): 25-30.[citado 2024 out. 09 ] Available from: https://doi.org/10.1016/s0003-9861(03)00280-7
    • Vancouver

      Nantes IL, Correia FM, Faljoni-Alario A, Kawanani AE, Ishiki HM, Amaral AT do, Carmona-Ribeiro AM. Nucleotide conformational change induced by cationic bilayers [Internet]. Archives of Biochemistry and Biophysics. 2003 ; 416( 1): 25-30.[citado 2024 out. 09 ] Available from: https://doi.org/10.1016/s0003-9861(03)00280-7
  • Source: Archives of Biochemistry and Biophysics. Unidade: FFCLRP

    Subjects: FOSFOLIPASES A, VENENOS, COBRAS

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      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 out. 2024.
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      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 2024 out. 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 2024 out. 09 ] Available from: https://doi.org/10.1016/s0003-9861(02)00712-9
  • Source: Archives of Biochemistry and Biophysics. Unidade: IQ

    Subjects: BIOQUÍMICA, RADICAIS LIVRES, FERRO

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      ROCHA, Maria E. M. et al. Oxidative damage to ferritin by 5-aminolevulinic acid. Archives of Biochemistry and Biophysics, v. 409, n. 2, p. 349-356, 2003Tradução . . Disponível em: https://doi.org/10.1016/s0003-9861(02)00633-1. Acesso em: 09 out. 2024.
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      Rocha, M. E. M., Dutra, F., Bandy, B., Baldini, R. L., Gomes, S. L., Faljoni-Alário, A., et al. (2003). Oxidative damage to ferritin by 5-aminolevulinic acid. Archives of Biochemistry and Biophysics, 409( 2), 349-356. doi:10.1016/s0003-9861(02)00633-1
    • NLM

      Rocha MEM, Dutra F, Bandy B, Baldini RL, Gomes SL, Faljoni-Alário A, Liria CW, Miranda MTM de, Bechara EJH. Oxidative damage to ferritin by 5-aminolevulinic acid [Internet]. Archives of Biochemistry and Biophysics. 2003 ; 409( 2): 349-356.[citado 2024 out. 09 ] Available from: https://doi.org/10.1016/s0003-9861(02)00633-1
    • Vancouver

      Rocha MEM, Dutra F, Bandy B, Baldini RL, Gomes SL, Faljoni-Alário A, Liria CW, Miranda MTM de, Bechara EJH. Oxidative damage to ferritin by 5-aminolevulinic acid [Internet]. Archives of Biochemistry and Biophysics. 2003 ; 409( 2): 349-356.[citado 2024 out. 09 ] Available from: https://doi.org/10.1016/s0003-9861(02)00633-1
  • Source: Archives of Biochemistry and Biophysics. Unidades: FFCLRP, FMRP

    Subjects: BIOQUÍMICA, BIOFÍSICA, FARMACOLOGIA

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      SOARES, Andreimar Martins et al. Dissociation of enzymatic and pharmacological properties of piratoxins-I and -III, two myotoxic phospholipases 'A IND.2' from Bothrops pirajai snake venom. Archives of Biochemistry and Biophysics, v. 387, n. 2, p. 188-196, 2001Tradução . . Disponível em: http://www.idealibrary.com/links/doi/10.1006/abbi.2000.2244/pdf. Acesso em: 09 out. 2024.
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      Soares, A. M., Andrião-Escarso, S. H., Bortoleto, R. K., Rodrigues-Simioni, L., Arni, R. K., Ward, R. J., et al. (2001). Dissociation of enzymatic and pharmacological properties of piratoxins-I and -III, two myotoxic phospholipases 'A IND.2' from Bothrops pirajai snake venom. Archives of Biochemistry and Biophysics, 387( 2), 188-196. Recuperado de http://www.idealibrary.com/links/doi/10.1006/abbi.2000.2244/pdf
    • NLM

      Soares AM, Andrião-Escarso SH, Bortoleto RK, Rodrigues-Simioni L, Arni RK, Ward RJ, Gutiérrez JM, Giglio JR. Dissociation of enzymatic and pharmacological properties of piratoxins-I and -III, two myotoxic phospholipases 'A IND.2' from Bothrops pirajai snake venom [Internet]. Archives of Biochemistry and Biophysics. 2001 ; 387( 2): 188-196.[citado 2024 out. 09 ] Available from: http://www.idealibrary.com/links/doi/10.1006/abbi.2000.2244/pdf
    • Vancouver

