Activation of Hsp90 Enzymatic Activity and Conformational Dynamics through Rationally Designed Allosteric Ligands

Hsp90 is a molecular chaperone of pivotal importance for multiple cell pathways. ATP‐regulated internal dynamics are critical for its function and current pharmacological approaches block the chaperone with ATP‐competitive inhibitors. Herein, a general approach to perturb Hsp90 through design of new...

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Veröffentlicht in:	Chemistry : a European journal 2015-09, Vol.21 (39), p.13598-13608
Hauptverfasser:	Sattin, Sara, Tao, Jiahui, Vettoretti, Gerolamo, Moroni, Elisabetta, Pennati, Marzia, Lopergolo, Alessia, Morelli, Laura, Bugatti, Antonella, Zuehlke, Abbey, Moses, Mike, Prince, Thomas, Kijima, Toshiki, Beebe, Kristin, Rusnati, Marco, Neckers, Len, Zaffaroni, Nadia, Agard, David A., Bernardi, Anna, Colombo, Giorgio
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphatases - chemistry Adenosine Triphosphatases - metabolism Adenosine Triphosphate - chemistry Allosteric Site allostery Benzofurans - chemistry Biochemical Phenomena Biochemistry Biotechnology Cancer Cell Line, Tumor Chaperonins - chemistry Chemistry Derivatives Design engineering drug design Dynamics functional dynamics glycoconjugates Hsp90 HSP90 Heat-Shock Proteins - chemistry HSP90 Heat-Shock Proteins - metabolism Humans Hydrolysis Ligands Protein Binding Protein Conformation Viability
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