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  • Fonte: Journal of Molecular Biology. Unidades: IFSC, IQSC

    Assuntos: PROTEÍNAS, POLIMERIZAÇÃO, BIOFÍSICA

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      MENDONÇA, Déborah Cezar et al. Structural insights into ciona intestinalis septins: complexes suggest a mechanism for nucleotide-dependent interfacial cross-talk. Journal of Molecular Biology, v. 436, n. 16, p. 168693-1-168693-20 + supplementary material, 2024Tradução . . Disponível em: https://doi.org/10.1016/j.jmb.2024.168693. Acesso em: 31 out. 2024.
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      Mendonça, D. C., Morais, S. T. do B., Ciol, H., Pinto, A. P. A., Leonardo, D. A., Pereira, H. d'M., et al. (2024). Structural insights into ciona intestinalis septins: complexes suggest a mechanism for nucleotide-dependent interfacial cross-talk. Journal of Molecular Biology, 436( 16), 168693-1-168693-20 + supplementary material. doi:10.1016/j.jmb.2024.168693
    • NLM

      Mendonça DC, Morais ST do B, Ciol H, Pinto APA, Leonardo DA, Pereira H d'M, Valadares NF, Portugal RV, Klaholz BP, Garratt RC, Araújo APU de. Structural insights into ciona intestinalis septins: complexes suggest a mechanism for nucleotide-dependent interfacial cross-talk [Internet]. Journal of Molecular Biology. 2024 ; 436( 16): 168693-1-168693-20 + supplementary material.[citado 2024 out. 31 ] Available from: https://doi.org/10.1016/j.jmb.2024.168693
    • Vancouver

      Mendonça DC, Morais ST do B, Ciol H, Pinto APA, Leonardo DA, Pereira H d'M, Valadares NF, Portugal RV, Klaholz BP, Garratt RC, Araújo APU de. Structural insights into ciona intestinalis septins: complexes suggest a mechanism for nucleotide-dependent interfacial cross-talk [Internet]. Journal of Molecular Biology. 2024 ; 436( 16): 168693-1-168693-20 + supplementary material.[citado 2024 out. 31 ] Available from: https://doi.org/10.1016/j.jmb.2024.168693
  • Fonte: Structure. Unidades: IQSC, IF

    Assuntos: BIOQUÍMICA, BIOFÍSICA, MACROMOLÉCULA, PROTEÍNAS

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      SERAPHIM, Thiago V et al. Assembly principles of the human R2TP chaperone complex reveal the presence of R2T and R2P complexes. Structure, v. 30, p. 156–171, 2022Tradução . . Disponível em: https://doi.org/10.1016/j.str.2021.08.002. Acesso em: 31 out. 2024.
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      Seraphim, T. V., Nano, N., Cheung, Y. W. S., Aluksanasuwan, S., Colleti, C., Mao, Y. -Q., et al. (2022). Assembly principles of the human R2TP chaperone complex reveal the presence of R2T and R2P complexes. Structure, 30, 156–171. doi:10.1016/j.str.2021.08.002
    • NLM

      Seraphim TV, Nano N, Cheung YWS, Aluksanasuwan S, Colleti C, Mao Y-Q, Bhandari V, Young G, Holl L, Phanse S, Gordiyenko Y, Southworth DR, Robinson CV, Thongboonkerd V, Gava LM, Borges JC, Babu M, Barbosa LRS, Ramos CHI, Kukura P, Houry WA. Assembly principles of the human R2TP chaperone complex reveal the presence of R2T and R2P complexes [Internet]. Structure. 2022 ; 30 156–171.[citado 2024 out. 31 ] Available from: https://doi.org/10.1016/j.str.2021.08.002
    • Vancouver

      Seraphim TV, Nano N, Cheung YWS, Aluksanasuwan S, Colleti C, Mao Y-Q, Bhandari V, Young G, Holl L, Phanse S, Gordiyenko Y, Southworth DR, Robinson CV, Thongboonkerd V, Gava LM, Borges JC, Babu M, Barbosa LRS, Ramos CHI, Kukura P, Houry WA. Assembly principles of the human R2TP chaperone complex reveal the presence of R2T and R2P complexes [Internet]. Structure. 2022 ; 30 156–171.[citado 2024 out. 31 ] Available from: https://doi.org/10.1016/j.str.2021.08.002
  • Fonte: Microbial Pathogenesis. Unidade: IQSC

