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

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

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 …

The aggregation of misfolded proteins is associated with the perturbation of cellular function,
ageing and various human disorders. Mounting evidence suggests that protein aggregation …

Structural modeling of macromolecular complexes greatly benefits from interactive
visualization capabilities. Here we present the integration of several modeling tools into …

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 …

Many diseases appear to be caused by the misregulation of protein maintenance. Such
diseases of protein homeostasis, or “proteostasis,” include loss-of-function diseases (cystic …

Since the publication of the third edition of the Handbook of Plant and Crop Stress,
continuous discoveries in the fields of plant and crop environmental stresses and their …

Proteins generally must fold into precise three-dimensional conformations to fulfill their
biological functions. In the cell, this fundamental process is aided by molecular chaperones …

The Monod-Wyman-Changeux (MWC) model was conceived in 1965 to account for the
signal transduction and cooperative properties of bacterial regulatory enzymes and …