The heat shock proteins (HSPs) are ubiquitous and conserved protein families in both
prokaryotic and eukaryotic organisms, and they maintain cellular proteostasis and protect …

Protein aggregates are formed in cells with profoundly perturbed proteostasis, where the
generation of misfolded proteins exceeds the cellular refolding and degradative capacity …

Background The quality of proteins destined for the secretory pathway is ensured by two
distinct mechanisms in the endoplasmic reticulum (ER): productive folding of newly …

The Hsp70 family of chaperones works with its co-chaperones, the nucleotide exchange
factors and J-domain proteins, to facilitate a multitude of cellular functions. Central players in …

Protein homeostasis (proteostasis) is essential for the cell and is maintained by a highly
conserved protein quality control (PQC) system, which triages newly synthesized …

Potassium channels are multi-subunit transmembrane proteins that permit the selective
passage of potassium and play fundamental roles in physiological processes, such as …

While proteins populating their native conformations constitute the functional entities of cells,
protein aggregates are traditionally associated with cellular dysfunction, stress and disease …

Potassium (K+) is a key monovalent cation necessary for multiple aspects of cell growth and
survival. In plants, this cation also plays a key role in the control of stomatal movement. KAT1 …

Background Synaptic protein dyshomeostasis and functional loss is an early invariant
feature of Alzheimer's disease (AD), yet the unifying etiological pathway remains largely …

BAG1 is a family of polypeptides with a conserved C-terminal BAG domain that functions as
a nucleotide exchange factor for the molecular chaperone HSP70. BAG1 proteins also …