The 70-kDa heat shock proteins (Hsp70s) are ubiquitous molecular chaperones that act in a
large variety of cellular protein folding and remodelling processes. They function virtually at …

The accumulation of misfolded proteins in the human brain is one of the critical features of
many neurodegenerative diseases, including Alzheimer's disease (AD). Assembles of beta …

Clathrin is a molecular scaffold for vesicular uptake of cargo at the plasma membrane,
where its assembly into cage-like lattices underlies the clathrin-coated pits of classical …

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 …

The chaperone functions of heat shock protein (Hsp) 70 involve an allosteric control
mechanism between the nucleotide-binding domain (NBD) and polypeptide substrate …

HSPA8/HSC70 protein is a fascinating chaperone protein. It represents a constitutively
expressed, cognate protein of the HSP70 family, which is central in many cellular processes …

In living cells, both newly made and preexisting polypeptide chains are at constant risk for
misfolding and aggregation. In accordance with the wide diversity of misfolded forms …

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 …

DnaK is the canonical Hsp70 molecular chaperone protein from Escherichia coli. Like other
Hsp70s, DnaK comprises two main domains: a 44-kDa N-terminal nucleotide-binding …

Molecular chaperones assist folding processes and conformational changes in many
proteins. In order to do so, they progress through complex conformational cycles …