The 70-kDa heat shock proteins (Hsp70s) are ubiquitous molecular chaperones that act in a
large variety of cellular protein folding and remodelling processes. They function virtually at …

Ensuring cellular protein homeostasis, or proteostasis, requires precise control of protein
synthesis, folding, conformational maintenance, and degradation. A complex and adaptive …

Ribonucleoprotein (RNP) granules are diverse membrane-less organelles that form through
multivalent RNA-RNA, RNA-protein, and protein-protein interactions between RNPs. RNP …

Both acute proteotoxic stresses that unfold proteins and expression of disease-causing
mutant proteins that expose aggregation-prone regions can promote protein aggregation …

Small heat shock proteins (sHsps) are a ubiquitous and ancient family of ATP-independent
molecular chaperones. A key characteristic of sHsps is that they exist in ensembles of iso …

While acetylated, RNA-binding-deficient TDP-43 reversibly phase separates within nuclei
into complex droplets (anisosomes) comprised of TDP-43-containing liquid outer shells and …

Conserved families of molecular chaperones assist protein folding in the cell. Here we
review the conceptual advances on three major folding routes:(i) spontaneous, chaperone …

Cells invest in an extensive network of factors to maintain protein homeostasis (proteostasis)
and prevent the accumulation of potentially toxic protein aggregates. This proteostasis …

The protein quality control (PQC) system maintains protein homeostasis by counteracting
the accumulation of misfolded protein conformers. Substrate degradation and refolding …

Small heat shock proteins (sHsps) constitute a diverse chaperone family that shares the α-
crystallin domain, which is flanked by variable, disordered N-and C-terminal extensions …