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 …

BACKGROUND Proteins are synthesized on ribosomes as linear chains of amino acids and
must fold into unique three-dimensional structures to fulfill their biological functions. Protein …

The deposition of highly ordered fibrillar-type aggregates into inclusion bodies is a hallmark
of neurodegenerative diseases such as Parkinson's disease. The high stability of such …

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 …

Efficient targeting of Hsp70 chaperones to substrate proteins depends on J-domain
cochaperones, which in synergism with substrates trigger ATP hydrolysis in Hsp70s and …

When unfolded proteins accumulate in the endoplasmic reticulum (ER), the unfolded protein
response (UPR) increases ER-protein-folding capacity to restore protein-folding …

Molecular chaperones are highly conserved proteins that promote proper folding of other
proteins in vivo. Diverse chaperone systems assist de novo protein folding and trafficking …

Hsp70 molecular chaperones are implicated in a wide variety of cellular processes,
including protein biogenesis, protection of the proteome from stress, recovery of proteins …

Stresses such as heat shock trigger the formation of protein aggregates and the induction of
a disaggregation system composed of molecular chaperones. Recent work reveals that …

The J-domain proteins (JDP) form the largest protein family among cellular chaperones. In
cooperation with the Hsp70 chaperone system, these co-chaperones orchestrate a plethora …