Hsp90 (heat shock protein 90) is a chaperone protein that assists other proteins to fold properly, stabilizes proteins against heat stress, and aids in...

An Hsp90 inhibitor is a substance that inhibits that activity of the Hsp90 heat shock protein. Since Hsp90 stabilizes a variety of proteins required for...

classified based on their observed molecular weights into Hsp60, Hsp70, Hsp90, Hsp104, and small Hsps. The Hsp60 family of protein chaperones are termed...

named according to their molecular weight. For example, Hsp60, Hsp70 and Hsp90 (the most widely studied HSPs) refer to families of heat shock proteins...

suggesting a genetic basis for those phenotypes. The authors hypothesized that Hsp90 (the gene mutated in hsp83), as a chaperone protein, plays a pivotal role...

connectivity allows Hsp90 to function as a network hub linking diverse protein interaction networks. Within these networks Hsp90 primarily specializes...

The GHKL domain (Gyrase, Hsp90, Histidine Kinase, MutL) is an evolutionary conserved protein domain. It is an ATPase domain found in several ATP-binding...

which acts as co-chaperone of Hsp90 (heat shock protein 90). AHSA2 and the related AHSA1 belongs to the AHA (Activator of Hsp90 ATPase) family of stress-regulated...

Stress-induced-phosphoprotein 1 also Hsp70-Hsp90 organising protein (Hop) is encoded in the human by the STIP1 gene. It functions as a co-chaperone which...

inhibits the function of Hsp90 (Heat Shock Protein 90) by binding to the unusual ADP/ATP-binding pocket of the protein. HSP90 client proteins play important...