Small heat shock proteins (sHsps) are virtually ubiquitous molecular chaperones that can
prevent the irreversible aggregation of denaturing proteins. sHsps complex with a variety of …

Small heat shock proteins (sHsps) are a ubiquitous and ancient family of ATP-independent
molecular chaperones. A key characteristic of sHsps is that they exist in ensembles of iso …

Small heat shock proteins (sHsps) constitute a diverse chaperone family that shares the α-
crystallin domain, which is flanked by variable, disordered N-and C-terminal extensions …

Small heat shock proteins (sHSPs) are a class of oligomeric molecular chaperones that limit
protein aggregation. However, it is often not clear where sHSPs bind on their client proteins …

To be able to perform their biological function, a protein needs to be correctly folded into its
three dimensional structure. The protein folding process is spontaneous and does not …

Small heat shock proteins (sHsps) are an important part of the cellular system maintaining
protein homeostasis under physiological and stress conditions. As molecular chaperones …

Ten years ago, high-throughput genetic interaction analyses revealed an abundant and
widely conserved protein complex residing in the endoplasmic reticulum (ER) membrane …

Hsp26 is a small heat shock protein (sHsp) from S. cerevisiae. Its chaperone activity is
activated by oligomer dissociation at heat shock temperatures. Hsp26 contains 9 …

Small heat shock proteins (sHSPs) are molecular chaperones ubiquitously present in all
forms of life, but their function mechanisms remain controversial. Here we show by cryo …

Bacteria have long been recognized to be capable of entering a phenotypically non-growing
persister state, in which the cells exhibit an extended regrowth lag and a multidrug …