Filtros : "BIOQUÍMICA" "IQSC-SQM" "Holanda" Removidos: "Demasi, M" "HIRATA, MARIO HIROYUKI" Limpar

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  • Source: Biochimica et Biophysica Acta. Proteins and Proteomics. Unidade: IQSC

    Subjects: PROTEÍNAS, BIOQUÍMICA

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      SILVA, Noeli Soares Melo da et al. The regulation of the thermal stability and affinity of the HSPA5 (Grp78/BiP) by clients and nucleotides is modulated by domains coupling. Biochimica et Biophysica Acta. Proteins and Proteomics, v. 1872, p. 141034, 2024Tradução . . Disponível em: https://doi.org/10.1016/j.bbapap.2024.141034. Acesso em: 02 set. 2024.
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      Silva, N. S. M. da, Siebeneichler, B., Oliveira, C. S. de, Dores-Silva, P. R., & Borges, J. C. (2024). The regulation of the thermal stability and affinity of the HSPA5 (Grp78/BiP) by clients and nucleotides is modulated by domains coupling. Biochimica et Biophysica Acta. Proteins and Proteomics, 1872, 141034. doi:10.1016/j.bbapap.2024.141034
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      Silva NSM da, Siebeneichler B, Oliveira CS de, Dores-Silva PR, Borges JC. The regulation of the thermal stability and affinity of the HSPA5 (Grp78/BiP) by clients and nucleotides is modulated by domains coupling [Internet]. Biochimica et Biophysica Acta. Proteins and Proteomics. 2024 ;1872 141034.[citado 2024 set. 02 ] Available from: https://doi.org/10.1016/j.bbapap.2024.141034
    • Vancouver

      Silva NSM da, Siebeneichler B, Oliveira CS de, Dores-Silva PR, Borges JC. The regulation of the thermal stability and affinity of the HSPA5 (Grp78/BiP) by clients and nucleotides is modulated by domains coupling [Internet]. Biochimica et Biophysica Acta. Proteins and Proteomics. 2024 ;1872 141034.[citado 2024 set. 02 ] Available from: https://doi.org/10.1016/j.bbapap.2024.141034
  • Source: Journal of Drug Delivery Science and Technology. Unidade: IQSC

    Subjects: BIOQUÍMICA, BIOMATERIAIS, BICHOS-DA-SEDA, LARVICIDAS, DENGUE

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      MARINHO, Victor H S et al. Development of an environmentally friendly formulation of silk fibroin combined with fatty acid from Astrocaryum murumuru Mart. effective against Aedes aegypti larvae. Journal of Drug Delivery Science and Technology, v. 75, p. 103626, 2022Tradução . . Disponível em: https://doi.org/10.1016/j.jddst.2022.103626. Acesso em: 02 set. 2024.
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      Marinho, V. H. S., Neves, F. B., Jimenez, D. E. Q., Oliveira, F. R., Santos, A. V. T. de L. T. dos, Ferreira, R. M. A., et al. (2022). Development of an environmentally friendly formulation of silk fibroin combined with fatty acid from Astrocaryum murumuru Mart. effective against Aedes aegypti larvae. Journal of Drug Delivery Science and Technology, 75, 103626. doi:10.1016/j.jddst.2022.103626
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      Marinho VHS, Neves FB, Jimenez DEQ, Oliveira FR, Santos AVT de LT dos, Ferreira RMA, Souto RNP, Carvalho JCT, Yoshioka SA, Ferreira IM. Development of an environmentally friendly formulation of silk fibroin combined with fatty acid from Astrocaryum murumuru Mart. effective against Aedes aegypti larvae [Internet]. Journal of Drug Delivery Science and Technology. 2022 ; 75 103626.[citado 2024 set. 02 ] Available from: https://doi.org/10.1016/j.jddst.2022.103626
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      Marinho VHS, Neves FB, Jimenez DEQ, Oliveira FR, Santos AVT de LT dos, Ferreira RMA, Souto RNP, Carvalho JCT, Yoshioka SA, Ferreira IM. Development of an environmentally friendly formulation of silk fibroin combined with fatty acid from Astrocaryum murumuru Mart. effective against Aedes aegypti larvae [Internet]. Journal of Drug Delivery Science and Technology. 2022 ; 75 103626.[citado 2024 set. 02 ] Available from: https://doi.org/10.1016/j.jddst.2022.103626
  • Source: Biochimica et Biophysica Acta - Proteins and Proteomics. Unidades: IQSC, IF, FM

