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  • Source: Biophysical Journal. Unidades: IQ, IFSC

    Subjects: RESSONÂNCIA PARAMAGNÉTICA ELETRÔNICA, FERRO, ESPECTROSCOPIA RAMAN, MITOCÔNDRIAS, REDUÇÃO

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      MUGNOL, Katia Cristina Ugolini et al. Spectroscopic, structural, and functional characterization of the alternative low-spin state of horse heart cytochrome c. Biophysical Journal, v. 94, n. 10, p. 4066-4077, 2008Tradução . . Acesso em: 01 nov. 2024.
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      Mugnol, K. C. U., Ando, R. A., Nagayasu, R. Y., Faljoni-Alário, A., Brochsztain, S., Santos, P. S., et al. (2008). Spectroscopic, structural, and functional characterization of the alternative low-spin state of horse heart cytochrome c. Biophysical Journal, 94( 10), 4066-4077.
    • NLM

      Mugnol KCU, Ando RA, Nagayasu RY, Faljoni-Alário A, Brochsztain S, Santos PS, Nascimento OR, Nantes IL. Spectroscopic, structural, and functional characterization of the alternative low-spin state of horse heart cytochrome c. Biophysical Journal. 2008 ; 94( 10): 4066-4077.[citado 2024 nov. 01 ]
    • Vancouver

      Mugnol KCU, Ando RA, Nagayasu RY, Faljoni-Alário A, Brochsztain S, Santos PS, Nascimento OR, Nantes IL. Spectroscopic, structural, and functional characterization of the alternative low-spin state of horse heart cytochrome c. Biophysical Journal. 2008 ; 94( 10): 4066-4077.[citado 2024 nov. 01 ]
  • Source: Bioconjugate Chemistry. Unidade: IQ

    Subjects: PROTEÍNAS DE FLUORESCÊNCIA VERDE, BIOQUÍMICA

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      HERING, Vitor Renaux et al. Energy transfer between CdSe/ZnS Core/Shell quantum dots and fluorescent proteins. Bioconjugate Chemistry, v. 18, n. 6, p. 1705-1708, 2007Tradução . . Acesso em: 01 nov. 2024.
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      Hering, V. R., Gibson, G., Schumacher, R. I., Faljoni-Alario, A., & Politi, M. J. (2007). Energy transfer between CdSe/ZnS Core/Shell quantum dots and fluorescent proteins. Bioconjugate Chemistry, 18( 6), 1705-1708.
    • NLM

      Hering VR, Gibson G, Schumacher RI, Faljoni-Alario A, Politi MJ. Energy transfer between CdSe/ZnS Core/Shell quantum dots and fluorescent proteins. Bioconjugate Chemistry. 2007 ; 18( 6): 1705-1708.[citado 2024 nov. 01 ]
    • Vancouver

      Hering VR, Gibson G, Schumacher RI, Faljoni-Alario A, Politi MJ. Energy transfer between CdSe/ZnS Core/Shell quantum dots and fluorescent proteins. Bioconjugate Chemistry. 2007 ; 18( 6): 1705-1708.[citado 2024 nov. 01 ]
  • Source: Journal of Biological Chemistry. Unidades: IFSC, IQ

    Subjects: RADICAIS LIVRES, MOLÉCULA, OXIGÊNIO

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      ESTEVAM, Mauren L. et al. Changes in the spin state and reactivity of cytochrome c induced by photochemically generated singlet oxygen and free radicals. Journal of Biological Chemistry, v. 279, n. 38, p. Se 2004, 2004Tradução . . Disponível em: https://doi.org/10.1074/jbc.M402093200. Acesso em: 01 nov. 2024.
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      Estevam, M. L., Nascimento, O. R., Baptista, M. da S., Di Mascio, P., Prado, F. M., Faljoni-Alario, A., et al. (2004). Changes in the spin state and reactivity of cytochrome c induced by photochemically generated singlet oxygen and free radicals. Journal of Biological Chemistry, 279( 38), Se 2004. doi:10.1074/jbc.M402093200
    • NLM

      Estevam ML, Nascimento OR, Baptista M da S, Di Mascio P, Prado FM, Faljoni-Alario A, Zucchi M do R, Nantes IL. Changes in the spin state and reactivity of cytochrome c induced by photochemically generated singlet oxygen and free radicals [Internet]. Journal of Biological Chemistry. 2004 ; 279( 38): Se 2004.[citado 2024 nov. 01 ] Available from: https://doi.org/10.1074/jbc.M402093200
    • Vancouver

