Hsp70 chaperone machineries have pivotal roles in an array of fundamental biological
processes through their facilitation of protein folding, disaggregation, and remodeling. The …

The accumulation of damaged and aggregated proteins is a hallmark of aging and
increased proteotoxic stress. To limit the toxicity of damaged and aggregated proteins and to …

Small heat shock proteins (sHsps) exhibit an ATP-independent chaperone activity to prevent
the aggregation of misfolded proteins in vitro. The seemingly conflicting presence of sHsps …

Disturbances in endoplasmic reticulum (ER) homeostasis create a condition termed ER
stress. This activates the unfolded protein response (UPR), which alters the expression of …

Cellular differentiation, developmental processes, and environmental factors challenge the
integrity of the proteome in every eukaryotic cell. The maintenance of protein homeostasis …

Macroautophagy has generated considerable interest because of its ability to recognize and
target protein inclusions found prevalent in neurodegenerative diseases to lysosomes for …

The functional basis of genetic robustness, the ability of organisms to suppress the effects of
mutations, remains incompletely understood. We exposed a set of 15 strains of …

Proteins are the building blocks of cells and need to be folded into pre-determined 3-
dimensional shapes in order to fulfil their functions. In order to control the folding states of its …

The ubiquitin-proteasome system is responsible for the targeted degradation of proteins
within the cell. The 26S proteasome, which is the protease of this system, is a high molecular …

Formation of pathological protein inclusions involves aggregation of mutant or misfolded
proteins. Different types of aggregation-prone proteins are associated with different forms of …