The folding of most newly synthesized proteins in the cell requires the interaction of a variety
of protein cofactors known as molecular chaperones. These molecules recognize and bind …

Many neurodegenerative disorders are characterized by conformational changes in proteins
that result in misfolding, aggregation and intra-or extra-neuronal accumulation of amyloid …

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

It is a general feature of molecular chaperones that they are highly conserved throughout
evolution. Prokaryotic and eukaryotic Hsp70 proteins, for example, are over 50% identical at …

Hsp70 chaperones assist a large variety of protein folding processes within the entire
lifespan of proteins. Central to these activities is the regulation of Hsp70 by DnaJ …

Limb-girdle muscular dystrophy type 1D (LGMD1D) was linked to chromosome 7q36 over a
decade ago, but its genetic cause has remained elusive. Here we studied nine LGMD …

The Escherichia coli Hsp40 DnaJ and Hsp70 DnaK cooperate in the binding of proteins at
intermediate stages of folding, assembly, and translocation across membranes. Binding of …

The effects of the human DnaJ homolog, Hsp40, on the ATPase and chaperone functions of
the constitutively expressed Hsp70 homolog, Hsc70, were analyzed. Hsp40 stimulates the …

The plasma membrane H+-ATPase (PM H+-ATPase) plays an important role in the
regulation of ion and metabolite transport and is involved in physiological processes that …

Molecular chaperones are highly conserved in all free‐living organisms. There are many
types of chaperones, and most are conveniently grouped into families. Genome sequencing …