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  • Source: Brazilian Journal of Microbiology. Unidade: ICB

    Assunto: MICROBIOLOGIA

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      GOMES, Priscila Aparecida Dal Pozo et al. Antibody Responses Elicited In Mice Immunized With Bacillus Subtilis Vaccine Strains Expressing STX2B Subunit of Enterohaemorragic Escherichia Coli O157:H7. Brazilian Journal of Microbiology, v. 40, n. 2, p. 333-338, 2009Tradução . . Acesso em: 26 set. 2024.
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      Gomes, P. A. D. P., Bentancor, L. V., Paccez, J. D., Sbrogio-Almeida, M. E., Palermo, M. S., Ferreira, R. de C. C., & Ferreira, L. C. de S. (2009). Antibody Responses Elicited In Mice Immunized With Bacillus Subtilis Vaccine Strains Expressing STX2B Subunit of Enterohaemorragic Escherichia Coli O157:H7. Brazilian Journal of Microbiology, 40( 2), 333-338.
    • NLM

      Gomes PADP, Bentancor LV, Paccez JD, Sbrogio-Almeida ME, Palermo MS, Ferreira R de CC, Ferreira LC de S. Antibody Responses Elicited In Mice Immunized With Bacillus Subtilis Vaccine Strains Expressing STX2B Subunit of Enterohaemorragic Escherichia Coli O157:H7. Brazilian Journal of Microbiology. 2009 ; 40( 2): 333-338.[citado 2024 set. 26 ]
    • Vancouver

      Gomes PADP, Bentancor LV, Paccez JD, Sbrogio-Almeida ME, Palermo MS, Ferreira R de CC, Ferreira LC de S. Antibody Responses Elicited In Mice Immunized With Bacillus Subtilis Vaccine Strains Expressing STX2B Subunit of Enterohaemorragic Escherichia Coli O157:H7. Brazilian Journal of Microbiology. 2009 ; 40( 2): 333-338.[citado 2024 set. 26 ]
  • Source: Infection and Immunity. Unidade: ICB

    Assunto: MICROBIOLOGIA

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      BRAGA, Catarina J. M. et al. Paracoccidioides brasiliensis vaccine formulations based on the gp43-derived P10 sequence and the Salmonella enterica FliC flagellin. Infection and Immunity, v. 77, n. 4, p. 1700-07, 2009Tradução . . Disponível em: https://doi.org/10.1128/iai.01470-08. Acesso em: 26 set. 2024.
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      Braga, C. J. M., Rittner, G. M. G., Henao, J. E. M., Teixeira, A. F., Massis, L. M., Sbrogio-Almeida, M. E., et al. (2009). Paracoccidioides brasiliensis vaccine formulations based on the gp43-derived P10 sequence and the Salmonella enterica FliC flagellin. Infection and Immunity, 77( 4), 1700-07. doi:10.1128/iai.01470-08
    • NLM

      Braga CJM, Rittner GMG, Henao JEM, Teixeira AF, Massis LM, Sbrogio-Almeida ME, Taborda CP, Travassos LR, Ferreira LC de S. Paracoccidioides brasiliensis vaccine formulations based on the gp43-derived P10 sequence and the Salmonella enterica FliC flagellin [Internet]. Infection and Immunity. 2009 ; 77( 4): 1700-07.[citado 2024 set. 26 ] Available from: https://doi.org/10.1128/iai.01470-08
    • Vancouver

      Braga CJM, Rittner GMG, Henao JEM, Teixeira AF, Massis LM, Sbrogio-Almeida ME, Taborda CP, Travassos LR, Ferreira LC de S. Paracoccidioides brasiliensis vaccine formulations based on the gp43-derived P10 sequence and the Salmonella enterica FliC flagellin [Internet]. Infection and Immunity. 2009 ; 77( 4): 1700-07.[citado 2024 set. 26 ] Available from: https://doi.org/10.1128/iai.01470-08
  • Source: Eukaryotic Cell. Unidade: ICB

