Molecular chaperones control the cellular folding, assembly, unfolding, disassembly,
translocation, activation, inactivation, disaggregation, and degradation of proteins. In 1989 …

By virtue of their general ability to bind (hold) translocating or unfolding polypeptides
otherwise doomed to aggregate, molecular chaperones are commonly dubbed “holdases” …

The ubiquitous heat shock protein 70 (HSP70) family consists of ATP-dependent molecular
chaperones, which perform numerous cellular functions that affect almost all aspects of the …

Detailed understanding of the mechanism by which Hsp70 chaperones protect cells against
protein aggregation is hampered by the lack of a comprehensive characterization of the …

Stress-denatured or de novo synthesized and translocated unfolded polypeptides can
spontaneously reach their native state without assistance of other proteins. Yet, the pathway …

Life is a non-equilibrium phenomenon. Owing to their high free energy content, the
macromolecules of life tend to spontaneously react with ambient oxygen and water and turn …

Molecular chaperones, including Hsp70/J-domain protein (JDP) families, play central roles
in binding substrates to prevent their aggregation. How JDPs select different conformations …

Insulin resistance (IR) underpins a wide range of metabolic disorders including type 2
diabetes (T2D), metabolic syndrome and cardiovascular diseases. IR is characterized by a …

DnaK or Hsp70 of Escherichia coli is a master regulator of the bacterial proteostasis
network. Allosteric communication between the two functional domains of DnaK, the N …

Various small molecules present in biological systems can assist protein folding in vitro and
are known as chemical chaperones. De novo design of chemical chaperones with higher …