    Subjects: BIOQUÍMICA, PROTEÍNAS

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      SILVA, Noeli Soares Melo da et al. Structural, thermodynamic and functional studies of human 71 kDa heat shock cognate protein (HSPA8/hHsc70). Biochimica et Biophysica Acta - Proteins and Proteomics, v. 1869, 2021Tradução . . Disponível em: https://doi.org/10.1016/j.bbapap.2021.140719. Acesso em: 02 set. 2024.
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      Silva, N. S. M. da, Rodrigues, L. F. de C., Silva, P. R. D., Montanari, C. A., Ramos, C. H. I., Barbosa, L. R. S., & Borges, J. C. (2021). Structural, thermodynamic and functional studies of human 71 kDa heat shock cognate protein (HSPA8/hHsc70). Biochimica et Biophysica Acta - Proteins and Proteomics, 1869. doi:10.1016/j.bbapap.2021.140719
    • NLM

      Silva NSM da, Rodrigues LF de C, Silva PRD, Montanari CA, Ramos CHI, Barbosa LRS, Borges JC. Structural, thermodynamic and functional studies of human 71 kDa heat shock cognate protein (HSPA8/hHsc70) [Internet]. Biochimica et Biophysica Acta - Proteins and Proteomics. 2021 ; 1869[citado 2024 set. 02 ] Available from: https://doi.org/10.1016/j.bbapap.2021.140719
    • Vancouver

      Silva NSM da, Rodrigues LF de C, Silva PRD, Montanari CA, Ramos CHI, Barbosa LRS, Borges JC. Structural, thermodynamic and functional studies of human 71 kDa heat shock cognate protein (HSPA8/hHsc70) [Internet]. Biochimica et Biophysica Acta - Proteins and Proteomics. 2021 ; 1869[citado 2024 set. 02 ] Available from: https://doi.org/10.1016/j.bbapap.2021.140719
  • Source: International Journal of Biological Macromolecules. Unidade: IQSC

    Subjects: BIOQUÍMICA, BIOLOGIA MOLECULAR, PROTEÍNAS

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      KIRALY, Vanessa T. R et al. Thermal aggregates of human mortalin and Hsp70-1A behave as supramolecular assemblies. International Journal of Biological Macromolecules, v. 146, p. 320-331, 2020Tradução . . Disponível em: https://doi.org/10.1016/j.ijbiomac.2019.12.236. Acesso em: 02 set. 2024.
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      Kiraly, V. T. R., Dores-Silva, P. R., Serrão, V. H. B., Cauvi, D. M., De Maio, A., & Borges, J. C. (2020). Thermal aggregates of human mortalin and Hsp70-1A behave as supramolecular assemblies. International Journal of Biological Macromolecules, 146, 320-331. doi:10.1016/j.ijbiomac.2019.12.236
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      Kiraly VTR, Dores-Silva PR, Serrão VHB, Cauvi DM, De Maio A, Borges JC. Thermal aggregates of human mortalin and Hsp70-1A behave as supramolecular assemblies [Internet]. International Journal of Biological Macromolecules. 2020 ;146 320-331.[citado 2024 set. 02 ] Available from: https://doi.org/10.1016/j.ijbiomac.2019.12.236
    • Vancouver

      Kiraly VTR, Dores-Silva PR, Serrão VHB, Cauvi DM, De Maio A, Borges JC. Thermal aggregates of human mortalin and Hsp70-1A behave as supramolecular assemblies [Internet]. International Journal of Biological Macromolecules. 2020 ;146 320-331.[citado 2024 set. 02 ] Available from: https://doi.org/10.1016/j.ijbiomac.2019.12.236
  • Source: Colloids and Surfaces B: Biointerfaces. Unidades: IQSC, FCFRP, FCF