    Assunto: PARASITOLOGIA

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      GODOY, Patrícia Diogo de Melo et al. Trypanosome prereplication machinery contains a single functional Orc1/Cdc6 protein, which is typical of Archaea. Eukaryotic Cell, v. 8, n. 10, p. 1592-1603, 2009Tradução . . Acesso em: 26 set. 2024.
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      Godoy, P. D. de M., Nogueira-Junior, L. A., Paes, L. S., Cornejo, A., Martins, R. M., Silber, A. M., et al. (2009). Trypanosome prereplication machinery contains a single functional Orc1/Cdc6 protein, which is typical of Archaea. Eukaryotic Cell, 8( 10), 1592-1603.
    • NLM

      Godoy PD de M, Nogueira-Junior LA, Paes LS, Cornejo A, Martins RM, Silber AM, Schenkman S, Elias MC. Trypanosome prereplication machinery contains a single functional Orc1/Cdc6 protein, which is typical of Archaea. Eukaryotic Cell. 2009 ; 8( 10): 1592-1603.[citado 2024 set. 26 ]
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      Godoy PD de M, Nogueira-Junior LA, Paes LS, Cornejo A, Martins RM, Silber AM, Schenkman S, Elias MC. Trypanosome prereplication machinery contains a single functional Orc1/Cdc6 protein, which is typical of Archaea. Eukaryotic Cell. 2009 ; 8( 10): 1592-1603.[citado 2024 set. 26 ]
  • Source: Brazilian Journal of Microbiology. Unidade: ICB

    Assunto: MICROBIOLOGIA

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      BRAGA, Catarina J. M. et al. Cytotoxic T cell adjuvant effects of three Salmonella Enterica Flagellins. Brazilian Journal of Microbiology, v. 39, n. 1, p. 44-49, 2008Tradução . . Disponível em: https://doi.org/10.1590/s1517-83822008000100011. Acesso em: 26 set. 2024.
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      Braga, C. J. M., Massis, L. M., Bargieri, B. C. de A., Rodrigues, M. M., Sbrogio-Almeida, M. E., & Ferreira, L. C. de S. (2008). Cytotoxic T cell adjuvant effects of three Salmonella Enterica Flagellins. Brazilian Journal of Microbiology, 39( 1), 44-49. doi:10.1590/s1517-83822008000100011
    • NLM

      Braga CJM, Massis LM, Bargieri BC de A, Rodrigues MM, Sbrogio-Almeida ME, Ferreira LC de S. Cytotoxic T cell adjuvant effects of three Salmonella Enterica Flagellins [Internet]. Brazilian Journal of Microbiology. 2008 ; 39( 1): 44-49.[citado 2024 set. 26 ] Available from: https://doi.org/10.1590/s1517-83822008000100011
    • Vancouver

      Braga CJM, Massis LM, Bargieri BC de A, Rodrigues MM, Sbrogio-Almeida ME, Ferreira LC de S. Cytotoxic T cell adjuvant effects of three Salmonella Enterica Flagellins [Internet]. Brazilian Journal of Microbiology. 2008 ; 39( 1): 44-49.[citado 2024 set. 26 ] Available from: https://doi.org/10.1590/s1517-83822008000100011
  • Source: Free Radical Biology & Medicine. Unidade: ICB

    Assunto: HISTOLOGIA

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      DEMASI, Marilene et al. Oligomerization of the cysteinyl-rich oligopeptidase EP24.15 is triggered by S-glutathionylation. Free Radical Biology & Medicine, v. 44, n. 6, p. 1180-1190, 2008Tradução . . Disponível em: https://doi.org/10.1016/j.freeradbiomed.2007.12.012. Acesso em: 26 set. 2024.
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      Demasi, M., Piassa Filho, G. M., Castro, L. M., Ferreira, J. C., Rioli, V., & Ferro, E. S. (2008). Oligomerization of the cysteinyl-rich oligopeptidase EP24.15 is triggered by S-glutathionylation. Free Radical Biology & Medicine, 44( 6), 1180-1190. doi:10.1016/j.freeradbiomed.2007.12.012
    • NLM

      Demasi M, Piassa Filho GM, Castro LM, Ferreira JC, Rioli V, Ferro ES. Oligomerization of the cysteinyl-rich oligopeptidase EP24.15 is triggered by S-glutathionylation [Internet]. Free Radical Biology & Medicine. 2008 ; 44( 6): 1180-1190.[citado 2024 set. 26 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2007.12.012
    • Vancouver

