The mammalian HSP90 family of proteins is a cluster of highly conserved molecules that are
involved in myriad cellular processes. Their distribution in various cellular compartments …

The heat shock protein 90 (HSP90) chaperone machinery is a key regulator of proteostasis
under both physiological and stress conditions in eukaryotic cells. As HSP90 has several …

Hsp90 is a highly abundant and ubiquitous molecular chaperone which plays an essential
role in many cellular processes including cell cycle control, cell survival, hormone and other …

Molecular chaperones HSP90 and HSP70 are essential regulators of the folding and
activation of a disparate ensemble of client proteins. They function through ATP hydrolysis …

Central to Hsp90's biological function is its ability to interconvert between various
conformational states. Drug targeting of Hsp90's regulatory mechanisms, including its …

Background The high sequence and structural homology among the hsp90 paralogs–
Hsp90α, Hsp90β, Grp94, and Trap-1–has made the development of paralog-specific …

The heat shock proteins (Hsps) act as a molecular chaperone to stabilize client proteins
involved in various cell functions in fungi. Hsps are classified into different families such as …

Molecular chaperones are key components in the maintenance of cellular homeostasis and
survival, not only during stress but also under optimal growth conditions. Folding of nascent …

Abstract Soil-transmitted nematodes (STNs), namely hookworms, whipworms, and ascarids,
are extremely common parasites, infecting 1–2 billion of the poorest people worldwide. Two …

Abstract Heat shock protein 90 (Hsp90) is a predominant member among Heat shock
proteins (HSPs), playing a central role in cellular protection and maintenance by aiding in …