      Estevam ML, Nascimento OR, Baptista M da S, Di Mascio P, Prado FM, Faljoni-Alario A, Zucchi M do R, Nantes IL. Changes in the spin state and reactivity of cytochrome c induced by photochemically generated singlet oxygen and free radicals [Internet]. Journal of Biological Chemistry. 2004 ; 279( 38): Se 2004.[citado 2024 nov. 01 ] Available from: https://doi.org/10.1074/jbc.M402093200
  • Source: Journal of Physical Chemistry B. Unidades: IFSC, IQ

    Subjects: ENZIMAS, BIOFÍSICA

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      PRIETO, Tatiana et al. Microperoxidase-8 associated to CTAB micelles: a new catalyst with peroxidase activity. Journal of Physical Chemistry B, v. 108, n. 30, p. 11124-11132, 2004Tradução . . Acesso em: 01 nov. 2024.
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      Prieto, T., Nascimento, O. R., Tersariol, I. L. S., Faljoni-Alario, A., & Nantes, I. L. (2004). Microperoxidase-8 associated to CTAB micelles: a new catalyst with peroxidase activity. Journal of Physical Chemistry B, 108( 30), 11124-11132.
    • NLM

      Prieto T, Nascimento OR, Tersariol ILS, Faljoni-Alario A, Nantes IL. Microperoxidase-8 associated to CTAB micelles: a new catalyst with peroxidase activity. Journal of Physical Chemistry B. 2004 ; 108( 30): 11124-11132.[citado 2024 nov. 01 ]
    • Vancouver

      Prieto T, Nascimento OR, Tersariol ILS, Faljoni-Alario A, Nantes IL. Microperoxidase-8 associated to CTAB micelles: a new catalyst with peroxidase activity. Journal of Physical Chemistry B. 2004 ; 108( 30): 11124-11132.[citado 2024 nov. 01 ]
  • 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: 01 nov. 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 nov. 01 ] 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 nov. 01 ] Available from: https://doi.org/10.1016/s0003-9861(03)00280-7
  • 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: 01 nov. 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
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      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 nov. 01 ] 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 nov. 01 ] Available from: https://doi.org/10.1016/s0003-9861(02)00633-1
  • Source: Journal of Biological Chemistry. Unidade: IQ

    Assunto: BIOQUÍMICA

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      ALMEIDA, Paulo C. et al. Cathepsin B activity regulation heparin-like glycosaminoglycans protect human cathepsin B from alkaline pH-induced inactivation. Journal of Biological Chemistry, v. 276, n. 2, p. 944-951, 2001Tradução . . Acesso em: 01 nov. 2024.
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      Almeida, P. C., Nantes, I. L., Chagas, J. R., Rizzi, C. C. A., Faljoni-Alario, A., Carmona, E., et al. (2001). Cathepsin B activity regulation heparin-like glycosaminoglycans protect human cathepsin B from alkaline pH-induced inactivation. Journal of Biological Chemistry, 276( 2), 944-951.
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      Almeida PC, Nantes IL, Chagas JR, Rizzi CCA, Faljoni-Alario A, Carmona E, Juliano L, Nader HB, Tersariol ILS. Cathepsin B activity regulation heparin-like glycosaminoglycans protect human cathepsin B from alkaline pH-induced inactivation. Journal of Biological Chemistry. 2001 ; 276( 2): 944-951.[citado 2024 nov. 01 ]
    • Vancouver

      Almeida PC, Nantes IL, Chagas JR, Rizzi CCA, Faljoni-Alario A, Carmona E, Juliano L, Nader HB, Tersariol ILS. Cathepsin B activity regulation heparin-like glycosaminoglycans protect human cathepsin B from alkaline pH-induced inactivation. Journal of Biological Chemistry. 2001 ; 276( 2): 944-951.[citado 2024 nov. 01 ]
  • Source: Journal of Biological Chemistry. Unidades: IFSC, IQ

