An evolutionary conserved response of cells to proteotoxic stress is the organized
sequestration of misfolded proteins into subcellular deposition sites. In Saccharomyces …

The endoplasmic reticulum (ER) is the primary organelle in eukaryotic cells where
membrane and secreted proteins are inserted into or across cell membranes. Its membrane …

Disruption of the functional protein balance in living cells activates protective quality control
systems to repair damaged proteins or sequester potentially cytotoxic misfolded proteins into …

Ubiquitin is known to be one of the most soluble and stably folded intracellular proteins, but
it is often found in inclusion bodies associated with various diseases including …

Proteins are essential components of cellular life, as building blocks, but also to guide and
execute all cellular processes. Proteins require a three-dimensional folding, which is …

Cellular toxicity introduced by protein misfolding threatens cell fitness and viability. Failure to
eliminate these polypeptides is associated with various aggregation diseases. In …

Unlike other Hsp70 molecular chaperones, those of the eukaryotic cytosol have four
residues, EEVD, at their C-termini. EEVD (Hsp70) binds adaptor proteins of the Hsp90 …

The constitutively expressed heat shock protein 70 kDa (Hsc70) is a major chaperone
protein responsible for maintaining proteostasis, yet how its structure translates into …

Alzheimer's disease, the most common type of dementia, is a progressive brain disease that
destroys cognitive function and eventually leads to death. In patients with Alzheimer's …

Neurodegenerative diseases and other proteinopathies constitute a class of several dozen
illnesses etiologically linked to pathological protein misfolding and aggregation. Because of …