    Subjects: BIOQUÍMICA, NEOPLASIAS, PRÓSTATA, MEDICAMENTO

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      ELOYA, Josimar O. et al. EGFR-targeted immunoliposomes efficiently deliver docetaxel to prostate cancer cells. Colloids and Surfaces B: Biointerfaces, v. 194, p. 111185, 2020Tradução . . Disponível em: https://doi.org/10.1016/j.colsurfb.2020.111185. Acesso em: 02 set. 2024.
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      Eloya, J. O., Ruiz, A., Lima, F. T. de, Petrilli, R., Raspantini, G. L., Nogueira, K. A. B., et al. (2020). EGFR-targeted immunoliposomes efficiently deliver docetaxel to prostate cancer cells. Colloids and Surfaces B: Biointerfaces, 194, 111185. doi:10.1016/j.colsurfb.2020.111185
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      Eloya JO, Ruiz A, Lima FT de, Petrilli R, Raspantini GL, Nogueira KAB, Santos E, Oliveira CS de, Borges JC, Marchetti JM, Al-Jamal WT, Chorilli M. EGFR-targeted immunoliposomes efficiently deliver docetaxel to prostate cancer cells [Internet]. Colloids and Surfaces B: Biointerfaces. 2020 ; 194 111185.[citado 2024 set. 02 ] Available from: https://doi.org/10.1016/j.colsurfb.2020.111185
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      Eloya JO, Ruiz A, Lima FT de, Petrilli R, Raspantini GL, Nogueira KAB, Santos E, Oliveira CS de, Borges JC, Marchetti JM, Al-Jamal WT, Chorilli M. EGFR-targeted immunoliposomes efficiently deliver docetaxel to prostate cancer cells [Internet]. Colloids and Surfaces B: Biointerfaces. 2020 ; 194 111185.[citado 2024 set. 02 ] Available from: https://doi.org/10.1016/j.colsurfb.2020.111185
  • Source: Biochimica et Biophysica Acta: Biomembranes. Unidade: IQSC

    Subjects: BIOQUÍMICA, MITOCÔNDRIAS, LIPÍDEOS DA MEMBRANA

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      DORES-SILVA, Paulo Roberto et al. Human HSPA9 (mtHsp70, mortalin) interacts with lipid bilayers containing cardiolipin, a major component of the inner mitochondrial membrane. Biochimica et Biophysica Acta: Biomembranes, v. 1862, 2020Tradução . . Disponível em: https://doi.org/10.1016/j.bbamem.2020.183436. Acesso em: 02 set. 2024.
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      Dores-Silva, P. R., Cauvi, D. M., Kiraly, V. T. R., Borges, J. C., & Maio, A. de. (2020). Human HSPA9 (mtHsp70, mortalin) interacts with lipid bilayers containing cardiolipin, a major component of the inner mitochondrial membrane. Biochimica et Biophysica Acta: Biomembranes, 1862. doi:10.1016/j.bbamem.2020.183436
    • NLM

      Dores-Silva PR, Cauvi DM, Kiraly VTR, Borges JC, Maio A de. Human HSPA9 (mtHsp70, mortalin) interacts with lipid bilayers containing cardiolipin, a major component of the inner mitochondrial membrane [Internet]. Biochimica et Biophysica Acta: Biomembranes. 2020 ; 1862[citado 2024 set. 02 ] Available from: https://doi.org/10.1016/j.bbamem.2020.183436
    • Vancouver

      Dores-Silva PR, Cauvi DM, Kiraly VTR, Borges JC, Maio A de. Human HSPA9 (mtHsp70, mortalin) interacts with lipid bilayers containing cardiolipin, a major component of the inner mitochondrial membrane [Internet]. Biochimica et Biophysica Acta: Biomembranes. 2020 ; 1862[citado 2024 set. 02 ] Available from: https://doi.org/10.1016/j.bbamem.2020.183436
  • Source: Biochimica et Biophysica Acta - Biomembranes. Unidades: IF, IQSC

    Subjects: LIPOPOLISSACARÍDEOS, BIOQUÍMICA

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      DOMINGUES, Marco M et al. rBPI21 interacts with negative membranes endothermically promoting the formation of rigid multilamellar structures. Biochimica et Biophysica Acta - Biomembranes, v. 1828, n. 11, p. 2419-2427, 2013Tradução . . Disponível em: https://doi.org/10.1016/j.bbamem.2013.06.009. Acesso em: 02 set. 2024.
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      Domingues, M. M., Bianconi, M. L., Barbosa, L. R. S., Santiago, P. S., Tabak, M., Castanho, M. A. R. B., et al. (2013). rBPI21 interacts with negative membranes endothermically promoting the formation of rigid multilamellar structures. Biochimica et Biophysica Acta - Biomembranes, 1828( 11), 2419-2427. doi:10.1016/j.bbamem.2013.06.009
    • NLM