    Subjects: BIOQUÍMICA, OXIDAÇÃO

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      NANTES, Iseli L. et al. Effect of heme iron valence state on the conformation of cytochrome c and its association with membrane interfaces: a CD and EPR investigation. Journal of Biological Chemistry, v. 276, n. 1, p. 153-158, 2001Tradução . . Disponível em: https://doi.org/10.1074/jbc.M006338200. Acesso em: 01 nov. 2024.
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      Nantes, I. L., Zucchi, M. do R., Nascimento, O. R., & Faljoni-Alario, A. (2001). Effect of heme iron valence state on the conformation of cytochrome c and its association with membrane interfaces: a CD and EPR investigation. Journal of Biological Chemistry, 276( 1), 153-158. doi:10.1074/jbc.M006338200
    • NLM

      Nantes IL, Zucchi M do R, Nascimento OR, Faljoni-Alario A. Effect of heme iron valence state on the conformation of cytochrome c and its association with membrane interfaces: a CD and EPR investigation [Internet]. Journal of Biological Chemistry. 2001 ; 276( 1): 153-158.[citado 2024 nov. 01 ] Available from: https://doi.org/10.1074/jbc.M006338200
    • Vancouver

      Nantes IL, Zucchi M do R, Nascimento OR, Faljoni-Alario A. Effect of heme iron valence state on the conformation of cytochrome c and its association with membrane interfaces: a CD and EPR investigation [Internet]. Journal of Biological Chemistry. 2001 ; 276( 1): 153-158.[citado 2024 nov. 01 ] Available from: https://doi.org/10.1074/jbc.M006338200
  • Source: Free Radical Biology and Medicine. Unidades: IQ, IFSC

    Assunto: BIOQUÍMICA

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      NANTES, Iseli L. et al. Modifications in heme iron of free and vesicle bound cytochrome c by tert-butyl hydroperoxide: a magnetic circular dichroism and electron paramagnetic resonance investigation. Free Radical Biology and Medicine, v. 28, n. 5, p. 786-796, 2000Tradução . . Disponível em: https://doi.org/10.1016/s0891-5849(00)00170-2. Acesso em: 01 nov. 2024.
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      Nantes, I. L., Faljoni-Alario, A., Nascimento, O. R., Bandy, B., Gatti, R., & Bechara, E. J. H. (2000). Modifications in heme iron of free and vesicle bound cytochrome c by tert-butyl hydroperoxide: a magnetic circular dichroism and electron paramagnetic resonance investigation. Free Radical Biology and Medicine, 28( 5), 786-796. doi:10.1016/s0891-5849(00)00170-2
    • NLM

      Nantes IL, Faljoni-Alario A, Nascimento OR, Bandy B, Gatti R, Bechara EJH. Modifications in heme iron of free and vesicle bound cytochrome c by tert-butyl hydroperoxide: a magnetic circular dichroism and electron paramagnetic resonance investigation [Internet]. Free Radical Biology and Medicine. 2000 ; 28( 5): 786-796.[citado 2024 nov. 01 ] Available from: https://doi.org/10.1016/s0891-5849(00)00170-2
    • Vancouver

      Nantes IL, Faljoni-Alario A, Nascimento OR, Bandy B, Gatti R, Bechara EJH. Modifications in heme iron of free and vesicle bound cytochrome c by tert-butyl hydroperoxide: a magnetic circular dichroism and electron paramagnetic resonance investigation [Internet]. Free Radical Biology and Medicine. 2000 ; 28( 5): 786-796.[citado 2024 nov. 01 ] Available from: https://doi.org/10.1016/s0891-5849(00)00170-2
  • Conference titles: Rocky Mountain Conference on Analytical Chemistry. Unidades: IQ, IFSC

    Assunto: BIOQUÍMICA

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      ZUCCHI, Maria do Rosário et al. Study of cytochrome-c and membranes by CW-EPR of iron heme. 1999, Anais.. Denver: Instituto de Química, Universidade de São Paulo, 1999. . Acesso em: 01 nov. 2024.
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      Zucchi, M. do R., Nantes, I. L., Faljoni-Alario, A., & Nascimento, O. R. (1999). Study of cytochrome-c and membranes by CW-EPR of iron heme. In . Denver: Instituto de Química, Universidade de São Paulo.
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      Zucchi M do R, Nantes IL, Faljoni-Alario A, Nascimento OR. Study of cytochrome-c and membranes by CW-EPR of iron heme. 1999 ;[citado 2024 nov. 01 ]
    • Vancouver

      Zucchi M do R, Nantes IL, Faljoni-Alario A, Nascimento OR. Study of cytochrome-c and membranes by CW-EPR of iron heme. 1999 ;[citado 2024 nov. 01 ]
  • Source: Journal of Inorganic Biochemistry. Unidade: IQ

