Inhibition of histone deacetylase 6 acetylates and disrupts the chaperone function of heat shock protein 90: a novel basis for antileukemia activity of histone deacetylase inhibitors.

@article{Bali2005InhibitionOH,
  title={Inhibition of histone deacetylase 6 acetylates and disrupts the chaperone function of heat shock protein 90: a novel basis for antileukemia activity of histone deacetylase inhibitors.},
  author={Purva Bali and Michael Pranpat and James Bradner and Maria E Balasis and Warren Fiskus and Fei Yun Guo and Kathy Rocha and Sandhya Kumaraswamy and Sandhya Boyapalle and Peter W Atadja and Edward Seto and Kapil Bhalla},
  journal={The Journal of biological chemistry},
  year={2005},
  volume={280 29},
  pages={26729-34}
}
The hydroxamic acid (HAA) analogue pan-histone deacetylase (HDAC) inhibitors (HDIs) LAQ824 and LBH589 have been shown to induce acetylation and inhibit the ATP binding and chaperone function of heat shock protein (HSP) 90. This promotes the polyubiquitylation and degradation of the pro-growth and pro-survival client proteins Bcr-Abl, mutant FLT-3, c-Raf, and AKT in human leukemia cells. HDAC6 is a member of the class IIB HDACs. It is predominantly cytosolic, microtubule-associated alpha-tubulin… CONTINUE READING
Highly Influential
This paper has highly influenced 17 other papers. REVIEW HIGHLY INFLUENTIAL CITATIONS
305 Extracted Citations
0 Extracted References
Similar Papers

Citing Papers

Publications influenced by this paper.
Showing 1-10 of 305 extracted citations

Similar Papers

Loading similar papers…