Filtros : "Archives of Biochemistry and Biophysics" "2014" Limpar

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

    Subjects: DANO AO DNA, MELANINAS

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    • ABNT

      PELLOSI, Maria Carolina et al. Effects of the melanin precursor 5,6-dihydroxy-indole-2-carboxylic acid (DHICA) on DNA damage and repair in the presence of reactive oxygen species. Archives of Biochemistry and Biophysics, v. 557, p. 55-64, 2014Tradução . . Disponível em: https://doi.org/10.1016/j.abb.2014.05.024. Acesso em: 08 nov. 2025.
    • APA

      Pellosi, M. C., Suzukawa, A. A., Scalfo, A. C., Di Mascio, P., Pereira, C. P. M., Souza-Pinto, N. C. de, et al. (2014). Effects of the melanin precursor 5,6-dihydroxy-indole-2-carboxylic acid (DHICA) on DNA damage and repair in the presence of reactive oxygen species. Archives of Biochemistry and Biophysics, 557, 55-64. doi:10.1016/j.abb.2014.05.024
    • NLM

      Pellosi MC, Suzukawa AA, Scalfo AC, Di Mascio P, Pereira CPM, Souza-Pinto NC de, Martins D de L, Martinez GR. Effects of the melanin precursor 5,6-dihydroxy-indole-2-carboxylic acid (DHICA) on DNA damage and repair in the presence of reactive oxygen species [Internet]. Archives of Biochemistry and Biophysics. 2014 ; 557 55-64.[citado 2025 nov. 08 ] Available from: https://doi.org/10.1016/j.abb.2014.05.024
    • Vancouver

      Pellosi MC, Suzukawa AA, Scalfo AC, Di Mascio P, Pereira CPM, Souza-Pinto NC de, Martins D de L, Martinez GR. Effects of the melanin precursor 5,6-dihydroxy-indole-2-carboxylic acid (DHICA) on DNA damage and repair in the presence of reactive oxygen species [Internet]. Archives of Biochemistry and Biophysics. 2014 ; 557 55-64.[citado 2025 nov. 08 ] Available from: https://doi.org/10.1016/j.abb.2014.05.024
  • Source: Archives of Biochemistry and Biophysics. Unidade: ICB

    Assunto: ANATOMIA

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    • ABNT

      PAIVA, Katiucia Batista da Silva e GRANJEIRO, José Mauro. Bone tissue remodeling and development: focus on matrix metalloproteinase functions. Archives of Biochemistry and Biophysics, v. 561, p. 74-87, 2014Tradução . . Disponível em: https://doi.org/10.1016/j.abb.2014.07.034. Acesso em: 08 nov. 2025.
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      Paiva, K. B. da S., & Granjeiro, J. M. (2014). Bone tissue remodeling and development: focus on matrix metalloproteinase functions. Archives of Biochemistry and Biophysics, 561, 74-87. doi:10.1016/j.abb.2014.07.034
    • NLM

      Paiva KB da S, Granjeiro JM. Bone tissue remodeling and development: focus on matrix metalloproteinase functions [Internet]. Archives of Biochemistry and Biophysics. 2014 ; 561 74-87.[citado 2025 nov. 08 ] Available from: https://doi.org/10.1016/j.abb.2014.07.034
    • Vancouver

      Paiva KB da S, Granjeiro JM. Bone tissue remodeling and development: focus on matrix metalloproteinase functions [Internet]. Archives of Biochemistry and Biophysics. 2014 ; 561 74-87.[citado 2025 nov. 08 ] Available from: https://doi.org/10.1016/j.abb.2014.07.034
  • Source: Archives of Biochemistry and Biophysics. Unidades: IF, IB

    Subjects: METABOLISMO DE PROTEÍNA, SACCHAROMYCES, PROTEÍNAS, BIOQUÍMICA CELULAR, LEVEDURAS

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    • ABNT

      DEMASI, Marilene et al. 20S proteasome activity is modified via S-glutathionylation based on intracellular redox status of the yeast Saccharomyces cerevisiae: implications for the degradation of oxidized proteins. Archives of Biochemistry and Biophysics, v. online, p. on-line, 2014Tradução . . Disponível em: https://doi.org/10.1016/j.abb.2014.05.002. Acesso em: 08 nov. 2025.
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      Demasi, M., Hand, A., Ohara, E., Oliveira, C. L. P. de, Bicev, R. N., Bertoncini, C. A., & Netto, L. E. S. (2014). 20S proteasome activity is modified via S-glutathionylation based on intracellular redox status of the yeast Saccharomyces cerevisiae: implications for the degradation of oxidized proteins. Archives of Biochemistry and Biophysics, online, on-line. doi:10.1016/j.abb.2014.05.002
    • NLM

