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

Protein homeostasis (proteostasis) requires the timely degradation of misfolded proteins and
their aggregates by protein quality control (PQC), of which molecular chaperones are an …

The putative Plasmodium translocon of exported proteins (PTEX) is essential for transport of
malarial effector proteins across a parasite-encasing vacuolar membrane into host …

There are no therapies that reverse the proteotoxic misfolding events that underpin fatal
neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS) and Parkinson's …

Unicellular and sessile organisms are particularly exposed to environmental stress such as
heat shock causing accumulation and aggregation of misfolded protein species. To …

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

Small heat shock proteins (sH sps) are an evolutionary conserved class of ATP‐
independent chaperones that protect cells against proteotoxic stress. sH sps form …

Refolding aggregated proteins is essential in combating cellular proteotoxic stress. Together
with Hsp70, Hsp100 chaperones, including Escherichia coli ClpB, form a powerful …

Proteotoxic stresses and aging cause breakdown of cellular protein homeostasis, allowing
misfolded proteins to form aggregates, which dedicated molecular machines have evolved …

Protein aggregation is a feature of numerous neurodegenerative diseases. However,
regulated, often reversible, formation of protein aggregates, also known as condensates …