      Domingues MM, Bianconi ML, Barbosa LRS, Santiago PS, Tabak M, Castanho MARB, Itri R, Santos NC. rBPI21 interacts with negative membranes endothermically promoting the formation of rigid multilamellar structures [Internet]. Biochimica et Biophysica Acta - Biomembranes. 2013 ; 1828( 11): 2419-2427.[citado 2024 set. 02 ] Available from: https://doi.org/10.1016/j.bbamem.2013.06.009
    • Vancouver

      Domingues MM, Bianconi ML, Barbosa LRS, Santiago PS, Tabak M, Castanho MARB, Itri R, Santos NC. rBPI21 interacts with negative membranes endothermically promoting the formation of rigid multilamellar structures [Internet]. Biochimica et Biophysica Acta - Biomembranes. 2013 ; 1828( 11): 2419-2427.[citado 2024 set. 02 ] Available from: https://doi.org/10.1016/j.bbamem.2013.06.009
  • Source: Biophysical Chemistry. Unidades: FFCLRP, IF, IQSC

    Assunto: BIOQUÍMICA

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      CARVALHO, José Wilson Pires et al. On the temperature stability of extracellular hemoglobin of Glossoscolex paulistus, at different oxidation states: SAXS and DLS studies. Biophysical Chemistry, v. 163-164, p. 44-55, 2012Tradução . . Disponível em: https://doi.org/10.1016/j.bpc.2012.02.004. Acesso em: 02 set. 2024.
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      Carvalho, J. W. P., Santiago, P. S., Batista, T., Salmon, C. E. G., Barbosa, L. R. S., Itri, R., & Tabak, M. (2012). On the temperature stability of extracellular hemoglobin of Glossoscolex paulistus, at different oxidation states: SAXS and DLS studies. Biophysical Chemistry, 163-164, 44-55. doi:10.1016/j.bpc.2012.02.004
    • NLM

      Carvalho JWP, Santiago PS, Batista T, Salmon CEG, Barbosa LRS, Itri R, Tabak M. On the temperature stability of extracellular hemoglobin of Glossoscolex paulistus, at different oxidation states: SAXS and DLS studies [Internet]. Biophysical Chemistry. 2012 ; 163-164 44-55.[citado 2024 set. 02 ] Available from: https://doi.org/10.1016/j.bpc.2012.02.004
    • Vancouver

      Carvalho JWP, Santiago PS, Batista T, Salmon CEG, Barbosa LRS, Itri R, Tabak M. On the temperature stability of extracellular hemoglobin of Glossoscolex paulistus, at different oxidation states: SAXS and DLS studies [Internet]. Biophysical Chemistry. 2012 ; 163-164 44-55.[citado 2024 set. 02 ] Available from: https://doi.org/10.1016/j.bpc.2012.02.004
  • Source: Protein and Peptide Letters. Unidade: IQSC

    Subjects: BIOLOGIA MOLECULAR, BIOQUÍMICA

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      SILVA, Kelly P da e BORGES, Julio Cesar. The molecular chaperone Hsp70 family members function by a bidirectional heterotrophic allosteric mechanism. Protein and Peptide Letters, v. 18, n. 2, p. 132-142, 2011Tradução . . Acesso em: 02 set. 2024.
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      Silva, K. P. da, & Borges, J. C. (2011). The molecular chaperone Hsp70 family members function by a bidirectional heterotrophic allosteric mechanism. Protein and Peptide Letters, 18( 2), 132-142.
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      Silva KP da, Borges JC. The molecular chaperone Hsp70 family members function by a bidirectional heterotrophic allosteric mechanism. Protein and Peptide Letters. 2011 ; 18( 2): 132-142.[citado 2024 set. 02 ]
    • Vancouver

      Silva KP da, Borges JC. The molecular chaperone Hsp70 family members function by a bidirectional heterotrophic allosteric mechanism. Protein and Peptide Letters. 2011 ; 18( 2): 132-142.[citado 2024 set. 02 ]
  • Source: Colloids and Surfaces B: Biointerfaces. Unidades: IQSC, FFCLRP