      Demasi M, Piassa Filho GM, Castro LM, Ferreira JC, Rioli V, Ferro ES. Oligomerization of the cysteinyl-rich oligopeptidase EP24.15 is triggered by S-glutathionylation [Internet]. Free Radical Biology & Medicine. 2008 ; 44( 6): 1180-1190.[citado 2024 set. 26 ] Available from: https://doi.org/10.1016/j.freeradbiomed.2007.12.012
  • Source: Journal of Peptide Science. Unidade: ICB

    Assunto: FISIOLOGIA

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      CABRERA, Marcia Perez dos Santos et al. Study of the mechanism of action of anoplin, a helical antimicrobial decapeptide with ion channel-like activity, and the role of the amidated C-terminus. Journal of Peptide Science, v. 14, n. 6, p. 661-669, 2008Tradução . . Disponível em: https://doi.org/10.1002/psc.960. Acesso em: 26 set. 2024.
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      Cabrera, M. P. dos S., Arcísio-Miranda, M., Costa, S. T. B., Konno, K., Ruggiero, J. R., Araújo Filho, J. P. de, & Ruggiero Neto, J. (2008). Study of the mechanism of action of anoplin, a helical antimicrobial decapeptide with ion channel-like activity, and the role of the amidated C-terminus. Journal of Peptide Science, 14( 6), 661-669. doi:10.1002/psc.960
    • NLM

      Cabrera MP dos S, Arcísio-Miranda M, Costa STB, Konno K, Ruggiero JR, Araújo Filho JP de, Ruggiero Neto J. Study of the mechanism of action of anoplin, a helical antimicrobial decapeptide with ion channel-like activity, and the role of the amidated C-terminus [Internet]. Journal of Peptide Science. 2008 ; 14( 6): 661-669.[citado 2024 set. 26 ] Available from: https://doi.org/10.1002/psc.960
    • Vancouver

      Cabrera MP dos S, Arcísio-Miranda M, Costa STB, Konno K, Ruggiero JR, Araújo Filho JP de, Ruggiero Neto J. Study of the mechanism of action of anoplin, a helical antimicrobial decapeptide with ion channel-like activity, and the role of the amidated C-terminus [Internet]. Journal of Peptide Science. 2008 ; 14( 6): 661-669.[citado 2024 set. 26 ] Available from: https://doi.org/10.1002/psc.960
  • Source: Toxicon. Unidade: ICB

    Assunto: IMUNOLOGIA

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      BALDO, C. et al. BnP1, a novel P-I metalloproteinase from Bothrops neuwiedi venom: biological effects benchmarking relatively to jararhagin, a P-III SVMP. Toxicon, v. 51, n. 1, p. 54-65, 2008Tradução . . Disponível em: https://doi.org/10.1016/j.toxicon.2007.08.005. Acesso em: 26 set. 2024.
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      Baldo, C., Tanjoni, I., León, I. R., Batista, I. F. C., Della-Casa, M. S., Clissa, P. B., et al. (2008). BnP1, a novel P-I metalloproteinase from Bothrops neuwiedi venom: biological effects benchmarking relatively to jararhagin, a P-III SVMP. Toxicon, 51( 1), 54-65. doi:10.1016/j.toxicon.2007.08.005
    • NLM

      Baldo C, Tanjoni I, León IR, Batista IFC, Della-Casa MS, Clissa PB, Weinlich R, Lopes-Ferreira M, Lebrun I, Amarante-Mendes JGP, Rodrigues VM, Perales J, Valente RH, Moura-da-Silva AM. BnP1, a novel P-I metalloproteinase from Bothrops neuwiedi venom: biological effects benchmarking relatively to jararhagin, a P-III SVMP [Internet]. Toxicon. 2008 ; 51( 1): 54-65.[citado 2024 set. 26 ] Available from: https://doi.org/10.1016/j.toxicon.2007.08.005
    • Vancouver