    Assuntos: BIOQUÍMICA, BIOFÍSICA, ESPOROTRICOSE, FUNGOS, PROTEÍNAS

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      PORTUONDO, Deivys Leandro et al. A Sporothrix spp. enolase derived multi-epitope vaccine confers protective response in BALB/c mice challenged with Sporothrix brasiliensis. Microbial Pathogenesis, v. 166, 2022Tradução . . Disponível em: https://doi.org/10.1016/j.micpath.2022.105539. Acesso em: 31 out. 2024.
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      Portuondo, D. L., Batista-Duharte, A., Cardenas, C., Oliveira, C. S. de, Borges, J. C., Téllez-Martínez, D., et al. (2022). A Sporothrix spp. enolase derived multi-epitope vaccine confers protective response in BALB/c mice challenged with Sporothrix brasiliensis. Microbial Pathogenesis, 166. doi:10.1016/j.micpath.2022.105539
    • NLM

      Portuondo DL, Batista-Duharte A, Cardenas C, Oliveira CS de, Borges JC, Téllez-Martínez D, Santana PA, Gauna A, Mercado L, Castilho BM de, Costa P, Guzman F, Carlos IZ. A Sporothrix spp. enolase derived multi-epitope vaccine confers protective response in BALB/c mice challenged with Sporothrix brasiliensis [Internet]. Microbial Pathogenesis. 2022 ; 166[citado 2024 out. 31 ] Available from: https://doi.org/10.1016/j.micpath.2022.105539
    • Vancouver

      Portuondo DL, Batista-Duharte A, Cardenas C, Oliveira CS de, Borges JC, Téllez-Martínez D, Santana PA, Gauna A, Mercado L, Castilho BM de, Costa P, Guzman F, Carlos IZ. A Sporothrix spp. enolase derived multi-epitope vaccine confers protective response in BALB/c mice challenged with Sporothrix brasiliensis [Internet]. Microbial Pathogenesis. 2022 ; 166[citado 2024 out. 31 ] Available from: https://doi.org/10.1016/j.micpath.2022.105539
  • Fonte: Biochimie: an international journal of biochemistry and molecular biology. Unidade: IQSC

    Assuntos: BIOQUÍMICA, BIOFÍSICA, PROTEÍNAS

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      CAMPANELLA, Jonatas Erick Maimoni et al. Biochemical and biophysical characterization of the RVB-1/RVB-2 protein complex, the RuvBL/RVB homologues in Neurospora crassa. Biochimie: an international journal of biochemistry and molecular biology, v. 191, p. 11-26, 2021Tradução . . Disponível em: https://doi.org/10.1016/j.biochi.2021.08.002. Acesso em: 31 out. 2024.
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      Campanella, J. E. M., Ramos Junior, S. L., Rodrigues, V. K. T., Gomes, A. A. S., Barros, A. C. de, Mateos, P. A., et al. (2021). Biochemical and biophysical characterization of the RVB-1/RVB-2 protein complex, the RuvBL/RVB homologues in Neurospora crassa. Biochimie: an international journal of biochemistry and molecular biology, 191, 11-26. doi:10.1016/j.biochi.2021.08.002
    • NLM

      Campanella JEM, Ramos Junior SL, Rodrigues VKT, Gomes AAS, Barros AC de, Mateos PA, Freitas FZ, Fontes MR de M, Borges JC, Bertolini MC. Biochemical and biophysical characterization of the RVB-1/RVB-2 protein complex, the RuvBL/RVB homologues in Neurospora crassa [Internet]. Biochimie: an international journal of biochemistry and molecular biology. 2021 ;191 11-26.[citado 2024 out. 31 ] Available from: https://doi.org/10.1016/j.biochi.2021.08.002
    • Vancouver