    Subjects: BIOQUÍMICA, BIORESSONÂNCIA PARAMAGNÉTICA DE SPIN

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      SOUSA NETO, Diógenes de et al. Interaction of bovine serum albumin (BSA) with ionic surfactants evaluated by electron paramagnetic resonance (EPR) spectroscopy. Colloids and Surfaces B: Biointerfaces, v. 70, n. 1, p. 147-156, 2009Tradução . . Disponível em: https://doi.org/10.1016/j.colsurfb.2008.12.026. Acesso em: 02 set. 2024.
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      Sousa Neto, D. de, Salmon, C. E. G., Alonso, A., & Tabak, M. (2009). Interaction of bovine serum albumin (BSA) with ionic surfactants evaluated by electron paramagnetic resonance (EPR) spectroscopy. Colloids and Surfaces B: Biointerfaces, 70( 1), 147-156. doi:10.1016/j.colsurfb.2008.12.026
    • NLM

      Sousa Neto D de, Salmon CEG, Alonso A, Tabak M. Interaction of bovine serum albumin (BSA) with ionic surfactants evaluated by electron paramagnetic resonance (EPR) spectroscopy [Internet]. Colloids and Surfaces B: Biointerfaces. 2009 ; 70( 1): 147-156.[citado 2024 set. 02 ] Available from: https://doi.org/10.1016/j.colsurfb.2008.12.026
    • Vancouver

      Sousa Neto D de, Salmon CEG, Alonso A, Tabak M. Interaction of bovine serum albumin (BSA) with ionic surfactants evaluated by electron paramagnetic resonance (EPR) spectroscopy [Internet]. Colloids and Surfaces B: Biointerfaces. 2009 ; 70( 1): 147-156.[citado 2024 set. 02 ] Available from: https://doi.org/10.1016/j.colsurfb.2008.12.026
  • Source: Colloids and Surfaces B: Biointerfaces. Unidade: IQSC

    Subjects: BIOQUÍMICA, BIOFÍSICA

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      SANTIAGO, Patricia Soares et al. On the localization of water-soluble porphyrins in micellar systems evaluated by static and time-resolved frequency-domanin fluorescence techniques. Colloids and Surfaces B: Biointerfaces, v. 65, n. 2, p. 247-256, 2008Tradução . . Disponível em: https://doi.org/10.1016/j.colsurfb.2008.04.010. Acesso em: 02 set. 2024.
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      Santiago, P. S., Sousa Neto, D. de, Gandini, S. de C. M., & Tabak, M. (2008). On the localization of water-soluble porphyrins in micellar systems evaluated by static and time-resolved frequency-domanin fluorescence techniques. Colloids and Surfaces B: Biointerfaces, 65( 2), 247-256. doi:10.1016/j.colsurfb.2008.04.010
    • NLM

      Santiago PS, Sousa Neto D de, Gandini S de CM, Tabak M. On the localization of water-soluble porphyrins in micellar systems evaluated by static and time-resolved frequency-domanin fluorescence techniques [Internet]. Colloids and Surfaces B: Biointerfaces. 2008 ; 65( 2): 247-256.[citado 2024 set. 02 ] Available from: https://doi.org/10.1016/j.colsurfb.2008.04.010
    • Vancouver

      Santiago PS, Sousa Neto D de, Gandini S de CM, Tabak M. On the localization of water-soluble porphyrins in micellar systems evaluated by static and time-resolved frequency-domanin fluorescence techniques [Internet]. Colloids and Surfaces B: Biointerfaces. 2008 ; 65( 2): 247-256.[citado 2024 set. 02 ] Available from: https://doi.org/10.1016/j.colsurfb.2008.04.010
  • Source: Current Drug Targets. Unidade: IQSC

    Subjects: BIOQUÍMICA, MODELAGEM MOLECULAR

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      CANDURI, Fernanda e AZEVEDO JUNIOR, Walter Filgueira de. Protein crystallography in drug discovery. Current Drug Targets, v. 9, n. 12, p. 1048-1053, 2008Tradução . . Acesso em: 02 set. 2024.
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      Canduri, F., & Azevedo Junior, W. F. de. (2008). Protein crystallography in drug discovery. Current Drug Targets, 9( 12), 1048-1053.
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      Canduri F, Azevedo Junior WF de. Protein crystallography in drug discovery. Current Drug Targets. 2008 ; 9( 12): 1048-1053.[citado 2024 set. 02 ]
    • Vancouver

