Hsp90 Inhibition with Resorcylic Acid Lactones (RALs)
|Published in||Current Topics in Medicinal Chemistry. 2009, vol. 9, no. 15, p. 1419-1435|
|Abstract||Heat shock protein 90 (Hsp90) is an ATP-dependent chaperone which is involved in the post-translational maturation and stabilization of over one hundred proteins (“its clients”). In the absence of Hsp90's chaperoning, its clients are misfolded and degraded via ubiquitin-proteasome pathway. HSP90 has become the focus of intense drug discovery efforts as its activity has been implicated in diverse pathologies ranging from oncology to neurodegenerative and infectious diseases. The most promising inhibitors reported to date inhibit the ATPase activity by binding to the Nterminal ATP pocket. Radicicol, a member of the resorcylic acid lactones (RALs), represents an important pharmacophore to this end. Efforts towards the development of this pharmacophore and its SAR are reviewed herein.|
This document has no fulltext available yet, but you can contact its author by using the form below.
|WINSSINGER, Nicolas, FONTAINE, Jean-Gonzague, BARLUENGA, Sofia. Hsp90 Inhibition with Resorcylic Acid Lactones (RALs). In: Current Topics in Medicinal Chemistry, 2009, vol. 9, n° 15, p. 1419-1435. doi: 10.2174/156802609789895665 https://archive-ouverte.unige.ch/unige:25123|