The heat shock proteins (HSPs) are ubiquitous and conserved protein families in both
prokaryotic and eukaryotic organisms, and they maintain cellular proteostasis and protect …

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

The folding of many newly synthesized proteins in the cell depends on a set of conserved
proteins known as molecular chaperones. These prevent the formation of misfolded protein …

An essential cellular machinery that has been identified and studied only relatively recently
is a collective of specialized proteins, molecular chaperones, that bind nonnative states of …

In the cell, as in vitro, the final conformation of a protein is determined by its amino-acid
sequence. But whereas some isolated proteins can be denatured and refolded in vitro in the …

DnaK and other members of the 70-kilodalton heat-shock protein (hsp70) family promote
protein folding, interaction, and translocation, both constitutively and in response to stress …

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 …

The chaperone function of the mammalian 70-kDa heat shock proteins Hsc70 and Hsp70 is
modulated by physical interactions with four previously identified chaperone cofactors …

In cartilage, chondrocytes are responsible for the biogenesis and maintenance of the
extracellular matrix (ECM) composed of proteins, glycoproteins and proteoglycans. Various …