      Canduri F, Azevedo Junior WF de. Protein crystallography in drug discovery. Current Drug Targets. 2008 ; 9( 12): 1048-1053.[citado 2024 set. 02 ]
  • Source: Colloids and Surfaces B: Biointerfaces. Unidade: IQSC

    Subjects: BIOQUÍMICA, BIOFÍSICA

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      MOREIRA, Leonardo Marmo et al. Interaction of giant extracellular glossoscolex paulistus hemoglobin (HbGp) with zwitterionic surfactant N-hexadecyl-N,N-dimethyl-3-ammonio-1-propanesulfonate (HPS): effects of oligomeric dissociation. Colloids and Surfaces B: Biointerfaces, v. 61, n. 2, p. 153-163, 2008Tradução . . Disponível em: https://doi.org/10.1016/j.colsurfb.2007.07.010. Acesso em: 02 set. 2024.
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      Moreira, L. M., Santiago, P. S., Almeida, Ë. V. de, & Tabak, M. (2008). Interaction of giant extracellular glossoscolex paulistus hemoglobin (HbGp) with zwitterionic surfactant N-hexadecyl-N,N-dimethyl-3-ammonio-1-propanesulfonate (HPS): effects of oligomeric dissociation. Colloids and Surfaces B: Biointerfaces, 61( 2), 153-163. doi:10.1016/j.colsurfb.2007.07.010
    • NLM

      Moreira LM, Santiago PS, Almeida ËV de, Tabak M. Interaction of giant extracellular glossoscolex paulistus hemoglobin (HbGp) with zwitterionic surfactant N-hexadecyl-N,N-dimethyl-3-ammonio-1-propanesulfonate (HPS): effects of oligomeric dissociation [Internet]. Colloids and Surfaces B: Biointerfaces. 2008 ; 61( 2): 153-163.[citado 2024 set. 02 ] Available from: https://doi.org/10.1016/j.colsurfb.2007.07.010
    • Vancouver

      Moreira LM, Santiago PS, Almeida ËV de, Tabak M. Interaction of giant extracellular glossoscolex paulistus hemoglobin (HbGp) with zwitterionic surfactant N-hexadecyl-N,N-dimethyl-3-ammonio-1-propanesulfonate (HPS): effects of oligomeric dissociation [Internet]. Colloids and Surfaces B: Biointerfaces. 2008 ; 61( 2): 153-163.[citado 2024 set. 02 ] Available from: https://doi.org/10.1016/j.colsurfb.2007.07.010
  • Source: Colloids and Surfaces B: Biointerfaces. Unidade: IQSC

    Subjects: BIOQUÍMICA, BIOFÍSICA

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      POLI, Alessandra Lima et al. SDS (sodium dodecyl sulfate) effect on the autoxidation of the glossoscolex paulistus giant extracellular hemoglobin:: Kinetic studies at pH 7.0 and 9.0. Colloids and Surfaces B: Biointerfaces, v. 52, n. 1, p. 96-104, 2006Tradução . . Disponível em: https://doi.org/10.1016/j.colsurfb.2006.07.010. Acesso em: 02 set. 2024.
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      Poli, A. L., Moreira, L. M., Tabak, M., & Imasato, H. (2006). SDS (sodium dodecyl sulfate) effect on the autoxidation of the glossoscolex paulistus giant extracellular hemoglobin:: Kinetic studies at pH 7.0 and 9.0. Colloids and Surfaces B: Biointerfaces, 52( 1), 96-104. doi:10.1016/j.colsurfb.2006.07.010
    • NLM

      Poli AL, Moreira LM, Tabak M, Imasato H. SDS (sodium dodecyl sulfate) effect on the autoxidation of the glossoscolex paulistus giant extracellular hemoglobin:: Kinetic studies at pH 7.0 and 9.0 [Internet]. Colloids and Surfaces B: Biointerfaces. 2006 ; 52( 1): 96-104.[citado 2024 set. 02 ] Available from: https://doi.org/10.1016/j.colsurfb.2006.07.010
    • Vancouver

      Poli AL, Moreira LM, Tabak M, Imasato H. SDS (sodium dodecyl sulfate) effect on the autoxidation of the glossoscolex paulistus giant extracellular hemoglobin:: Kinetic studies at pH 7.0 and 9.0 [Internet]. Colloids and Surfaces B: Biointerfaces. 2006 ; 52( 1): 96-104.[citado 2024 set. 02 ] Available from: https://doi.org/10.1016/j.colsurfb.2006.07.010
  • Source: Biophysical Chemistry. Unidades: IFSC, IQSC

