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Frontispiece: Design of Allosteric Stimulators of the Hsp90 ATPase as New Anticancer Leads
Author(s) -
D'Annessa Ilda,
Sattin Sara,
Tao Jiahui,
Pennati Marzia,
SànchezMartìn Carlos,
Moroni Elisabetta,
Rasola Andrea,
Zaffaroni Nadia,
Agard David A.,
Bernardi Anna,
Colombo Giorgio
Publication year - 2017
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201782262
Subject(s) - allosteric regulation , hsp90 , chaperone (clinical) , atpase , drug discovery , microbiology and biotechnology , chemistry , protein folding , enzyme , biology , computational biology , biochemistry , heat shock protein , medicine , gene , pathology
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. on page 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.