      Campanella JEM, Ramos Junior SL, Rodrigues VKT, Gomes AAS, Barros AC de, Mateos PA, Freitas FZ, Fontes MR de M, Borges JC, Bertolini MC. Biochemical and biophysical characterization of the RVB-1/RVB-2 protein complex, the RuvBL/RVB homologues in Neurospora crassa [Internet]. Biochimie: an international journal of biochemistry and molecular biology. 2021 ;191 11-26.[citado 2024 out. 31 ] Available from: https://doi.org/10.1016/j.biochi.2021.08.002
  • Fonte: Abstract Book. Nome do evento: Fungal Genetics Conference. Unidade: IQSC

    Assuntos: BIOQUÍMICA, BIOFÍSICA, PROTEÍNAS

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      CAMPANELLA, J. E. M. et al. The Neurospora crassa RVB-1/2 protein complex, two proteins belonging to the AAA+ ATPase protein family, plays a functional role in heat stress response. 2019, Anais.. Pacific Grove: Genetics Society of America, 2019. Disponível em: http://conferences.genetics-gsa.org/fungal/2019/program-book. Acesso em: 31 out. 2024.
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      Campanella, J. E. M., Ramos Junior, S. L., Barros, A. C., Freitas, F. Z., Borges, J. C., Fontes, M. R. M., & Bertolini, M. C. (2019). The Neurospora crassa RVB-1/2 protein complex, two proteins belonging to the AAA+ ATPase protein family, plays a functional role in heat stress response. In Abstract Book. Pacific Grove: Genetics Society of America. Recuperado de http://conferences.genetics-gsa.org/fungal/2019/program-book
    • NLM

      Campanella JEM, Ramos Junior SL, Barros AC, Freitas FZ, Borges JC, Fontes MRM, Bertolini MC. The Neurospora crassa RVB-1/2 protein complex, two proteins belonging to the AAA+ ATPase protein family, plays a functional role in heat stress response [Internet]. Abstract Book. 2019 ;[citado 2024 out. 31 ] Available from: http://conferences.genetics-gsa.org/fungal/2019/program-book
    • Vancouver

      Campanella JEM, Ramos Junior SL, Barros AC, Freitas FZ, Borges JC, Fontes MRM, Bertolini MC. The Neurospora crassa RVB-1/2 protein complex, two proteins belonging to the AAA+ ATPase protein family, plays a functional role in heat stress response [Internet]. Abstract Book. 2019 ;[citado 2024 out. 31 ] Available from: http://conferences.genetics-gsa.org/fungal/2019/program-book
  • Fonte: Biophysical Journal. Nome do evento: Annual Meeting of the Biophysical Society. Unidade: IQSC

    Assunto: BIOFÍSICA

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      SANTIAGO, Patricia Soares et al. Characterization of amynthas gracilis hemoglobin (HbAg) and its subunits by AUC and MALDI-TOF-MS. Biophysical Journal. St Louis: Cell Press. . Acesso em: 31 out. 2024. , 2015
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      Santiago, P. S., Carvalho, F. A., Oliveira, J. B. S., Linhares, A. P. D., Morgante, P. G., Carvalho, J. W. P., & Tabak, M. (2015). Characterization of amynthas gracilis hemoglobin (HbAg) and its subunits by AUC and MALDI-TOF-MS. Biophysical Journal. St Louis: Cell Press.
    • NLM

      Santiago PS, Carvalho FA, Oliveira JBS, Linhares APD, Morgante PG, Carvalho JWP, Tabak M. Characterization of amynthas gracilis hemoglobin (HbAg) and its subunits by AUC and MALDI-TOF-MS. Biophysical Journal. 2015 ; 108( 2): 375A.[citado 2024 out. 31 ]
    • Vancouver

      Santiago PS, Carvalho FA, Oliveira JBS, Linhares APD, Morgante PG, Carvalho JWP, Tabak M. Characterization of amynthas gracilis hemoglobin (HbAg) and its subunits by AUC and MALDI-TOF-MS. Biophysical Journal. 2015 ; 108( 2): 375A.[citado 2024 out. 31 ]
  • Fonte: Photodiagnosis and Photodynamic Terapy. Unidade: IQSC

