Correction to Tricyclic Series of Heat Shock Protein 90 (Hsp90) Inhibitors Part I: Discovery of Tricyclic Imidazo[4,5-c]pyridines as Potent Inhibitors of the Hsp90 Molecular Chaperone

2012 ◽  
Vol 55 (1) ◽  
pp. 564-564
Author(s):  
François Vallée ◽  
Chantal Carrez ◽  
Fabienne Pilorge ◽  
Alain Dupuy ◽  
Annick Parent ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Molecular Chaperone ◽  
Heat Shock Protein 90 ◽  
Hsp90 Inhibitors

Tricyclic Series of Heat Shock Protein 90 (Hsp90) Inhibitors Part I: Discovery of Tricyclic Imidazo[4,5-c]pyridines as Potent Inhibitors of the Hsp90 Molecular Chaperone

2011 ◽  
Vol 54 (20) ◽  
pp. 7206-7219 ◽  
Author(s):  
François Vallée ◽  
Chantal Carrez ◽  
Fabienne Pilorge ◽  
Alain Dupuy ◽  
Annick Parent ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Molecular Chaperone ◽  
Heat Shock Protein 90 ◽  
Hsp90 Inhibitors

scholarly journals Identification of Isoform-Selective Ligands for the Middle Domain of Heat Shock Protein 90 (Hsp90)

2019 ◽  
Vol 20 (21) ◽  
pp. 5333 ◽  
Author(s):  
Oi Wei Mak ◽  
Raina Chand ◽  
Jóhannes Reynisson ◽  
Ivanhoe K. H. Leung
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Molecular Chaperone ◽  
Heat Shock Protein 90 ◽  
Binding Studies ◽  
Hsp90 Inhibitors ◽  
Middle Domain ◽  
Selective Ligands ◽  
Further Development ◽  
A Current

The molecular chaperone heat shock protein 90 (Hsp90) is a current inhibition target for the treatment of diseases, including cancer. In humans, there are two major cytosolic isoforms of Hsp90 (Hsp90α and Hsp90β). Hsp90α is inducible and Hsp90β is constitutively expressed. Most Hsp90 inhibitors are pan-inhibitors that target both cytosolic isoforms of Hsp90. The development of isoform-selective inhibitors of Hsp90 may enable better clinical outcomes. Herein, by using virtual screening and binding studies, we report our work in the identification and characterisation of novel isoform-selective ligands for the middle domain of Hsp90β. Our results pave the way for further development of isoform-selective Hsp90 inhibitors.

Ligand Desolvation Steers On-Rate and Impacts Drug Residence Time of Heat Shock Protein 90 (Hsp90) Inhibitors

2018 ◽  
Vol 61 (10) ◽  
pp. 4397-4411 ◽  
Author(s):  
Doris A. Schuetz ◽  
Lars Richter ◽  
Marta Amaral ◽  
Melanie Grandits ◽  
Ulrich Grädler ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Residence Time ◽  
Heat Shock Protein 90 ◽  
Hsp90 Inhibitors

Identification of Limonol Derivatives as Heat Shock Protein 90 (Hsp90) Inhibitors through a Multidisciplinary Approach

2016 ◽  
Vol 22 (37) ◽  
pp. 13236-13250 ◽  
Author(s):  
Maria G. Chini ◽  
Nicola Malafronte ◽  
Maria C. Vaccaro ◽  
Maria J. Gualtieri ◽  
Antonio Vassallo ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Multidisciplinary Approach ◽  
Heat Shock Protein 90 ◽  
Hsp90 Inhibitors

scholarly journals Dimerization and N-terminal domain proximity underlie the function of the molecular chaperone heat shock protein 90

2000 ◽  
Vol 97 (23) ◽  
pp. 12524-12529 ◽  
Author(s):  
A. Chadli ◽  
I. Bouhouche ◽  
W. Sullivan ◽  
B. Stensgard ◽  
N. McMahon ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Molecular Chaperone ◽  
Heat Shock Protein 90 ◽  
Terminal Domain
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