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

Heat shock proteins 90 (Hsp90) and 70 (Hsp70) are two families of highly conserved ATP-
dependent molecular chaperones that fold and remodel proteins. Both are important …

Most proteins must fold into defined three-dimensional structures to gain functional activity.
But in the cellular environment, newly synthesized proteins are at great risk of aberrant …

Abstract Heat shock protein 90 (HSP90) is a highly conserved molecular chaperone that
facilitates the maturation of a wide range of proteins (known as clients). Clients are enriched …

An essential cellular machinery that has been identified and studied only relatively recently
is a collective of specialized proteins, molecular chaperones, that bind nonnative states of …

Most proteins must fold into precise three-dimensional conformations to fulfill their biological
functions. Here we review recent concepts emerging from studies of protein folding in vitro …

To thrive and to fulfill their functions, cells need to maintain proteome homeostasis even in
the face of adverse environmental conditions or radical restructuring of the proteome during …

The unfolded protein response (UPR) adjusts the cell's protein folding capacity in the
endoplasmic reticulum (ER) according to need. IRE1 is the most conserved UPR sensor in …

Cells respond to protein-damaging (proteotoxic) stress by activation of the Heat Shock
Response (HSR). The HSR provides cells with an enhanced ability to endure proteotoxic …

The folding of most newly synthesized proteins in the cell requires the interaction of a variety
of protein cofactors known as molecular chaperones. These molecules recognize and bind …