    Subjects: QUÍMICA INORGÂNICA, BIOQUÍMICA

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      ESPÓSITO, Breno Pannia et al. A circular dichroism and fluorescence quenching study of the interactions between rhodium(II) complexes and human serum albumin. Journal of Inorganic Biochemistry, v. 75, n. 1, p. 55-61, 1999Tradução . . Disponível em: https://doi.org/10.1016/s0162-0134(99)00032-x. Acesso em: 01 nov. 2024.
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      Espósito, B. P., Faljoni-Alário, A., Menezes, J. F. S. de, Brito, H. F. de, & Najjar, R. (1999). A circular dichroism and fluorescence quenching study of the interactions between rhodium(II) complexes and human serum albumin. Journal of Inorganic Biochemistry, 75( 1), 55-61. doi:10.1016/s0162-0134(99)00032-x
    • NLM

      Espósito BP, Faljoni-Alário A, Menezes JFS de, Brito HF de, Najjar R. A circular dichroism and fluorescence quenching study of the interactions between rhodium(II) complexes and human serum albumin [Internet]. Journal of Inorganic Biochemistry. 1999 ; 75( 1): 55-61.[citado 2024 nov. 01 ] Available from: https://doi.org/10.1016/s0162-0134(99)00032-x
    • Vancouver

      Espósito BP, Faljoni-Alário A, Menezes JFS de, Brito HF de, Najjar R. A circular dichroism and fluorescence quenching study of the interactions between rhodium(II) complexes and human serum albumin [Internet]. Journal of Inorganic Biochemistry. 1999 ; 75( 1): 55-61.[citado 2024 nov. 01 ] Available from: https://doi.org/10.1016/s0162-0134(99)00032-x
  • Source: Free Radical Biology Medicine. Unidade: IQ

    Assunto: BIOQUÍMICA

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      NANTES, I L et al. Liposome effect on the cytochrome C-catalyzed peroxidation of carbonyl substrates to triplet species. Free Radical Biology Medicine, v. 25, p. 546-553, 1998Tradução . . Disponível em: https://doi.org/10.1016/s0891-5849(98)00082-3. Acesso em: 01 nov. 2024.
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      Nantes, I. L., Faljoni-Alario, A., Vercesi, A. E., Santos, K. E., & Bechara, E. J. H. (1998). Liposome effect on the cytochrome C-catalyzed peroxidation of carbonyl substrates to triplet species. Free Radical Biology Medicine, 25, 546-553. doi:10.1016/s0891-5849(98)00082-3
    • NLM

      Nantes IL, Faljoni-Alario A, Vercesi AE, Santos KE, Bechara EJH. Liposome effect on the cytochrome C-catalyzed peroxidation of carbonyl substrates to triplet species [Internet]. Free Radical Biology Medicine. 1998 ; 25 546-553.[citado 2024 nov. 01 ] Available from: https://doi.org/10.1016/s0891-5849(98)00082-3
    • Vancouver

      Nantes IL, Faljoni-Alario A, Vercesi AE, Santos KE, Bechara EJH. Liposome effect on the cytochrome C-catalyzed peroxidation of carbonyl substrates to triplet species [Internet]. Free Radical Biology Medicine. 1998 ; 25 546-553.[citado 2024 nov. 01 ] Available from: https://doi.org/10.1016/s0891-5849(98)00082-3
  • Source: Journal of Inorganic Biochemistry. Unidade: IQ

    Subjects: QUÍMICA INORGÂNICA, BIOQUÍMICA

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      SANTOS, M L P et al. Antioxidant and pro-oxidant properties of some di-schiff base copper (II) complexes. Journal of Inorganic Biochemistry, v. 71, n. 1/2, p. 71-78, 1998Tradução . . Disponível em: https://doi.org/10.1016/s0162-0134(98)10034-x. Acesso em: 01 nov. 2024.
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      Santos, M. L. P., Faljoni-Alario, A., Mangrich, A. S., & Ferreira, A. M. da C. (1998). Antioxidant and pro-oxidant properties of some di-schiff base copper (II) complexes. Journal of Inorganic Biochemistry, 71( 1/2), 71-78. doi:10.1016/s0162-0134(98)10034-x
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      Santos MLP, Faljoni-Alario A, Mangrich AS, Ferreira AM da C. Antioxidant and pro-oxidant properties of some di-schiff base copper (II) complexes [Internet]. Journal of Inorganic Biochemistry. 1998 ; 71( 1/2): 71-78.[citado 2024 nov. 01 ] Available from: https://doi.org/10.1016/s0162-0134(98)10034-x
    • Vancouver