      Baldo C, Tanjoni I, León IR, Batista IFC, Della-Casa MS, Clissa PB, Weinlich R, Lopes-Ferreira M, Lebrun I, Amarante-Mendes JGP, Rodrigues VM, Perales J, Valente RH, Moura-da-Silva AM. BnP1, a novel P-I metalloproteinase from Bothrops neuwiedi venom: biological effects benchmarking relatively to jararhagin, a P-III SVMP [Internet]. Toxicon. 2008 ; 51( 1): 54-65.[citado 2024 set. 26 ] Available from: https://doi.org/10.1016/j.toxicon.2007.08.005
  • Source: Toxicon. Unidade: ICB

    Assunto: FISIOLOGIA

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      ARCISIO-MIRANDA, Manoel et al. Effects of the cationic antimicrobial peptide eumenitin from the venom of solitary wasp Eumenes rubronotatus in planar lipid bilayers: surface charge and pore formation activity. Toxicon, v. 51, n. 5, p. 736-745, 2008Tradução . . Disponível em: https://doi.org/10.1016/j.toxicon.2007.11.023. Acesso em: 26 set. 2024.
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      Arcisio-Miranda, M., Cabrera, M. P. dos S., Konno, K., Rangel, M., & Procópio, J. (2008). Effects of the cationic antimicrobial peptide eumenitin from the venom of solitary wasp Eumenes rubronotatus in planar lipid bilayers: surface charge and pore formation activity. Toxicon, 51( 5), 736-745. doi:10.1016/j.toxicon.2007.11.023
    • NLM

      Arcisio-Miranda M, Cabrera MP dos S, Konno K, Rangel M, Procópio J. Effects of the cationic antimicrobial peptide eumenitin from the venom of solitary wasp Eumenes rubronotatus in planar lipid bilayers: surface charge and pore formation activity [Internet]. Toxicon. 2008 ; 51( 5): 736-745.[citado 2024 set. 26 ] Available from: https://doi.org/10.1016/j.toxicon.2007.11.023
    • Vancouver

      Arcisio-Miranda M, Cabrera MP dos S, Konno K, Rangel M, Procópio J. Effects of the cationic antimicrobial peptide eumenitin from the venom of solitary wasp Eumenes rubronotatus in planar lipid bilayers: surface charge and pore formation activity [Internet]. Toxicon. 2008 ; 51( 5): 736-745.[citado 2024 set. 26 ] Available from: https://doi.org/10.1016/j.toxicon.2007.11.023
  • Source: Archives of Microbiology. Unidades: ICB, IQ

    Assunto: MICROBIOLOGIA

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      SILVA NETO, José F. da et al. Role of 'sigma POT. 54' in the regulation of genes involved in type I and type IV pili biogenesis in Xylella fastidiosa. Archives of Microbiology, v. 189, n. 3, p. 249-261, 2008Tradução . . Acesso em: 26 set. 2024.
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      Silva Neto, J. F. da, Koide, T., Abe, C. M., Gomes, S. L., & Marques, M. do V. (2008). Role of 'sigma POT. 54' in the regulation of genes involved in type I and type IV pili biogenesis in Xylella fastidiosa. Archives of Microbiology, 189( 3), 249-261.
    • NLM

      Silva Neto JF da, Koide T, Abe CM, Gomes SL, Marques M do V. Role of 'sigma POT. 54' in the regulation of genes involved in type I and type IV pili biogenesis in Xylella fastidiosa. Archives of Microbiology. 2008 ; 189( 3): 249-261.[citado 2024 set. 26 ]
    • Vancouver

      Silva Neto JF da, Koide T, Abe CM, Gomes SL, Marques M do V. Role of 'sigma POT. 54' in the regulation of genes involved in type I and type IV pili biogenesis in Xylella fastidiosa. Archives of Microbiology. 2008 ; 189( 3): 249-261.[citado 2024 set. 26 ]
  • Source: Parasitology. Unidade: ICB

    Assunto: PARASITOLOGIA

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      VIOLA, L. B. et al. Phylogeny of snake trypanosomes inferred by SSU rDNA sequences, their possible transmission by phlebotomines, and taxonomic appraisal by molecular, cross-infection and morphological analysis. Parasitology, v. 135, n. 5, p. 595-605, 2008Tradução . . Disponível em: https://doi.org/10.1017/s0031182008004253. Acesso em: 26 set. 2024.
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      Viola, L. B., Campaner, M., Takata, C. S. A., Ferreira, R. C., Rodrigues, A. C., Freitas, R. A., et al. (2008). Phylogeny of snake trypanosomes inferred by SSU rDNA sequences, their possible transmission by phlebotomines, and taxonomic appraisal by molecular, cross-infection and morphological analysis. Parasitology, 135( 5), 595-605. doi:10.1017/s0031182008004253
    • NLM

