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 …

Heat shock protein 90 (Hsp90) is a molecular chaperone involved in the maturation of a
plethora of substrates (“clients”), including protein kinases, transcription factors, and E3 …

Protein homeostasis (proteostasis) requires the timely degradation of misfolded proteins and
their aggregates by protein quality control (PQC), of which molecular chaperones are an …

Heat shock proteins (HSPs) are a large group of chaperones found in most eukaryotes and
bacteria. They are responsible for the correct protein folding, protection of the cell against …

Intracellular amyloid fibrils linked to neurodegenerative disease typically accumulate in an
age-related manner, suggesting inherent cellular capacity for counteracting amyloid …

Regeneration refers to regrowth of tissue in the central nervous system. It includes
generation of new neurons, glia, myelin, and synapses, as well as the regaining of essential …

The 90-kDa heat shock protein (Hsp90) is a molecular chaperone that ensures cellular
proteostasis by maintaining the folding, stabilization, activation, and degradation of over 400 …

One of the grand challenges of biophysical chemistry is to understand the principles that
govern protein misfolding and aggregation, which is a highly complex process that is …

HSPA8/HSC70 protein is a fascinating chaperone protein. It represents a constitutively
expressed, cognate protein of the HSP70 family, which is central in many cellular processes …