    Assuntos: BIOFÍSICA, TERAPIA FOTODINÂMICA

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      BERNAL, Cláudia et al. Photodynamic efficiency of hypericincompared with chlorin andhematoporphyrin derivatives in HEp-2 and Vero epithelial cell lines. Photodiagnosis and Photodynamic Terapy, v. 12, n. 2, p. 176-185, 2015Tradução . . Disponível em: https://doi.org/10.1016/j.pdpdt.2015.04.003. Acesso em: 31 out. 2024.
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      Bernal, C., Ribeiro, A. O., Andrade, G. P., & Perussi, J. R. (2015). Photodynamic efficiency of hypericincompared with chlorin andhematoporphyrin derivatives in HEp-2 and Vero epithelial cell lines. Photodiagnosis and Photodynamic Terapy, 12( 2), 176-185. doi:10.1016/j.pdpdt.2015.04.003
    • NLM

      Bernal C, Ribeiro AO, Andrade GP, Perussi JR. Photodynamic efficiency of hypericincompared with chlorin andhematoporphyrin derivatives in HEp-2 and Vero epithelial cell lines [Internet]. Photodiagnosis and Photodynamic Terapy. 2015 ; 12( 2): 176-185.[citado 2024 out. 31 ] Available from: https://doi.org/10.1016/j.pdpdt.2015.04.003
    • Vancouver

      Bernal C, Ribeiro AO, Andrade GP, Perussi JR. Photodynamic efficiency of hypericincompared with chlorin andhematoporphyrin derivatives in HEp-2 and Vero epithelial cell lines [Internet]. Photodiagnosis and Photodynamic Terapy. 2015 ; 12( 2): 176-185.[citado 2024 out. 31 ] Available from: https://doi.org/10.1016/j.pdpdt.2015.04.003
  • Fonte: Archives of Biochemistry and Biophysics. Unidades: IQSC, IF

    Assuntos: 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: 31 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. 31 ] 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. 31 ] Available from: https://doi.org/10.1016/j.abb.2014.10.015
  • Fonte: Colloids and Surfaces B: Biointerfaces. Unidade: IQSC

    Assunto: BIOFÍSICA

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      CARVALHO, José Wilson Pires et al. Cetyltrimethylammonium chloride (CTAC) effect on the thermal stability of oxy-HbGp: dynamic light scattering (DLS) and small angle X-ray scattering (SAXS) studies. Colloids and Surfaces B: Biointerfaces, v. 118, n. 1, p. 14-24, 2014Tradução . . Disponível em: https://doi.org/10.1016/j.colsurfb.2014.03.021. Acesso em: 31 out. 2024.
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      Carvalho, J. W. P., Carvalho, F. A. de O., Batista, T., Santiago, P. S., & Tabak, M. (2014). Cetyltrimethylammonium chloride (CTAC) effect on the thermal stability of oxy-HbGp: dynamic light scattering (DLS) and small angle X-ray scattering (SAXS) studies. Colloids and Surfaces B: Biointerfaces, 118( 1), 14-24. doi:10.1016/j.colsurfb.2014.03.021
    • NLM

      Carvalho JWP, Carvalho FA de O, Batista T, Santiago PS, Tabak M. Cetyltrimethylammonium chloride (CTAC) effect on the thermal stability of oxy-HbGp: dynamic light scattering (DLS) and small angle X-ray scattering (SAXS) studies [Internet]. Colloids and Surfaces B: Biointerfaces. 2014 ; 118( 1): 14-24.[citado 2024 out. 31 ] Available from: https://doi.org/10.1016/j.colsurfb.2014.03.021
    • Vancouver

      Carvalho JWP, Carvalho FA de O, Batista T, Santiago PS, Tabak M. Cetyltrimethylammonium chloride (CTAC) effect on the thermal stability of oxy-HbGp: dynamic light scattering (DLS) and small angle X-ray scattering (SAXS) studies [Internet]. Colloids and Surfaces B: Biointerfaces. 2014 ; 118( 1): 14-24.[citado 2024 out. 31 ] Available from: https://doi.org/10.1016/j.colsurfb.2014.03.021
  • Fonte: International Journal of Biological Macromolecules. Unidade: IQSC