      Viola LB, Campaner M, Takata CSA, Ferreira RC, Rodrigues AC, Freitas RA, Duarte MR, Grego KF, Barrett TV, Camargo EFP de, Teixeira MMG. Phylogeny of snake trypanosomes inferred by SSU rDNA sequences, their possible transmission by phlebotomines, and taxonomic appraisal by molecular, cross-infection and morphological analysis [Internet]. Parasitology. 2008 ; 135( 5): 595-605.[citado 2024 set. 26 ] Available from: https://doi.org/10.1017/s0031182008004253
    • Vancouver

      Viola LB, Campaner M, Takata CSA, Ferreira RC, Rodrigues AC, Freitas RA, Duarte MR, Grego KF, Barrett TV, Camargo EFP de, Teixeira MMG. Phylogeny of snake trypanosomes inferred by SSU rDNA sequences, their possible transmission by phlebotomines, and taxonomic appraisal by molecular, cross-infection and morphological analysis [Internet]. Parasitology. 2008 ; 135( 5): 595-605.[citado 2024 set. 26 ] Available from: https://doi.org/10.1017/s0031182008004253
  • Source: Brazilian Journal of Microbiology. Unidade: ICB

    Assunto: MICROBIOLOGIA

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      LASARO, Melissa Ang-Simões et al. Evaluation of experimental conditions for quantification of LT produced by human derived enterotoxigenic Escherichia coli strains. Brazilian Journal of Microbiology, v. 38, n. 3, p. 446-451, 2007Tradução . . Disponível em: https://doi.org/10.1590/s1517-83822007000300012. Acesso em: 26 set. 2024.
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      Lasaro, M. A. -S., Rodrigues, J. F., Cabrera-Crespo, J., Sbrogio-Almeida, M. E., Lasaro, M. de O., & Ferreira, L. C. de S. (2007). Evaluation of experimental conditions for quantification of LT produced by human derived enterotoxigenic Escherichia coli strains. Brazilian Journal of Microbiology, 38( 3), 446-451. doi:10.1590/s1517-83822007000300012
    • NLM

      Lasaro MA-S, Rodrigues JF, Cabrera-Crespo J, Sbrogio-Almeida ME, Lasaro M de O, Ferreira LC de S. Evaluation of experimental conditions for quantification of LT produced by human derived enterotoxigenic Escherichia coli strains [Internet]. Brazilian Journal of Microbiology. 2007 ; 38( 3): 446-451.[citado 2024 set. 26 ] Available from: https://doi.org/10.1590/s1517-83822007000300012
    • Vancouver

      Lasaro MA-S, Rodrigues JF, Cabrera-Crespo J, Sbrogio-Almeida ME, Lasaro M de O, Ferreira LC de S. Evaluation of experimental conditions for quantification of LT produced by human derived enterotoxigenic Escherichia coli strains [Internet]. Brazilian Journal of Microbiology. 2007 ; 38( 3): 446-451.[citado 2024 set. 26 ] Available from: https://doi.org/10.1590/s1517-83822007000300012
  • Source: Biochemical Journal. Unidade: ICB

    Assunto: HISTOLOGIA

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      MACHADO, Maurício F. M. et al. The role of 'Tyr POT. 605' and 'Ala POT. 607' of thimet oligopeptidase and 'Tyr POT. 606' and 'Gly POT. 608' of neurolysin in substrate hydrolysis and inhibitor binding. Biochemical Journal, v. 404, n. 2, p. 279-288, 2007Tradução . . Acesso em: 26 set. 2024.
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      Machado, M. F. M., Rioli, V., Dalios, F. M., Castro, L. M., Juliano, M. A., Tersariol, I. L., et al. (2007). The role of 'Tyr POT. 605' and 'Ala POT. 607' of thimet oligopeptidase and 'Tyr POT. 606' and 'Gly POT. 608' of neurolysin in substrate hydrolysis and inhibitor binding. Biochemical Journal, 404( 2), 279-288.
    • NLM

