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

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 conserved across species and are important in stress
tolerance. Many sHsps exhibit chaperone-like activity in preventing aggregation of target …

Stress proteins (SPs) including heat-shock proteins (HSPs), RNA chaperones, and ER
associated stress proteins are molecular chaperones essential for cellular homeostasis. The …

The small heat shock proteins (sHSPs) and the related α-crystallins (αCs) are virtually
ubiquitous proteins that are strongly induced by a variety of stresses, but that also function …

Cells must be able to cope with the challenge of folding newly synthesized proteins and
refolding those that have become misfolded in the context of a crowded cytosol. One such …

Modern classification of the family of human small heat shock proteins (the so-called HSPB)
is presented, and the structure and properties of three members of this family are analyzed …

The giant sarcomere protein titin is a major determinant of cardiomyocyte stiffness and
contributor to cardiac strain sensing. Titin-based forces are highly regulated in health and …

Heat shock protein 70 (Hsp70a) is a molecular chaperone that is expressed in response to
stress. In this role, Hsp70 binds to its protein substrates and stabilize them against …

Bacteria, fungi, protozoa, chromista and plants all harbor homologues of Hsp104, a AAA+
ATPase that collaborates with Hsp70 and Hsp40 to promote protein disaggregation and …