    Assunto: BIOQUÍMICA

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      MOREIRA, Leonardo Marmo et al. Pentacoordinate and hexacoordinate ferric hemes in acid medium:: EPR, UV-Vis and CD studies of the giant extracellular hemoglobin of Glossoscolex paulistus. Biophysical Chemistry, v. 124, n. 1, p. 62-72, 2006Tradução . . Disponível em: https://doi.org/10.1016/j.bpc.2006.05.030. Acesso em: 02 set. 2024.
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      Moreira, L. M., Poli, A. L., Costa Filho, A. J. da, & Imasato, H. (2006). Pentacoordinate and hexacoordinate ferric hemes in acid medium:: EPR, UV-Vis and CD studies of the giant extracellular hemoglobin of Glossoscolex paulistus. Biophysical Chemistry, 124( 1), 62-72. doi:10.1016/j.bpc.2006.05.030
    • NLM

      Moreira LM, Poli AL, Costa Filho AJ da, Imasato H. Pentacoordinate and hexacoordinate ferric hemes in acid medium:: EPR, UV-Vis and CD studies of the giant extracellular hemoglobin of Glossoscolex paulistus [Internet]. Biophysical Chemistry. 2006 ; 124( 1): 62-72.[citado 2024 set. 02 ] Available from: https://doi.org/10.1016/j.bpc.2006.05.030
    • Vancouver

      Moreira LM, Poli AL, Costa Filho AJ da, Imasato H. Pentacoordinate and hexacoordinate ferric hemes in acid medium:: EPR, UV-Vis and CD studies of the giant extracellular hemoglobin of Glossoscolex paulistus [Internet]. Biophysical Chemistry. 2006 ; 124( 1): 62-72.[citado 2024 set. 02 ] Available from: https://doi.org/10.1016/j.bpc.2006.05.030
  • Source: Biophysical Chemistry. Unidade: IQSC

    Assunto: BIOQUÍMICA

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    • ABNT

      POLI, Alessandra Lima et al. Autoxidation studies of extracellular hemoglobin of glossoscolex paulistus at pH 9 :: Cyanide and hydroxyl effect. Biophysical Chemistry, v. 114, n. 2-3, p. 253-260, 2005Tradução . . Disponível em: https://doi.org/10.1016/j.bpc.2004.12.041. Acesso em: 02 set. 2024.
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      Poli, A. L., Moreira, L. M., Hidalgo, Á. A., & Imasato, H. (2005). Autoxidation studies of extracellular hemoglobin of glossoscolex paulistus at pH 9 :: Cyanide and hydroxyl effect. Biophysical Chemistry, 114( 2-3), 253-260. doi:10.1016/j.bpc.2004.12.041
    • NLM

      Poli AL, Moreira LM, Hidalgo ÁA, Imasato H. Autoxidation studies of extracellular hemoglobin of glossoscolex paulistus at pH 9 :: Cyanide and hydroxyl effect [Internet]. Biophysical Chemistry. 2005 ;114( 2-3): 253-260.[citado 2024 set. 02 ] Available from: https://doi.org/10.1016/j.bpc.2004.12.041
    • Vancouver

      Poli AL, Moreira LM, Hidalgo ÁA, Imasato H. Autoxidation studies of extracellular hemoglobin of glossoscolex paulistus at pH 9 :: Cyanide and hydroxyl effect [Internet]. Biophysical Chemistry. 2005 ;114( 2-3): 253-260.[citado 2024 set. 02 ] Available from: https://doi.org/10.1016/j.bpc.2004.12.041
  • Source: Biochimica et Biophysica Acta. Unidade: IQSC

    Subjects: BIOQUÍMICA, BIOFÍSICA

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      ALONSO, Antonio e SILVA, Junaine Vasques da e TABAK, Marcel. Hydration effects on the protein dynamics in stratum corneum as evaluated by EPR spectroscopy. Biochimica et Biophysica Acta, v. 1646, p. 32-41, 2003Tradução . . Disponível em: https://doi.org/10.1016/s1570-9639(02)00545-9. Acesso em: 02 set. 2024.
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      Alonso, A., Silva, J. V. da, & Tabak, M. (2003). Hydration effects on the protein dynamics in stratum corneum as evaluated by EPR spectroscopy. Biochimica et Biophysica Acta, 1646, 32-41. doi:10.1016/s1570-9639(02)00545-9
    • NLM