      Demasi M, Hand A, Ohara E, Oliveira CLP de, Bicev RN, Bertoncini CA, Netto LES. 20S proteasome activity is modified via S-glutathionylation based on intracellular redox status of the yeast Saccharomyces cerevisiae: implications for the degradation of oxidized proteins [Internet]. Archives of Biochemistry and Biophysics. 2014 ; online on-line.[citado 2025 nov. 08 ] Available from: https://doi.org/10.1016/j.abb.2014.05.002
    • Vancouver

      Demasi M, Hand A, Ohara E, Oliveira CLP de, Bicev RN, Bertoncini CA, Netto LES. 20S proteasome activity is modified via S-glutathionylation based on intracellular redox status of the yeast Saccharomyces cerevisiae: implications for the degradation of oxidized proteins [Internet]. Archives of Biochemistry and Biophysics. 2014 ; online on-line.[citado 2025 nov. 08 ] Available from: https://doi.org/10.1016/j.abb.2014.05.002
  • Source: Archives of Biochemistry and Biophysics. Unidade: IQ

    Subjects: SUPERÓXIDO DISMUTASE, DOENÇAS NEURODEGENERATIVAS

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    • ABNT

      IQBAL, Asif et al. Oxidation, inactivation and aggregation of protein disulfide isomerase promoted by the bicarbonate dependent peroxidase activity of human superoxide dismutase. Archives of Biochemistry and Biophysics, v. 557, p. 72-81, 2014Tradução . . Disponível em: https://doi.org/10.1016/j.abb.2014.06.013. Acesso em: 08 nov. 2025.
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      Iqbal, A., Paviani, V., Moretti, A. I. S., Laurindo, F. R. M., & Augusto, O. (2014). Oxidation, inactivation and aggregation of protein disulfide isomerase promoted by the bicarbonate dependent peroxidase activity of human superoxide dismutase. Archives of Biochemistry and Biophysics, 557, 72-81. doi:10.1016/j.abb.2014.06.013
    • NLM

      Iqbal A, Paviani V, Moretti AIS, Laurindo FRM, Augusto O. Oxidation, inactivation and aggregation of protein disulfide isomerase promoted by the bicarbonate dependent peroxidase activity of human superoxide dismutase [Internet]. Archives of Biochemistry and Biophysics. 2014 ; 557 72-81.[citado 2025 nov. 08 ] Available from: https://doi.org/10.1016/j.abb.2014.06.013
    • Vancouver

      Iqbal A, Paviani V, Moretti AIS, Laurindo FRM, Augusto O. Oxidation, inactivation and aggregation of protein disulfide isomerase promoted by the bicarbonate dependent peroxidase activity of human superoxide dismutase [Internet]. Archives of Biochemistry and Biophysics. 2014 ; 557 72-81.[citado 2025 nov. 08 ] Available from: https://doi.org/10.1016/j.abb.2014.06.013
  • Source: Archives of Biochemistry and Biophysics. Unidade: IQ

    Subjects: PROCESSOS QUÍMICOS, BIOQUÍMICA, ANTIOXIDANTES

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    • ABNT

      MIYAMOTO, Sayuri e TERAO, Junji. Antioxidants and redox processes in health: bilateral meeting Brazil-Japan [Editorial]. Archives of Biochemistry and Biophysics. New York: Instituto de Química, Universidade de São Paulo. Disponível em: https://doi.org/10.1016/j.abb.2014.07.007. Acesso em: 08 nov. 2025. , 2014
    • APA

      Miyamoto, S., & Terao, J. (2014). Antioxidants and redox processes in health: bilateral meeting Brazil-Japan [Editorial]. Archives of Biochemistry and Biophysics. New York: Instituto de Química, Universidade de São Paulo. doi:10.1016/j.abb.2014.07.007
    • NLM

      Miyamoto S, Terao J. Antioxidants and redox processes in health: bilateral meeting Brazil-Japan [Editorial] [Internet]. Archives of Biochemistry and Biophysics. 2014 ; 557 1-2.[citado 2025 nov. 08 ] Available from: https://doi.org/10.1016/j.abb.2014.07.007
    • Vancouver

      Miyamoto S, Terao J. Antioxidants and redox processes in health: bilateral meeting Brazil-Japan [Editorial] [Internet]. Archives of Biochemistry and Biophysics. 2014 ; 557 1-2.[citado 2025 nov. 08 ] Available from: https://doi.org/10.1016/j.abb.2014.07.007
  • Source: Archives of Biochemistry and Biophysics. Unidade: FFCLRP

    Subjects: CALORÍMETROS, ENZIMAS, MEMBRANAS CELULARES, LIPÍDEOS DA MEMBRANA

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      YONEDA, Juliana Sakamoto et al. Na, K-ATPase reconstituted in ternary liposome: the presence of cholesterol affects protein activity and thermal stability. Archives of Biochemistry and Biophysics, v. 564, p. 136-141, 2014Tradução . . Disponível em: https://doi.org/10.1016/j.abb.2014.09.015. Acesso em: 08 nov. 2025.
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      Yoneda, J. S., Rigos, C. F., Lourenço, T. F. A. de, Sebinelli, H. G., & Ciancaglini, P. (2014). Na, K-ATPase reconstituted in ternary liposome: the presence of cholesterol affects protein activity and thermal stability. Archives of Biochemistry and Biophysics, 564, 136-141. doi:10.1016/j.abb.2014.09.015
    • NLM