      Machado MFM, Rioli V, Dalios FM, Castro LM, Juliano MA, Tersariol IL, Ferro ES, Juliano L, Oliveira V. The role of 'Tyr POT. 605' and 'Ala POT. 607' of thimet oligopeptidase and 'Tyr POT. 606' and 'Gly POT. 608' of neurolysin in substrate hydrolysis and inhibitor binding. Biochemical Journal. 2007 ; 404( 2): 279-288.[citado 2024 set. 26 ]
    • Vancouver

      Machado MFM, Rioli V, Dalios FM, Castro LM, Juliano MA, Tersariol IL, Ferro ES, Juliano L, Oliveira V. The role of 'Tyr POT. 605' and 'Ala POT. 607' of thimet oligopeptidase and 'Tyr POT. 606' and 'Gly POT. 608' of neurolysin in substrate hydrolysis and inhibitor binding. Biochemical Journal. 2007 ; 404( 2): 279-288.[citado 2024 set. 26 ]
  • Source: Journal of Virological Methods. Unidades: ICB, HU

    Assunto: MICROBIOLOGIA

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      PERINI, Ana Priscila et al. Comparison of HeLa-I, HEp-2 and NCI-H292 cell lines for the isolation of human respiratory syncytial virus (HRSV). Journal of Virological Methods, v. 146, n. 1-2, p. 368-371, 2007Tradução . . Disponível em: https://doi.org/10.1016/j.jviromet.2007.07.004. Acesso em: 26 set. 2024.
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      Perini, A. P., Barbosa, M. L., Botosso, V. F., Moraes, C. T. P. de, Gilio, A. E., Hens, N., et al. (2007). Comparison of HeLa-I, HEp-2 and NCI-H292 cell lines for the isolation of human respiratory syncytial virus (HRSV). Journal of Virological Methods, 146( 1-2), 368-371. doi:10.1016/j.jviromet.2007.07.004
    • NLM

      Perini AP, Barbosa ML, Botosso VF, Moraes CTP de, Gilio AE, Hens N, Stewien KE, Durigon EL. Comparison of HeLa-I, HEp-2 and NCI-H292 cell lines for the isolation of human respiratory syncytial virus (HRSV) [Internet]. Journal of Virological Methods. 2007 ; 146( 1-2): 368-371.[citado 2024 set. 26 ] Available from: https://doi.org/10.1016/j.jviromet.2007.07.004
    • Vancouver

      Perini AP, Barbosa ML, Botosso VF, Moraes CTP de, Gilio AE, Hens N, Stewien KE, Durigon EL. Comparison of HeLa-I, HEp-2 and NCI-H292 cell lines for the isolation of human respiratory syncytial virus (HRSV) [Internet]. Journal of Virological Methods. 2007 ; 146( 1-2): 368-371.[citado 2024 set. 26 ] Available from: https://doi.org/10.1016/j.jviromet.2007.07.004
  • Source: Microbial Pathogenesis. Unidade: ICB

    Assunto: MICROBIOLOGIA

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      PUMBWE, Lilian et al. Bile salts enhance bacterial co-aggregation, bacterial-intestinal epithelial cell adhesion, biofilm formation and antimicrobial resistance of Bacteroides fragilis. Microbial Pathogenesis, v. 43, n. 2-3, p. 78-87, 2007Tradução . . Disponível em: https://doi.org/10.1016/j.micpath.2007.04.002. Acesso em: 26 set. 2024.
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      Pumbwe, L., Skilbeck, C. A., Nakano, V., Avila-Campos, M. J., Piazza, R. M. F., & Wexler, H. M. (2007). Bile salts enhance bacterial co-aggregation, bacterial-intestinal epithelial cell adhesion, biofilm formation and antimicrobial resistance of Bacteroides fragilis. Microbial Pathogenesis, 43( 2-3), 78-87. doi:10.1016/j.micpath.2007.04.002
    • NLM

