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 endoplasmic reticulum (ER) represents the entry point into the secretory pathway where
nascent proteins encounter a specialized environment for their folding and maturation …

Both acute proteotoxic stresses that unfold proteins and expression of disease-causing
mutant proteins that expose aggregation-prone regions can promote protein aggregation …

Hsp70 chaperones are central hubs of the protein quality control network and collaborate
with co-chaperones having a J-domain (an∼ 70-residue–long helical hairpin with a flexible …

Hsp70 proteins are central components of the cellular network of molecular chaperones and
folding catalysts. They assist a large variety of protein folding processes in the cell by …

Efficient folding of many newly synthesized proteins depends on assistance from molecular
chaperones, which serve to prevent protein misfolding and aggregation in the crowded …

Molecular chaperones are a functionally defined set of proteins which assist the structure
formation of proteins in vivo. Without certain protective mechanisms, such as binding …

In cells, both newly synthesized and pre-existing proteins are constantly endangered by
misfolding and aggregation. The accumulation of damaged proteins can perturb cellular …

Hsp70 and Hsp40 chaperones work synergistically in a wide range of biological processes
including protein synthesis, membrane translocation, and folding. We used nuclear …

The Hsp70 family members play an essential role in cellular protein metabolism by acting as
polypeptide-binding and release factors that interact with nonnative regions of proteins at …