      Santos MLP, Faljoni-Alario A, Mangrich AS, Ferreira AM da C. Antioxidant and pro-oxidant properties of some di-schiff base copper (II) complexes [Internet]. Journal of Inorganic Biochemistry. 1998 ; 71( 1/2): 71-78.[citado 2024 nov. 01 ] Available from: https://doi.org/10.1016/s0162-0134(98)10034-x
  • Source: Faseb Journal. Conference titles: International Congress of Biochemistry and Molecular Biology. Unidade: IQ

    Assunto: BIOQUÍMICA

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      BANDY, B. et al. Peroxide-induced bleaching of cytochrome C: interactions of ascorbate and urate. Faseb Journal. Bethesda: Instituto de Química, Universidade de São Paulo. . Acesso em: 01 nov. 2024. , 1997
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      Bandy, B., Nates, I., Faljoni-Alario, A., & Bechara, E. J. H. (1997). Peroxide-induced bleaching of cytochrome C: interactions of ascorbate and urate. Faseb Journal. Bethesda: Instituto de Química, Universidade de São Paulo.
    • NLM

      Bandy B, Nates I, Faljoni-Alario A, Bechara EJH. Peroxide-induced bleaching of cytochrome C: interactions of ascorbate and urate. Faseb Journal. 1997 ; 11( 9): 1084 res. 1334.[citado 2024 nov. 01 ]
    • Vancouver

      Bandy B, Nates I, Faljoni-Alario A, Bechara EJH. Peroxide-induced bleaching of cytochrome C: interactions of ascorbate and urate. Faseb Journal. 1997 ; 11( 9): 1084 res. 1334.[citado 2024 nov. 01 ]
  • Source: Abstracts. Conference titles: Annual Meeting of the Oxygen Society. Unidade: IQ

    Assunto: BIOQUÍMICA

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      BANDY, B et al. Peroxide - induced bleaching of cytochrome c interactions of ascorbate urate, and phospholipid vesicles. 1996, Anais.. Miami Beach: Instituto de Química, Universidade de São Paulo, 1996. . Acesso em: 01 nov. 2024.
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      Bandy, B., Nantes, I. L., Faljoni-Alario, A., & Bechara, E. J. H. (1996). Peroxide - induced bleaching of cytochrome c interactions of ascorbate urate, and phospholipid vesicles. In Abstracts. Miami Beach: Instituto de Química, Universidade de São Paulo.
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      Bandy B, Nantes IL, Faljoni-Alario A, Bechara EJH. Peroxide - induced bleaching of cytochrome c interactions of ascorbate urate, and phospholipid vesicles. Abstracts. 1996 ;[citado 2024 nov. 01 ]
    • Vancouver

      Bandy B, Nantes IL, Faljoni-Alario A, Bechara EJH. Peroxide - induced bleaching of cytochrome c interactions of ascorbate urate, and phospholipid vesicles. Abstracts. 1996 ;[citado 2024 nov. 01 ]
  • Source: Abstracts. Conference titles: Annual Meeting of the Oxygen Society. Unidade: IQ

    Assunto: BIOQUÍMICA

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      BANDY, B et al. Peroxide -induced bleaching of cytochrone c and production of radicals: influences of phosphate and liposomes. 1996, Anais.. Miami Beach: Instituto de Química, Universidade de São Paulo, 1996. . Acesso em: 01 nov. 2024.
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      Bandy, B., Nantes, I. L., Gatti, R., Faljoni-Alario, A., & Bechara, E. J. H. (1996). Peroxide -induced bleaching of cytochrone c and production of radicals: influences of phosphate and liposomes. In Abstracts. Miami Beach: Instituto de Química, Universidade de São Paulo.
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      Bandy B, Nantes IL, Gatti R, Faljoni-Alario A, Bechara EJH. Peroxide -induced bleaching of cytochrone c and production of radicals: influences of phosphate and liposomes. Abstracts. 1996 ;[citado 2024 nov. 01 ]
    • Vancouver

