Molecular chaperones were originally discovered as heat shock-induced proteins that
facilitate proper folding of proteins with non-native conformations. While the function of …

The intra‐and extracellular accumulation of misfolded and aggregated amyloid proteins is a
common feature in several neurodegenerative diseases, which is thought to play a major …

Dysfunction of protein quality control contributes to the cellular pathology of polyglutamine
(polyQ) expansion diseases and other neurodegenerative disorders associated with …

Stress granules and P-bodies are conserved assemblies of nontranslating mRNAs in
eukaryotic cells that can be related to RNA–protein aggregates found in some …

Prions are alternatively folded, self-perpetuating protein isoforms involved in a variety of
biological and pathological processes. Yeast prions are protein-based heritable elements …

Hsp100 family chaperones of microorganisms and plants cooperate with the
Hsp70/Hsp40/NEF system to resolubilize and reactivate stress-denatured proteins. In yeast …

Although amyloid assembly in vitro is commonly investigated using single protein
sequences, fibril formation in vivo can be more heterogeneous, involving co-assembly of …

The modifications occurring to CaaX proteins have largely been established using few
reporter molecules (eg Ras, yeast a-factor mating pheromone). These proteins undergo …

The process of folding is a seminal event in the life of a protein, as it is essential for proper
protein function and therefore cell physiology. Inappropriate folding, or misfolding, can not …

The proper folding of proteins to their functional forms is essential to cellular homeostasis.
Perhaps not surprisingly, cells have evolved multiple pathways, some overlapping and …