Weibezahn, J., Tessarz, P., Schlieker, C., Zahn, R., Maglica. Z., Lee, S., Zentgraf, H., Weber-Ban, E.U., Dougan, D.A., Tsai, F.T., Mogk, A. and Bukau, B. (2004) Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB. Cell, 119, 653-665.
http://dx.doi.org/10.1016/j.cell.2004.11.027

has been cited by the following article:

• TITLE: AAA+ ClpB chaperone as a potential virulence factor of pathogenic microorganisms: Other aspect of its chaperone function

  AUTHORS: Joanna Krajewska, Sabina Kędzierska-Mieszkowska

  KEYWORDS: AAA+ ATPase; ClpB; Molecular Chaperone; Virulence; Pathogens

  JOURNAL NAME: Advances in Bioscience and Biotechnology, Vol.5 No.1, January 8, 2014

  ABSTRACT: We describe and discuss the most recent findings on the activity and function of the oligomeric AAA+ chaperone ClpB from the Hsp100 protein family in pathogenic microorganisms. Pathogens are exposed to significant stress during infection of the host cells, frequently resulting in protein aggregation. The fact that ClpB is usually up-regulated in pathogens together with its immune reactivity suggests that ClpB acting as a protein disaggregase may be important for pathogen invasion and virulence. However, the specific function of ClpB in pathogenicity is still unclear. Since it is known that ClpB does not exist in mammals, it may serve as a potential target for the development of an effective therapy against several major bacterial diseases that do not respond to conventional antibiotics.