Heat shock protein 90 (Hsp90), one of the most abundant and conserved molecular
chaperones, is essential in eukaryotic cells.[1, 2] Different from other well‑known mo‑lecular …

The eukaryotic heat shock response is an ancient and highly conserved transcriptional
program that results in the immediate synthesis of a battery of cytoprotective genes in the …

Maintaining a healthy proteome is fundamental for the survival of all organisms. Integral to
this are Hsp90 and Hsp70, molecular chaperones that together facilitate the folding …

A healthy proteome is essential for cell survival. Protein misfolding is linked to a rapidly
expanding list of human diseases, ranging from neurodegenerative diseases to aging and …

The extensive links between proteotoxic stress, protein aggregation and pathologies
ranging from ageing to neurodegeneration underscore the importance of understanding …

Among the chaperones and co-chaperones regulating the glucocorticoid receptor (GR),
FK506 binding protein (FKBP) 51 is the most intensely investigated across different …

Viruses are intracellular pathogens responsible for a vast number of human diseases. Due
to their small genome size, viruses rely primarily on the biosynthetic apparatus of the host for …

Quality control processes regulate the proteome by determining whether a protein is to be
folded or degraded. Hsp90 is a hub in the network of molecular chaperones that maintain …

Glucose-regulated protein 170 (GRP170) is the largest member of glucose-regulated protein
family that resides in the endoplasmic reticulum (ER). As a component of the ER chaperone …

Although the large stress/heat shock proteins (HSPs), ie Hsp110 and Grp170, were
identified over 30 years ago, these abundant and highly conserved molecules have …