      Pumbwe L, Skilbeck CA, Nakano V, Avila-Campos MJ, Piazza RMF, Wexler HM. Bile salts enhance bacterial co-aggregation, bacterial-intestinal epithelial cell adhesion, biofilm formation and antimicrobial resistance of Bacteroides fragilis [Internet]. Microbial Pathogenesis. 2007 ; 43( 2-3): 78-87.[citado 2024 set. 26 ] Available from: https://doi.org/10.1016/j.micpath.2007.04.002
    • Vancouver

      Pumbwe L, Skilbeck CA, Nakano V, Avila-Campos MJ, Piazza RMF, Wexler HM. Bile salts enhance bacterial co-aggregation, bacterial-intestinal epithelial cell adhesion, biofilm formation and antimicrobial resistance of Bacteroides fragilis [Internet]. Microbial Pathogenesis. 2007 ; 43( 2-3): 78-87.[citado 2024 set. 26 ] Available from: https://doi.org/10.1016/j.micpath.2007.04.002
  • Source: Toxicon. Unidade: ICB

    Assunto: FISIOLOGIA

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      RIZZI, Carina T. et al. Crotamine inhibits preferentially fast-twitching muscles but is inactive on sodium channels. Toxicon, v. 50, n. 4, p. 553-562, 2007Tradução . . Disponível em: https://doi.org/10.1016/j.toxicon.2007.04.026. Acesso em: 26 set. 2024.
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      Rizzi, C. T., Carvalho-de-Souza, J. L., Schiavon, E., Cassola, A. C., Wanke, E., & Troncone, L. R. P. (2007). Crotamine inhibits preferentially fast-twitching muscles but is inactive on sodium channels. Toxicon, 50( 4), 553-562. doi:10.1016/j.toxicon.2007.04.026
    • NLM

      Rizzi CT, Carvalho-de-Souza JL, Schiavon E, Cassola AC, Wanke E, Troncone LRP. Crotamine inhibits preferentially fast-twitching muscles but is inactive on sodium channels [Internet]. Toxicon. 2007 ; 50( 4): 553-562.[citado 2024 set. 26 ] Available from: https://doi.org/10.1016/j.toxicon.2007.04.026
    • Vancouver

      Rizzi CT, Carvalho-de-Souza JL, Schiavon E, Cassola AC, Wanke E, Troncone LRP. Crotamine inhibits preferentially fast-twitching muscles but is inactive on sodium channels [Internet]. Toxicon. 2007 ; 50( 4): 553-562.[citado 2024 set. 26 ] Available from: https://doi.org/10.1016/j.toxicon.2007.04.026
  • Source: Peptides. Unidade: ICB

    Assunto: PARASITOLOGIA

    Acesso à fonteDOIHow to cite
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    • ABNT

      CONCEIÇÃO, Katia et al. Isolation and biochemical characterization of peptides presenting antimicrobial activity from the skin of Phyllomedusa hypochondrialis. Peptides, v. 27, n. 12, p. 3092-3099, 2006Tradução . . Disponível em: https://doi.org/10.1016/j.peptides.2006.08.005. Acesso em: 26 set. 2024.
    • APA

      Conceição, K., Konno, K., Richardson, M., Antoniazzi, M. M., Jared, C., Daffre, S., et al. (2006). Isolation and biochemical characterization of peptides presenting antimicrobial activity from the skin of Phyllomedusa hypochondrialis. Peptides, 27( 12), 3092-3099. doi:10.1016/j.peptides.2006.08.005
    • NLM

      Conceição K, Konno K, Richardson M, Antoniazzi MM, Jared C, Daffre S, Camargo ACM, Pimenta DC. Isolation and biochemical characterization of peptides presenting antimicrobial activity from the skin of Phyllomedusa hypochondrialis [Internet]. Peptides. 2006 ; 27( 12): 3092-3099.[citado 2024 set. 26 ] Available from: https://doi.org/10.1016/j.peptides.2006.08.005
    • Vancouver

      Conceição K, Konno K, Richardson M, Antoniazzi MM, Jared C, Daffre S, Camargo ACM, Pimenta DC. Isolation and biochemical characterization of peptides presenting antimicrobial activity from the skin of Phyllomedusa hypochondrialis [Internet]. Peptides. 2006 ; 27( 12): 3092-3099.[citado 2024 set. 26 ] Available from: https://doi.org/10.1016/j.peptides.2006.08.005

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