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

    Subjects: NUCLEAÇÃO, MICROSCOPIA

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    • ABNT

      PLAUT, Justin S. et al. Quantitative atomic force microscopy provides new insight into matrix vesicle mineralization. Archives of Biochemistry and Biophysics, v. 667, p. 14-21, 2019Tradução . . Disponível em: https://doi.org/10.1016/j.abb.2019.04.003. Acesso em: 19 nov. 2025.
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      Plaut, J. S., Strzelecka-Kiliszek, A., Bozycki, L., Pikula, S., Buchet, R., Mebarek, S., et al. (2019). Quantitative atomic force microscopy provides new insight into matrix vesicle mineralization. Archives of Biochemistry and Biophysics, 667, 14-21. doi:10.1016/j.abb.2019.04.003
    • NLM

      Plaut JS, Strzelecka-Kiliszek A, Bozycki L, Pikula S, Buchet R, Mebarek S, Chadli M, Bolean M, Simão AMS, Ciancaglini P, Magrini A, Rosato N, Magne D, Girard-Egrot A, Farquharson C, Esener SC, Millán JL, Bottini M. Quantitative atomic force microscopy provides new insight into matrix vesicle mineralization [Internet]. Archives of Biochemistry and Biophysics. 2019 ; 667 14-21.[citado 2025 nov. 19 ] Available from: https://doi.org/10.1016/j.abb.2019.04.003
    • Vancouver

      Plaut JS, Strzelecka-Kiliszek A, Bozycki L, Pikula S, Buchet R, Mebarek S, Chadli M, Bolean M, Simão AMS, Ciancaglini P, Magrini A, Rosato N, Magne D, Girard-Egrot A, Farquharson C, Esener SC, Millán JL, Bottini M. Quantitative atomic force microscopy provides new insight into matrix vesicle mineralization [Internet]. Archives of Biochemistry and Biophysics. 2019 ; 667 14-21.[citado 2025 nov. 19 ] Available from: https://doi.org/10.1016/j.abb.2019.04.003
  • Source: Archives of Biochemistry and Biophysics. Unidade: FFCLRP

    Subjects: FOSFATASE ALCALINA, MEMBRANA CELULAR VEGETAL, BIOMINERALIZAÇÃO

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    • ABNT

      ANDRADE, Marco Aurélio Raz de et al. Is alkaline phosphatase biomimeticaly immobilized on titanium able to propagate the biomineralization process?. Archives of Biochemistry and Biophysics, v. 663, p. 192-198, 2019Tradução . . Disponível em: https://doi.org/10.1016/j.abb.2019.01.014. Acesso em: 19 nov. 2025.
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      Andrade, M. A. R. de, Derradi, R., Simão, A. M. S., Millán, J. L., Ramos, A. P., Ciancaglini, P., & Bolean, M. (2019). Is alkaline phosphatase biomimeticaly immobilized on titanium able to propagate the biomineralization process? Archives of Biochemistry and Biophysics, 663, 192-198. doi:10.1016/j.abb.2019.01.014
    • NLM

      Andrade MAR de, Derradi R, Simão AMS, Millán JL, Ramos AP, Ciancaglini P, Bolean M. Is alkaline phosphatase biomimeticaly immobilized on titanium able to propagate the biomineralization process? [Internet]. Archives of Biochemistry and Biophysics. 2019 ; 663 192-198.[citado 2025 nov. 19 ] Available from: https://doi.org/10.1016/j.abb.2019.01.014
    • Vancouver

      Andrade MAR de, Derradi R, Simão AMS, Millán JL, Ramos AP, Ciancaglini P, Bolean M. Is alkaline phosphatase biomimeticaly immobilized on titanium able to propagate the biomineralization process? [Internet]. Archives of Biochemistry and Biophysics. 2019 ; 663 192-198.[citado 2025 nov. 19 ] Available from: https://doi.org/10.1016/j.abb.2019.01.014
  • Source: Archives of Biochemistry and Biophysics. Unidades: IF, FFCLRP

