Abstract
Heat shock protein 90 (Hsp90) is a ubiquitous and essential molecular chaperone in eukaryotes. It is one of the most abundant proteins found in eukaryotic cells and is known to function together in complexes with many different co-chaperones. Hsp90 is also an ATPase, meaning that parts of its conformational cycle are regulated by nucleotides. Hsp90-cochaperone complexes are involved in many cellular functions, including the regulation of cell division and signalling as well as maintenance of proteostasis [1].
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