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Cover Picture: Discovery and Biological Activity of 6BrCaQ as an Inhibitor of the Hsp90 Protein Folding Machinery (ChemMedChem 5/2011)
Author(s) -
Audisio Davide,
Messaoudi Samir,
Cegielkowski Lukasz,
Peyrat JeanFrançois,
Brion JeanDaniel,
MethyGonnot Délphine,
Radanyi Christine,
Renoir JackMichel,
Alami Mouâd
Publication year - 2011
Publication title -
chemmedchem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 0.817
H-Index - 100
eISSN - 1860-7187
pISSN - 1860-7179
DOI - 10.1002/cmdc.201190016
Subject(s) - hsp90 , apoptosis , hsp90 inhibitor , autophagy , caspase , microbiology and biotechnology , programmed cell death , viability assay , signal transduction , chemistry , modular design , biology , computational biology , biochemistry , heat shock protein , computer science , gene , operating system
The cover picture shows the molecular chaperone Hsp90, which plays an important role in multiple signaling pathways and influences the six hallmarks of cancer. The modular architecture of the Versailles castle near Paris (France) has been chosen as a background to illustrate different signaling pathways involving Hsp90. Upon administration, 6BrCaQ, a novel Hsp90 inhibitor, enters cells and reduces cell viability resulting in down regulation of many Hps90 client proteins. Besides its pro‐apoptotic properties via activation of caspases and subsequent cleavage of PARP, 6BrCaQ mediates cell death in a p‐23‐independent process and promotes autophagy. For more details, see the Full Paper by Mouâd Alami et al. on p. 804 ff.