    Subjects: PROTEÍNAS DE TRANSPORTE, PROTEÍNAS DA MEMBRANA, CÁLCIO

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    • ABNT

      BOLEAN, Maytê et al. Proteoliposomes with the ability to transport Ca2+ into the vesicles and hydrolyze phosphosubstrates on their surface. Archives of Biochemistry and Biophysics, v. 584, p. 79-89, 2015Tradução . . Disponível em: https://doi.org/10.1016/j.abb.2015.08.018. Acesso em: 19 nov. 2025.
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      Bolean, M., Simão, A. M. S., Kiffer-Moreira, T., Hoylaerts, M. F., Millán, J. L., Itri, R., & Ciancaglini, P. (2015). Proteoliposomes with the ability to transport Ca2+ into the vesicles and hydrolyze phosphosubstrates on their surface. Archives of Biochemistry and Biophysics, 584, 79-89. doi:10.1016/j.abb.2015.08.018
    • NLM

      Bolean M, Simão AMS, Kiffer-Moreira T, Hoylaerts MF, Millán JL, Itri R, Ciancaglini P. Proteoliposomes with the ability to transport Ca2+ into the vesicles and hydrolyze phosphosubstrates on their surface [Internet]. Archives of Biochemistry and Biophysics. 2015 ; 584 79-89.[citado 2025 nov. 19 ] Available from: https://doi.org/10.1016/j.abb.2015.08.018
    • Vancouver

      Bolean M, Simão AMS, Kiffer-Moreira T, Hoylaerts MF, Millán JL, Itri R, Ciancaglini P. Proteoliposomes with the ability to transport Ca2+ into the vesicles and hydrolyze phosphosubstrates on their surface [Internet]. Archives of Biochemistry and Biophysics. 2015 ; 584 79-89.[citado 2025 nov. 19 ] Available from: https://doi.org/10.1016/j.abb.2015.08.018
  • 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: 19 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. 19 ] 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. 19 ] Available from: https://doi.org/10.1016/j.abb.2014.09.015
  • Source: Archives of Biochemistry and Biophysics. Unidade: FFCLRP

    Subjects: PROTEÍNAS DA MEMBRANA, POTÁSSIO, ENZIMAS

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    • ABNT

      YONEDA, Juliana Sakamoto e RIGOS, Carolina Fortes e CIANCAGLINI, Pietro. Addition of subunit 'gama', 'K POT.+' ions, and lipid restores the thermal stability of solubilized Na, K-ATPase. Archives of Biochemistry and Biophysics, v. 530, n. 2, p. 93-100, 2013Tradução . . Disponível em: https://doi.org/10.1016/j.abb.2012.12.022. Acesso em: 19 nov. 2025.
    • APA

      Yoneda, J. S., Rigos, C. F., & Ciancaglini, P. (2013). Addition of subunit 'gama', 'K POT.+' ions, and lipid restores the thermal stability of solubilized Na, K-ATPase. Archives of Biochemistry and Biophysics, 530( 2), 93-100. doi:10.1016/j.abb.2012.12.022
    • NLM

      Yoneda JS, Rigos CF, Ciancaglini P. Addition of subunit 'gama', 'K POT.+' ions, and lipid restores the thermal stability of solubilized Na, K-ATPase [Internet]. Archives of Biochemistry and Biophysics. 2013 ; 530( 2): 93-100.[citado 2025 nov. 19 ] Available from: https://doi.org/10.1016/j.abb.2012.12.022
    • Vancouver

      Yoneda JS, Rigos CF, Ciancaglini P. Addition of subunit 'gama', 'K POT.+' ions, and lipid restores the thermal stability of solubilized Na, K-ATPase [Internet]. Archives of Biochemistry and Biophysics. 2013 ; 530( 2): 93-100.[citado 2025 nov. 19 ] Available from: https://doi.org/10.1016/j.abb.2012.12.022
  • Source: Archives of Biochemistry and Biophysics. Unidade: FFCLRP