    Assuntos: BIOFÍSICA, BIOLOGIA MOLECULAR

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      CARVALHO, Francisco Adriano de Oliveira et al. pH effect upon HbGp oligomeric stability: characterization of the dissociated species by AUC and DLS studies. International Journal of Biological Macromolecules, v. 59, n. 1, p. 333-341, 2013Tradução . . Disponível em: https://doi.org/10.1016/j.ijbiomac.2013.04.070. Acesso em: 31 out. 2024.
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      Carvalho, F. A. de O., Carvalho, J. W. P., Alves, F. R., & Tabak, M. (2013). pH effect upon HbGp oligomeric stability: characterization of the dissociated species by AUC and DLS studies. International Journal of Biological Macromolecules, 59( 1), 333-341. doi:10.1016/j.ijbiomac.2013.04.070
    • NLM

      Carvalho FA de O, Carvalho JWP, Alves FR, Tabak M. pH effect upon HbGp oligomeric stability: characterization of the dissociated species by AUC and DLS studies [Internet]. International Journal of Biological Macromolecules. 2013 ; 59( 1): 333-341.[citado 2024 out. 31 ] Available from: https://doi.org/10.1016/j.ijbiomac.2013.04.070
    • Vancouver

      Carvalho FA de O, Carvalho JWP, Alves FR, Tabak M. pH effect upon HbGp oligomeric stability: characterization of the dissociated species by AUC and DLS studies [Internet]. International Journal of Biological Macromolecules. 2013 ; 59( 1): 333-341.[citado 2024 out. 31 ] Available from: https://doi.org/10.1016/j.ijbiomac.2013.04.070
  • Fonte: Photodiagnosis and Photodynamic Therapy. Unidade: IQSC

    Assunto: BIOFÍSICA

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      MELO, Wanessa de Cássia Martins Antunes de et al. Electroporation enhances antimicrobial photodynamic therapy mediated by the hydrophobic photosensitizer, hypericin. Photodiagnosis and Photodynamic Therapy, v. 10, n. 4, p. 647-650, 2013Tradução . . Disponível em: https://doi.org/10.1016/j.pdpdt.2013.08.001. Acesso em: 31 out. 2024.
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      Melo, W. de C. M. A. de, Lee , A. N., Perussi, J. R., & Hamblin, M. R. (2013). Electroporation enhances antimicrobial photodynamic therapy mediated by the hydrophobic photosensitizer, hypericin. Photodiagnosis and Photodynamic Therapy, 10( 4), 647-650. doi:10.1016/j.pdpdt.2013.08.001
    • NLM

      Melo W de CMA de, Lee AN, Perussi JR, Hamblin MR. Electroporation enhances antimicrobial photodynamic therapy mediated by the hydrophobic photosensitizer, hypericin [Internet]. Photodiagnosis and Photodynamic Therapy. 2013 ; 10( 4): 647-650.[citado 2024 out. 31 ] Available from: https://doi.org/10.1016/j.pdpdt.2013.08.001
    • Vancouver

      Melo W de CMA de, Lee AN, Perussi JR, Hamblin MR. Electroporation enhances antimicrobial photodynamic therapy mediated by the hydrophobic photosensitizer, hypericin [Internet]. Photodiagnosis and Photodynamic Therapy. 2013 ; 10( 4): 647-650.[citado 2024 out. 31 ] Available from: https://doi.org/10.1016/j.pdpdt.2013.08.001
  • Fonte: European Biophysics Journal. Nome do evento: European Biophysics Congress - EBSA. Unidade: IQSC

    Assuntos: PROTEÍNAS, BIOFÍSICA

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      TABAK, Marcel et al. ANS fluorescence on the stability of extracellular glossoscolex paulistus hemoglobin with denaturant. European Biophysics Journal. Heidelberg: Springer. Disponível em: https://doi.org/10.1007/s00249-013-0917-x. Acesso em: 31 out. 2024. , 2013
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      Tabak, M., Barros, A. E. B., Carvalho, F. A. O., & Carvalho, J. W. P. (2013). ANS fluorescence on the stability of extracellular glossoscolex paulistus hemoglobin with denaturant. European Biophysics Journal. Heidelberg: Springer. doi:10.1007/s00249-013-0917-x
    • NLM