      Soares AM, Andrião-Escarso SH, Bortoleto RK, Rodrigues-Simioni L, Arni RK, Ward RJ, Gutiérrez JM, Giglio JR. Dissociation of enzymatic and pharmacological properties of piratoxins-I and -III, two myotoxic phospholipases 'A IND.2' from Bothrops pirajai snake venom [Internet]. Archives of Biochemistry and Biophysics. 2001 ; 387( 2): 188-196.[citado 2024 out. 09 ] Available from: http://www.idealibrary.com/links/doi/10.1006/abbi.2000.2244/pdf
  • Source: Archives of Biochemistry and Biophysics. Unidades: FM, IQ

    Subjects: DNA, PEROXIDASE, BIOQUÍMICA

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      MATOS, Humberto R. et al. Lycopene inhibits DNA damage and liver necrosis in rats treated with ferric nitrilotriacetate. Archives of Biochemistry and Biophysics, v. 396, n. 2, p. 171-177, 2001Tradução . . Disponível em: http://www.idealibrary.com/links/doi/10.1006/abbi.2001.2611/pdf. Acesso em: 09 out. 2024.
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      Matos, H. R., Capelozzi, V. L., Gomes, O. F., Di Mascio, P., & Medeiros, M. H. G. de. (2001). Lycopene inhibits DNA damage and liver necrosis in rats treated with ferric nitrilotriacetate. Archives of Biochemistry and Biophysics, 396( 2), 171-177. Recuperado de http://www.idealibrary.com/links/doi/10.1006/abbi.2001.2611/pdf
    • NLM

      Matos HR, Capelozzi VL, Gomes OF, Di Mascio P, Medeiros MHG de. Lycopene inhibits DNA damage and liver necrosis in rats treated with ferric nitrilotriacetate [Internet]. Archives of Biochemistry and Biophysics. 2001 ; 396( 2): 171-177.[citado 2024 out. 09 ] Available from: http://www.idealibrary.com/links/doi/10.1006/abbi.2001.2611/pdf
    • Vancouver

      Matos HR, Capelozzi VL, Gomes OF, Di Mascio P, Medeiros MHG de. Lycopene inhibits DNA damage and liver necrosis in rats treated with ferric nitrilotriacetate [Internet]. Archives of Biochemistry and Biophysics. 2001 ; 396( 2): 171-177.[citado 2024 out. 09 ] Available from: http://www.idealibrary.com/links/doi/10.1006/abbi.2001.2611/pdf
  • Source: Archives of Biochemistry and Biophysics. Unidades: FCF, IQ

    Assunto: QUÍMICA ORGÂNICA

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      XIMENES, Valdecir Farias e CAMPA, Ana e CATALANI, Luiz Henrique. The oxidation of indole derivatives catalyzed by horseradish peroxidase is highly chemiluminescent. Archives of Biochemistry and Biophysics, v. 387, n. 2, p. 173-179, 2001Tradução . . Disponível em: http://www.idealibrary.com/links/doi/10.1006/abbi.2000.2228/pdf. Acesso em: 09 out. 2024.
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      Ximenes, V. F., Campa, A., & Catalani, L. H. (2001). The oxidation of indole derivatives catalyzed by horseradish peroxidase is highly chemiluminescent. Archives of Biochemistry and Biophysics, 387( 2), 173-179. Recuperado de http://www.idealibrary.com/links/doi/10.1006/abbi.2000.2228/pdf
    • NLM

      Ximenes VF, Campa A, Catalani LH. The oxidation of indole derivatives catalyzed by horseradish peroxidase is highly chemiluminescent [Internet]. Archives of Biochemistry and Biophysics. 2001 ; 387( 2): 173-179.[citado 2024 out. 09 ] Available from: http://www.idealibrary.com/links/doi/10.1006/abbi.2000.2228/pdf
    • Vancouver

      Ximenes VF, Campa A, Catalani LH. The oxidation of indole derivatives catalyzed by horseradish peroxidase is highly chemiluminescent [Internet]. Archives of Biochemistry and Biophysics. 2001 ; 387( 2): 173-179.[citado 2024 out. 09 ] Available from: http://www.idealibrary.com/links/doi/10.1006/abbi.2000.2228/pdf

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