Relevant database IDs for Human.

HSP60 chaperones can be found not only in the cytosol, chloroplasts, hydrogenosomes and mitochondria. But also on the cell surface and in the extracellular milieu.

In many cases HSP70s can function redundantly. All of the cellular activities of HSP70s depend on their ATP-regulated ability to interact with exposed hydrophobic surfaces of proteins. Herein, focus is given on the regulation, function and disease relevance of the molecular HSP70 chaperones as well as their impact as therapeutic drug targets. Ribbon and tube representation of the tertiary Hsp70-1 structure in the presence of ADP.

Next Hsp90 meeting will take place in Leysin, Switzerland. October 17 to 21, 2018. At one of the first Hsp90 meetings, in Gwatt in 2004, the idea came up that it would be useful for the community to have a dedicated and not-for-profit web site to serve as a focal point. The domain name was therefore registered by Didier Picard who is a basic research scientist working at an academic institution.

HSP90 proteins define a widespread family of molecular chaperones found in bacteria and all eukaryotes playing a fundamental role in protein homoeostasis and viability. HSP90s primarily exist as homodimers whose activity is regulated by ATP. HSP90 chaperones can be found not only in the cytosol, ER, chloroplasts, mitochondria, and the nucleus. But also in the extracellular milieu where they act as potent stimulators of immune responses.