      Tabak M, Barros AEB, Carvalho FAO, Carvalho JWP. ANS fluorescence on the stability of extracellular glossoscolex paulistus hemoglobin with denaturant [Internet]. European Biophysics Journal. 2013 ; 42( 1): S71.[citado 2024 out. 31 ] Available from: https://doi.org/10.1007/s00249-013-0917-x
    • Vancouver

      Tabak M, Barros AEB, Carvalho FAO, Carvalho JWP. ANS fluorescence on the stability of extracellular glossoscolex paulistus hemoglobin with denaturant [Internet]. European Biophysics Journal. 2013 ; 42( 1): S71.[citado 2024 out. 31 ] Available from: https://doi.org/10.1007/s00249-013-0917-x
  • Fonte: Biochimica et Biophysica Acta. Unidade: IQSC

    Assuntos: BIOFÍSICA, BIOLOGIA MOLECULAR

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      SILVA, Kelly Prata e SERAPHIM, T e BORGES, Julio Cesar. Structural and functional studies of leishmania braziliensis Hsp90. Biochimica et Biophysica Acta, v. 1834, n. 1, p. 351-361, 2013Tradução . . Disponível em: https://doi.org/10.1016/j.bbapap.2012.08.004. Acesso em: 31 out. 2024.
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      Silva, K. P., Seraphim, T., & Borges, J. C. (2013). Structural and functional studies of leishmania braziliensis Hsp90. Biochimica et Biophysica Acta, 1834( 1), 351-361. doi:10.1016/j.bbapap.2012.08.004
    • NLM

      Silva KP, Seraphim T, Borges JC. Structural and functional studies of leishmania braziliensis Hsp90 [Internet]. Biochimica et Biophysica Acta. 2013 ; 1834( 1): 351-361.[citado 2024 out. 31 ] Available from: https://doi.org/10.1016/j.bbapap.2012.08.004
    • Vancouver

      Silva KP, Seraphim T, Borges JC. Structural and functional studies of leishmania braziliensis Hsp90 [Internet]. Biochimica et Biophysica Acta. 2013 ; 1834( 1): 351-361.[citado 2024 out. 31 ] Available from: https://doi.org/10.1016/j.bbapap.2012.08.004
  • Fonte: International Journal of Biological Macromolecules. Unidade: IQSC

    Assuntos: BIOFÍSICA, BIOLOGIA MOLECULAR

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      CARVALHO, José Wilson Pires et al. Thermal denaturation and aggregation of hemoglobin of glossoscolex paulistus in acid and neutral media. International Journal of Biological Macromolecules, v. 54, n. 1, p. 109-118, 2013Tradução . . Disponível em: https://doi.org/10.1016/j.ijbiomac.2012.11.022. Acesso em: 31 out. 2024.
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      Carvalho, J. W. P., Carvalho, F. A. de O., Santiago, P. S., & Tabak, M. (2013). Thermal denaturation and aggregation of hemoglobin of glossoscolex paulistus in acid and neutral media. International Journal of Biological Macromolecules, 54( 1), 109-118. doi:10.1016/j.ijbiomac.2012.11.022
    • NLM

      Carvalho JWP, Carvalho FA de O, Santiago PS, Tabak M. Thermal denaturation and aggregation of hemoglobin of glossoscolex paulistus in acid and neutral media [Internet]. International Journal of Biological Macromolecules. 2013 ; 54( 1): 109-118.[citado 2024 out. 31 ] Available from: https://doi.org/10.1016/j.ijbiomac.2012.11.022
    • Vancouver

      Carvalho JWP, Carvalho FA de O, Santiago PS, Tabak M. Thermal denaturation and aggregation of hemoglobin of glossoscolex paulistus in acid and neutral media [Internet]. International Journal of Biological Macromolecules. 2013 ; 54( 1): 109-118.[citado 2024 out. 31 ] Available from: https://doi.org/10.1016/j.ijbiomac.2012.11.022
  • Fonte: Colloids and Surfaces B: Biointerfaces. Unidade: IQSC

