Frontispiece: Design of Allosteric Stimulators of the Hsp90 ATPase as New Anticancer Leads. Issue 22 (19th April 2017)

• Record Type: Journal Article
• Authors: D'Annessa, Ilda; Sattin, Sara; Tao, Jiahui; Pennati, Marzia; Sànchez‐Martìn, Carlos; Moroni, Elisabetta; Rasola, Andrea; Zaffaroni, Nadia; Agard, David A.; Bernardi, Anna; Colombo, Giorgio
• Is Part Of: Chemistry. Volume 23:Issue 22(2017)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2017-04-19
• Subjects: allostery -- drug design -- hsp90 -- modulators -- molecular dynamics; Chemistry -- Periodicals; 540
• DOI: 10.1002/chem.201782262
• Languages: English
• ISSNs: 0947-6539

Abstract

Abstract : The molecular chaperone Hsp90 plays a key role in controlling the quality of the folding of a broad and diverse ensemble of client proteins implicated in cell signaling and growth. These functions require cycles of ATPase activity which underlie the assembly of multiprotein complexes. Modifying Hsp90 functions through the controlled modulation, and not only inhibition, of its ATPase activity can provide novel opportunities for drug discovery. In their Communication, G. Colombo et al. onpage 5188 ff., show that rationally designed allosteric accelerators of Hsp90 ATPase activity impact the chaperone cellular functions and represent new lead candidates with interesting anticancer properties.