      Yoneda JS, Rigos CF, Lourenço TFA de, Sebinelli HG, Ciancaglini P. Na, K-ATPase reconstituted in ternary liposome: the presence of cholesterol affects protein activity and thermal stability [Internet]. Archives of Biochemistry and Biophysics. 2014 ; 564 136-141.[citado 2025 nov. 08 ] Available from: https://doi.org/10.1016/j.abb.2014.09.015
    • Vancouver

      Yoneda JS, Rigos CF, Lourenço TFA de, Sebinelli HG, Ciancaglini P. Na, K-ATPase reconstituted in ternary liposome: the presence of cholesterol affects protein activity and thermal stability [Internet]. Archives of Biochemistry and Biophysics. 2014 ; 564 136-141.[citado 2025 nov. 08 ] Available from: https://doi.org/10.1016/j.abb.2014.09.015
  • Source: Archives of Biochemistry and Biophysics. Unidade: FCF

    Subjects: PRÓPOLIS, ARTERIOSCLEROSE

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      CUEVAS, Alejandro et al. Identification of microRNAs involved in the modulation of pro-angiogenic factors in atherosclerosis by a polyphenol-rich extract from propolis. Archives of Biochemistry and Biophysics, v. 557, n. 1, p. 28-35, 2014Tradução . . Disponível em: https://doi.org/10.1016/j.abb.2014.04.009. Acesso em: 08 nov. 2025.
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      Cuevas, A., Saavedra, N., Cavalcante, M. F., Salazar, L. A., & Abdalla, D. S. P. (2014). Identification of microRNAs involved in the modulation of pro-angiogenic factors in atherosclerosis by a polyphenol-rich extract from propolis. Archives of Biochemistry and Biophysics, 557( 1), 28-35. doi:10.1016/j.abb.2014.04.009
    • NLM

      Cuevas A, Saavedra N, Cavalcante MF, Salazar LA, Abdalla DSP. Identification of microRNAs involved in the modulation of pro-angiogenic factors in atherosclerosis by a polyphenol-rich extract from propolis [Internet]. Archives of Biochemistry and Biophysics. 2014 ; 557( 1): 28-35.[citado 2025 nov. 08 ] Available from: https://doi.org/10.1016/j.abb.2014.04.009
    • Vancouver

      Cuevas A, Saavedra N, Cavalcante MF, Salazar LA, Abdalla DSP. Identification of microRNAs involved in the modulation of pro-angiogenic factors in atherosclerosis by a polyphenol-rich extract from propolis [Internet]. Archives of Biochemistry and Biophysics. 2014 ; 557( 1): 28-35.[citado 2025 nov. 08 ] Available from: https://doi.org/10.1016/j.abb.2014.04.009
  • Source: Archives of Biochemistry and Biophysics. Unidades: ICB, FOB

    Subjects: OSSO E OSSOS, BIOENGENHARIA, OSTEOBLASTO, TRANSDUÇÃO DE SINAL CELULAR, CÉLULAS

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      GEMINI-PIPERNI, Sara et al. Cellular behavior as a dynamic field for exploring bone bioengineering: a closer look at cell–biomaterial interface. Archives of Biochemistry and Biophysics, v. No 2014, p. 88-98, 2014Tradução . . Disponível em: https://doi.org/10.1016/j.abb.2014.06.019. Acesso em: 08 nov. 2025.
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      Gemini-Piperni, S., Takamori, E. R., Sartoretto, S. C., Paiva, K. B. da S., Granjeiro, J. M., Oliveira, R. C. de, & Zambuzzi, W. F. (2014). Cellular behavior as a dynamic field for exploring bone bioengineering: a closer look at cell–biomaterial interface. Archives of Biochemistry and Biophysics, No 2014, 88-98. doi:10.1016/j.abb.2014.06.019
    • NLM

      Gemini-Piperni S, Takamori ER, Sartoretto SC, Paiva KB da S, Granjeiro JM, Oliveira RC de, Zambuzzi WF. Cellular behavior as a dynamic field for exploring bone bioengineering: a closer look at cell–biomaterial interface [Internet]. Archives of Biochemistry and Biophysics. 2014 ; No 2014 88-98.[citado 2025 nov. 08 ] Available from: https://doi.org/10.1016/j.abb.2014.06.019
    • Vancouver

      Gemini-Piperni S, Takamori ER, Sartoretto SC, Paiva KB da S, Granjeiro JM, Oliveira RC de, Zambuzzi WF. Cellular behavior as a dynamic field for exploring bone bioengineering: a closer look at cell–biomaterial interface [Internet]. Archives of Biochemistry and Biophysics. 2014 ; No 2014 88-98.[citado 2025 nov. 08 ] Available from: https://doi.org/10.1016/j.abb.2014.06.019

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