    Assunto: BIOFÍSICA

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      CARVALHO, Jose Wilson Pires et al. Sodium dodecyl sulfate (SDS) effect on the thermal stability of oxy-HbGp: dynamic light scattering (DLS) and small angle X-ray scattering (SAXS) studies. Colloids and Surfaces B: Biointerfaces, v. 111, n. 1, p. 561-570, 2013Tradução . . Disponível em: https://doi.org/10.1016/j.colsurfb.2013.06.050. Acesso em: 31 out. 2024.
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      Carvalho, J. W. P., Alves, F. R., Batista, T., Carvalho, F. A. de O., Santiago, P. S., & Tabak, M. (2013). Sodium dodecyl sulfate (SDS) effect on the thermal stability of oxy-HbGp: dynamic light scattering (DLS) and small angle X-ray scattering (SAXS) studies. Colloids and Surfaces B: Biointerfaces, 111( 1), 561-570. doi:10.1016/j.colsurfb.2013.06.050
    • NLM

      Carvalho JWP, Alves FR, Batista T, Carvalho FA de O, Santiago PS, Tabak M. Sodium dodecyl sulfate (SDS) effect on the thermal stability of oxy-HbGp: dynamic light scattering (DLS) and small angle X-ray scattering (SAXS) studies [Internet]. Colloids and Surfaces B: Biointerfaces. 2013 ; 111( 1): 561-570.[citado 2024 out. 31 ] Available from: https://doi.org/10.1016/j.colsurfb.2013.06.050
    • Vancouver

      Carvalho JWP, Alves FR, Batista T, Carvalho FA de O, Santiago PS, Tabak M. Sodium dodecyl sulfate (SDS) effect on the thermal stability of oxy-HbGp: dynamic light scattering (DLS) and small angle X-ray scattering (SAXS) studies [Internet]. Colloids and Surfaces B: Biointerfaces. 2013 ; 111( 1): 561-570.[citado 2024 out. 31 ] Available from: https://doi.org/10.1016/j.colsurfb.2013.06.050
  • Fonte: International Journal of Biological Macromolecules. Unidade: IQSC

    Assuntos: BIOFÍSICA, BIOLOGIA MOLECULAR

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    • ABNT

      CARVALHO, Francisco Adriano de Oliveira et al. Urea-induced unfolding of glossoscolex paulistus hemoglobin , in oxy-and cyanomet-forms: a dissociation model. International Journal of Biological Macromolecules, v. 52, n. 2, p. 340-348, 2013Tradução . . Disponível em: https://doi.org/10.1016/j.ijbiomac.2012.09.023. Acesso em: 31 out. 2024.
    • APA

      Carvalho, F. A. de O., Carvalho, J. W. P., Santiago, P. S., & Tabak, M. (2013). Urea-induced unfolding of glossoscolex paulistus hemoglobin , in oxy-and cyanomet-forms: a dissociation model. International Journal of Biological Macromolecules, 52( 2), 340-348. doi:10.1016/j.ijbiomac.2012.09.023
    • NLM

      Carvalho FA de O, Carvalho JWP, Santiago PS, Tabak M. Urea-induced unfolding of glossoscolex paulistus hemoglobin , in oxy-and cyanomet-forms: a dissociation model [Internet]. International Journal of Biological Macromolecules. 2013 ; 52( 2): 340-348.[citado 2024 out. 31 ] Available from: https://doi.org/10.1016/j.ijbiomac.2012.09.023
    • Vancouver

      Carvalho FA de O, Carvalho JWP, Santiago PS, Tabak M. Urea-induced unfolding of glossoscolex paulistus hemoglobin , in oxy-and cyanomet-forms: a dissociation model [Internet]. International Journal of Biological Macromolecules. 2013 ; 52( 2): 340-348.[citado 2024 out. 31 ] Available from: https://doi.org/10.1016/j.ijbiomac.2012.09.023
  • Fonte: Archives of Biochemistry and Biophysics. Unidades: IF, IQSC

    Assuntos: BIOFÍSICA, BIOLOGIA MOLECULAR

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    • ABNT

      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: 31 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. 31 ] 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. 31 ] Available from: https://doi.org/10.1016/j.abb.2012.02.009
  • Fonte: Archives of Biochemistry and Biophysics. Unidade: IQSC

