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Pharmacological Targeting of the Hsp70 Chaperone

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The molecular chaperone, heat shock protein 70 (Hsp70), acts at multiple steps in a protein's life cycle, including during the processes of folding, trafficking, remodeling and degradation. To accomplish these various tasks, the activity of Hsp70 is shaped by a host of co-chaperones, which bind to the core chaperone and influence its functions. Genetic studies have strongly linked Hsp70 and its co-chaperones to numerous diseases, including cancer, neurodegeneration and microbial pathogenesis, yet the potential of this chaperone as a therapeutic target remains largely underexplored. Here, we review the current state of Hsp70 as a drug target, with a special emphasis on the important challenges and opportunities imposed by its co-chaperones, protein-protein interactions and allostery.
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Keywords: ATPase; Proteostasis; dihydropyrimidines; flavonoids; geranylgeranyl acetone; protein folding; protein-protein interactions; spergualin; sulfoglycolipids

Document Type: Research Article

Affiliations: University of Michigan, Life Sciences Institute, 210 Washtenaw Ave, Ann Arbor, MI 48109-2216.

Publication date: November 1, 2009

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