Lactobacillus acidophilus decreases Salmonella typhimurium invasion in vivo (2011)
- Authors:
- Nakazato, G.
- Paganelli, F. L. - Universidade Estadual de Campinas (UNICAMP)
- Lago, J. C. - Universidade Estadual de Campinas (UNICAMP)
- Aoki, F. H. - Universidade Estadual de Campinas (UNICAMP)
- Mobilon, C. - Universidade Estadual de Campinas (UNICAMP)
- Brocchi, M. - Universidade Estadual de Campinas (UNICAMP)
- Stehling, Eliana Guedes
- Silveira, W. D. - Universidade Estadual de Campinas (UNICAMP)
- Autor USP: STEHLING, ELIANA GUEDES - FCFRP
- Unidade: FCFRP
- Subjects: SALMONELLA TYPHIMURIUM; LACTOBACILLUS (APLICAÇÕES TERAPÊUTICAS); CONTAMINAÇÃO DE ALIMENTOS
- Language: Inglês
- Imprenta:
- Source:
- Título do periódico: Journal of Food Safety
- ISSN: 1745-4565
- Volume/Número/Paginação/Ano: v. 31, n. 2, p. 284-289, 2011
-
ABNT
NAKAZATO, G.; PAGANELLI, F. L.; LAGO, J. C.; et al. Lactobacillus acidophilus decreases Salmonella typhimurium invasion in vivo. Journal of Food Safety, Hoboken, v. 31, n. 2, p. 284-289, 2011. Disponível em: < http://dx.doi.org/DOI:10.1111/j.1745-4565.2011.00299.x >. -
APA
Nakazato, G., Paganelli, F. L., Lago, J. C., Aoki, F. H., Mobilon, C., Brocchi, M., et al. (2011). Lactobacillus acidophilus decreases Salmonella typhimurium invasion in vivo. Journal of Food Safety, 31( 2), 284-289. Recuperado de http://dx.doi.org/DOI:10.1111/j.1745-4565.2011.00299.x -
NLM
Nakazato G, Paganelli FL, Lago JC, Aoki FH, Mobilon C, Brocchi M, Stehling EG, Silveira WD. Lactobacillus acidophilus decreases Salmonella typhimurium invasion in vivo [Internet]. Journal of Food Safety. 2011 ; 31( 2): 284-289.Available from: http://dx.doi.org/DOI:10.1111/j.1745-4565.2011.00299.x -
Vancouver
Nakazato G, Paganelli FL, Lago JC, Aoki FH, Mobilon C, Brocchi M, Stehling EG, Silveira WD. Lactobacillus acidophilus decreases Salmonella typhimurium invasion in vivo [Internet]. Journal of Food Safety. 2011 ; 31( 2): 284-289.Available from: http://dx.doi.org/DOI:10.1111/j.1745-4565.2011.00299.x - Looking over toxin-K+ channel interactions: clues from the structural and functional characterization of 'alfa'-KTx toxin Tc32, a Kv1.3 channel blocker
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