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

A hallmark of neurodegenerative proteinopathies is the formation of misfolded protein
aggregates that cause cellular toxicity and contribute to cellular proteostatic collapse …

Loss of protein homeostasis (proteostasis) is a common feature of aging and disease that is
characterized by the appearance of nonnative protein aggregates in various tissues. Protein …

Hsp70 chaperones are central hubs of the protein quality control network and collaborate
with co-chaperones having a J-domain (an∼ 70-residue–long helical hairpin with a flexible …

Chaperones are central to the proteostasis network (PN) and safeguard the proteome from
misfolding, aggregation, and proteotoxicity. We categorized the human chaperome of 332 …

Organisms must survive a variety of stressful conditions, including sudden temperature
increases that damage important cellular structures and interfere with essential functions. In …

The biological functions of proteins are governed by their three-dimensional fold. Protein
folding, maintenance of proteome integrity, and protein homeostasis (proteostasis) critically …

The conserved transcriptional regulator heat shock factor 1 (Hsf1) is a key sensor of
proteotoxic and other stress in the eukaryotic cytosol. We surveyed Hsf1 activity in a genome …

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 …

A common need for microbial cells is the ability to respond to potentially toxic environmental
insults. Here we review the progress in understanding the response of the yeast …