    Assuntos: BIOFÍSICA, BIOLOGIA MOLECULAR

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    • ABNT

      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: 31 out. 2024.
    • APA

      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. 31 ] 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. 31 ] Available from: https://doi.org/10.1016/j.abb.2012.01.007
  • Fonte: International Journal of Biological Macromolecules. Unidade: IQSC

    Assuntos: BIOFÍSICA, BIOLOGIA MOLECULAR

    Acesso à fonteDOIComo citar
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    • ABNT

      CARVALHO, Francisco Adriano de Oliveira et al. Molecular masses and sedimentation coefficients of extracellular hemoglobin og glossoscolex paulistus: alkaline oligomeric dissociation. International Journal of Biological Macromolecules, v. 48, n. 1, p. 183-193, 2011Tradução . . Disponível em: https://doi.org/10.1016/j.ijbiomac.2010.11.002. Acesso em: 31 out. 2024.
    • APA

      Carvalho, F. A. de O., Santiago, P. S., Borges, J. C., & Tabak, M. (2011). Molecular masses and sedimentation coefficients of extracellular hemoglobin og glossoscolex paulistus: alkaline oligomeric dissociation. International Journal of Biological Macromolecules, 48( 1), 183-193. doi:10.1016/j.ijbiomac.2010.11.002
    • NLM

      Carvalho FA de O, Santiago PS, Borges JC, Tabak M. Molecular masses and sedimentation coefficients of extracellular hemoglobin og glossoscolex paulistus: alkaline oligomeric dissociation [Internet]. International Journal of Biological Macromolecules. 2011 ; 48( 1): 183-193.[citado 2024 out. 31 ] Available from: https://doi.org/10.1016/j.ijbiomac.2010.11.002
    • Vancouver

      Carvalho FA de O, Santiago PS, Borges JC, Tabak M. Molecular masses and sedimentation coefficients of extracellular hemoglobin og glossoscolex paulistus: alkaline oligomeric dissociation [Internet]. International Journal of Biological Macromolecules. 2011 ; 48( 1): 183-193.[citado 2024 out. 31 ] Available from: https://doi.org/10.1016/j.ijbiomac.2010.11.002
  • Fonte: Colloids and Surfaces B: Biointerfaces. Unidade: IQSC

    Assunto: BIOFÍSICA

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    • ABNT

      ANJOS, Jorge Luiz Vieira et al. On the interaction of bovine serum albumin with ionic surfactants:: temperature induced EPR changes of a maleimide nitroxide reflect local protein dynamics and probe solvent accessibility. Colloids and Surfaces B: Biointerfaces, v. 88, n. 1, p. 463-470, 2011Tradução . . Disponível em: https://doi.org/10.1016/j.colsurfb.2011.07.030. Acesso em: 31 out. 2024.
    • APA

      Anjos, J. L. V., Santiago, P. S., Tabak, M., & Alonso, A. (2011). On the interaction of bovine serum albumin with ionic surfactants:: temperature induced EPR changes of a maleimide nitroxide reflect local protein dynamics and probe solvent accessibility. Colloids and Surfaces B: Biointerfaces, 88( 1), 463-470. doi:10.1016/j.colsurfb.2011.07.030
    • NLM

      Anjos JLV, Santiago PS, Tabak M, Alonso A. On the interaction of bovine serum albumin with ionic surfactants:: temperature induced EPR changes of a maleimide nitroxide reflect local protein dynamics and probe solvent accessibility [Internet]. Colloids and Surfaces B: Biointerfaces. 2011 ; 88( 1): 463-470.[citado 2024 out. 31 ] Available from: https://doi.org/10.1016/j.colsurfb.2011.07.030
    • Vancouver

      Anjos JLV, Santiago PS, Tabak M, Alonso A. On the interaction of bovine serum albumin with ionic surfactants:: temperature induced EPR changes of a maleimide nitroxide reflect local protein dynamics and probe solvent accessibility [Internet]. Colloids and Surfaces B: Biointerfaces. 2011 ; 88( 1): 463-470.[citado 2024 out. 31 ] Available from: https://doi.org/10.1016/j.colsurfb.2011.07.030

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