      Alonso A, Silva JV da, Tabak M. Hydration effects on the protein dynamics in stratum corneum as evaluated by EPR spectroscopy [Internet]. Biochimica et Biophysica Acta. 2003 ; 1646 32-41.[citado 2024 set. 02 ] Available from: https://doi.org/10.1016/s1570-9639(02)00545-9
    • Vancouver

      Alonso A, Silva JV da, Tabak M. Hydration effects on the protein dynamics in stratum corneum as evaluated by EPR spectroscopy [Internet]. Biochimica et Biophysica Acta. 2003 ; 1646 32-41.[citado 2024 set. 02 ] Available from: https://doi.org/10.1016/s1570-9639(02)00545-9
  • Source: Biochimica et Biophysica Acta. Unidade: IQSC

    Subjects: BIOQUÍMICA, BIOFÍSICA

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    • ABNT

      GELAMO, Emerson Luiz et al. Interaction of bovine (BSA) and human (HSA) serum albumins with ionic surfactants: spectroscopy and modelling. Biochimica et Biophysica Acta, v. 1594, n. 1, p. 84-99, 2002Tradução . . Disponível em: https://doi.org/10.1016/s0167-4838(01)00287-4. Acesso em: 02 set. 2024.
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      Gelamo, E. L., Silva, C. H. T. P., Imasato, H., & Tabak, M. (2002). Interaction of bovine (BSA) and human (HSA) serum albumins with ionic surfactants: spectroscopy and modelling. Biochimica et Biophysica Acta, 1594( 1), 84-99. doi:10.1016/s0167-4838(01)00287-4
    • NLM

      Gelamo EL, Silva CHTP, Imasato H, Tabak M. Interaction of bovine (BSA) and human (HSA) serum albumins with ionic surfactants: spectroscopy and modelling [Internet]. Biochimica et Biophysica Acta. 2002 ; 1594( 1): 84-99.[citado 2024 set. 02 ] Available from: https://doi.org/10.1016/s0167-4838(01)00287-4
    • Vancouver

      Gelamo EL, Silva CHTP, Imasato H, Tabak M. Interaction of bovine (BSA) and human (HSA) serum albumins with ionic surfactants: spectroscopy and modelling [Internet]. Biochimica et Biophysica Acta. 2002 ; 1594( 1): 84-99.[citado 2024 set. 02 ] Available from: https://doi.org/10.1016/s0167-4838(01)00287-4
  • Source: Biomaterials. Unidade: IQSC

    Assunto: BIOQUÍMICA

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      CIRELLI, Joni Augusto et al. Evaluation of anionic collagen membranes in the treatment of class II furcation lesions: an histometric analysis in dogs. Biomaterials, v. 18, n. 18, p. 1227-1234, 1997Tradução . . Disponível em: https://doi.org/10.1016/s0142-9612(97)00053-7. Acesso em: 02 set. 2024.
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      Cirelli, J. A., Marcantonio Júnior, E., Marcantonio, R. A. C., Lia, R. C. C., Goissis, G., & Rossa Júnior, C. (1997). Evaluation of anionic collagen membranes in the treatment of class II furcation lesions: an histometric analysis in dogs. Biomaterials, 18( 18), 1227-1234. doi:10.1016/s0142-9612(97)00053-7
    • NLM

      Cirelli JA, Marcantonio Júnior E, Marcantonio RAC, Lia RCC, Goissis G, Rossa Júnior C. Evaluation of anionic collagen membranes in the treatment of class II furcation lesions: an histometric analysis in dogs [Internet]. Biomaterials. 1997 ; 18( 18): 1227-1234.[citado 2024 set. 02 ] Available from: https://doi.org/10.1016/s0142-9612(97)00053-7
    • Vancouver

      Cirelli JA, Marcantonio Júnior E, Marcantonio RAC, Lia RCC, Goissis G, Rossa Júnior C. Evaluation of anionic collagen membranes in the treatment of class II furcation lesions: an histometric analysis in dogs [Internet]. Biomaterials. 1997 ; 18( 18): 1227-1234.[citado 2024 set. 02 ] Available from: https://doi.org/10.1016/s0142-9612(97)00053-7

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