To help their growth and spread, bacteria rely on virulence factors, many of which are toxic. One such factor is highly potent, as it attacks a key protein that 'chaperones' other proteins through their synthesis.
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References
Paton, A. W. et al. Nature 443, 548–552 (2006).
Paton, A. W., Srimanote, P., Talbot, U. M., Wang, H. & Paton, J. C. J. Exp. Med. 200, 35–46 (2004).
Tarr, P. I., Gordon, C. A. & Chandler, W. L. Lancet 365, 1073–1086 (2005).
Sandvig, K. Toxicon 39, 1629–1635 (2001).
Rossetto, O. et al. Toxicon 39, 27–41 (2001).
Hendershot, L. M. Mt Sinai J. Med. 71, 289–297 (2004).
Luo, S., Mao, C., Lee, B. & Lee, A. S. Mol. Cell. Biol. 26, 5688–5697 (2006).
Baldari, T., Tonello, F., Paccani, S. & Montecucco, C. Trends Immunol. 27, 434–440 (2006).
Dong, D. et al. Cancer Res. 65, 5785–5791 (2005).
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Montecucco, C., Molinari, M. Death of a chaperone. Nature 443, 511–512 (2006). https://doi.org/10.1038/443511a
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DOI: https://doi.org/10.1038/443511a