    Subjects: AMÔNIA, ARTRÓPODES, PROTEÍNAS, COMPOSTOS DE FÓSFORO

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      GARÇON, Daniela P. et al. Synergistic stimulation by potassium and ammonium of 'K POT.+'-phosphatase activity in gill microsomes from the crab Callinectes ornatus acclimated to low salinity: novel property of a primordial pump. Archives of Biochemistry and Biophysics, v. 530, n. 2, p. 55-63, 2013Tradução . . Disponível em: https://doi.org/10.1016/j.abb.2012.12.006. Acesso em: 19 nov. 2025.
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      Garçon, D. P., Lucena, M. N., Pinto, M. R., Fontes, C. F. L., McNamara, J. C., & Leone, F. de A. (2013). Synergistic stimulation by potassium and ammonium of 'K POT.+'-phosphatase activity in gill microsomes from the crab Callinectes ornatus acclimated to low salinity: novel property of a primordial pump. Archives of Biochemistry and Biophysics, 530( 2), 55-63. doi:10.1016/j.abb.2012.12.006
    • NLM

      Garçon DP, Lucena MN, Pinto MR, Fontes CFL, McNamara JC, Leone F de A. Synergistic stimulation by potassium and ammonium of 'K POT.+'-phosphatase activity in gill microsomes from the crab Callinectes ornatus acclimated to low salinity: novel property of a primordial pump [Internet]. Archives of Biochemistry and Biophysics. 2013 ; 530( 2): 55-63.[citado 2025 nov. 19 ] Available from: https://doi.org/10.1016/j.abb.2012.12.006
    • Vancouver

      Garçon DP, Lucena MN, Pinto MR, Fontes CFL, McNamara JC, Leone F de A. Synergistic stimulation by potassium and ammonium of 'K POT.+'-phosphatase activity in gill microsomes from the crab Callinectes ornatus acclimated to low salinity: novel property of a primordial pump [Internet]. Archives of Biochemistry and Biophysics. 2013 ; 530( 2): 55-63.[citado 2025 nov. 19 ] Available from: https://doi.org/10.1016/j.abb.2012.12.006
  • Source: Archives of Biochemistry and Biophysics. Unidade: FFCLRP

    Subjects: CRUSTACEA, SÓDIO, POTÁSSIO, BIOQUÍMICA

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    • ABNT

      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: 19 nov. 2025.
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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 2025 nov. 19 ] 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 2025 nov. 19 ] Available from: https://doi.org/10.1016/j.abb.2008.08.018
  • 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: 19 nov. 2025.
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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 2025 nov. 19 ] 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. 19 ] 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: 19 nov. 2025.
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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 2025 nov. 19 ] 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. 19 ] Available from: https://doi.org/10.1016/s0003-9861(02)00712-9
  • 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: 19 nov. 2025.
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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 2025 nov. 19 ] 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 2025 nov. 19 ] Available from: http://www.idealibrary.com/links/doi/10.1006/abbi.2000.2244/pdf
  • Source: Archives of Biochemistry and Biophysics. Unidade: FFCLRP

    Assunto: TOXICOLOGIA

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      ARNI, R. K. et al. Crystal structure of mitoxin II, a manomeric Lys49-Phospholipase 'A IND. 2' homologue isolated from the venom of Cerrophidion (Bothrops) godmani. Archives of Biochemistry and Biophysics, v. 366, n. 2, p. 177-182, 1999Tradução . . Acesso em: 19 nov. 2025.
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      Arni, R. K., Fontes, M. R., Barberato, C., Gutiérrez, J. M., Diaz C.,, & Ward, R. J. (1999). Crystal structure of mitoxin II, a manomeric Lys49-Phospholipase 'A IND. 2' homologue isolated from the venom of Cerrophidion (Bothrops) godmani. Archives of Biochemistry and Biophysics, 366( 2), 177-182.
    • NLM

      Arni RK, Fontes MR, Barberato C, Gutiérrez JM, Diaz C., Ward RJ. Crystal structure of mitoxin II, a manomeric Lys49-Phospholipase 'A IND. 2' homologue isolated from the venom of Cerrophidion (Bothrops) godmani. Archives of Biochemistry and Biophysics. 1999 ; 366( 2): 177-182.[citado 2025 nov. 19 ]
    • Vancouver

      Arni RK, Fontes MR, Barberato C, Gutiérrez JM, Diaz C., Ward RJ. Crystal structure of mitoxin II, a manomeric Lys49-Phospholipase 'A IND. 2' homologue isolated from the venom of Cerrophidion (Bothrops) godmani. Archives of Biochemistry and Biophysics. 1999 ; 366( 2): 177-182.[citado 2025 nov. 19 ]

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