      Bandy B, Nantes IL, Gatti R, Faljoni-Alario A, Bechara EJH. Peroxide -induced bleaching of cytochrone c and production of radicals: influences of phosphate and liposomes. Abstracts. 1996 ;[citado 2024 nov. 01 ]
  • Source: Journal of Pharmaceutical Sciences. Unidades: IQ, IF

    Assunto: BIOFÍSICA

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      LAMY, Maria Teresa Moura et al. Effect of aggregation on the kinetics of autoxidation of the polyene antibiotic amphotericin-b. Journal of Pharmaceutical Sciences, v. fe 1993, n. 2 , p. 162-6, 1993Tradução . . Acesso em: 01 nov. 2024.
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      Lamy, M. T. M., Ferreira, V. F. N., Faljoni-Alario, A., & Schreier, S. (1993). Effect of aggregation on the kinetics of autoxidation of the polyene antibiotic amphotericin-b. Journal of Pharmaceutical Sciences, fe 1993( 2 ), 162-6.
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      Lamy MTM, Ferreira VFN, Faljoni-Alario A, Schreier S. Effect of aggregation on the kinetics of autoxidation of the polyene antibiotic amphotericin-b. Journal of Pharmaceutical Sciences. 1993 ; fe 1993( 2 ): 162-6.[citado 2024 nov. 01 ]
    • Vancouver

      Lamy MTM, Ferreira VFN, Faljoni-Alario A, Schreier S. Effect of aggregation on the kinetics of autoxidation of the polyene antibiotic amphotericin-b. Journal of Pharmaceutical Sciences. 1993 ; fe 1993( 2 ): 162-6.[citado 2024 nov. 01 ]
  • Source: Photochemistry and Photobiology. Unidade: IQ

    Assunto: BIOFÍSICA

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      SILVA, E et al. Excitation of mesophyll and bundle sheat chloroplasts of atriplex repanda in the absence of light. Photochemistry and Photobiology, v. 53, p. 271-4, 1991Tradução . . Acesso em: 01 nov. 2024.
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      Silva, E., Rodrigues, G., Faljoni-Alario, A., & Cilento, G. (1991). Excitation of mesophyll and bundle sheat chloroplasts of atriplex repanda in the absence of light. Photochemistry and Photobiology, 53, 271-4.
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      Silva E, Rodrigues G, Faljoni-Alario A, Cilento G. Excitation of mesophyll and bundle sheat chloroplasts of atriplex repanda in the absence of light. Photochemistry and Photobiology. 1991 ;53 271-4.[citado 2024 nov. 01 ]
    • Vancouver

      Silva E, Rodrigues G, Faljoni-Alario A, Cilento G. Excitation of mesophyll and bundle sheat chloroplasts of atriplex repanda in the absence of light. Photochemistry and Photobiology. 1991 ;53 271-4.[citado 2024 nov. 01 ]
  • Source: Archives of Biochemistry and Biophysics. Unidade: IQ

    Subjects: BIOFÍSICA, BIOQUÍMICA

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    • ABNT

      SILVA, E e EDWARDS, A M e FALJONI-ALARIO, A. Enzymatic generation of triplet acetone by deglycosylated horseradish peroxidase. Archives of Biochemistry and Biophysics, v. 276, n. 2 , p. 527-30, 1990Tradução . . Disponível em: https://doi.org/10.1016/0003-9861(90)90754-m. Acesso em: 01 nov. 2024.
    • APA

      Silva, E., Edwards, A. M., & Faljoni-Alario, A. (1990). Enzymatic generation of triplet acetone by deglycosylated horseradish peroxidase. Archives of Biochemistry and Biophysics, 276( 2 ), 527-30. doi:10.1016/0003-9861(90)90754-m
    • NLM

      Silva E, Edwards AM, Faljoni-Alario A. Enzymatic generation of triplet acetone by deglycosylated horseradish peroxidase [Internet]. Archives of Biochemistry and Biophysics. 1990 ;276( 2 ): 527-30.[citado 2024 nov. 01 ] Available from: https://doi.org/10.1016/0003-9861(90)90754-m
    • Vancouver

      Silva E, Edwards AM, Faljoni-Alario A. Enzymatic generation of triplet acetone by deglycosylated horseradish peroxidase [Internet]. Archives of Biochemistry and Biophysics. 1990 ;276( 2 ): 527-30.[citado 2024 nov. 01 ] Available from: https://doi.org/10.1016/0003-9861(90)90754-m

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