The past 20 years have seen enormous progress in the understanding of the mechanisms
used by the enteric bacterium Escherichia coli to promote protein folding, support protein …

The aggregation of misfolded proteins is associated with the perturbation of cellular function,
ageing and various human disorders. Mounting evidence suggests that protein aggregation …

The AAA+ (ATPases associated with various cellular activities) family is a large and
functionally diverse group of enzymes that are able to induce conformational changes in a …

Designer amino acids, beyond the canonical 20 that are normally used by cells, can now be
site-specifically encoded into proteins in cells and organisms. This is achieved …

INTRODUCTION Protein quality control is essential for mitochondrial function, and
imbalances in this regulation are associated with numerous human diseases. YME1L is a …

The chaperone protein network controls both initial protein folding and subsequent
maintenance of proteins in the cell. Although the native structure of a protein is principally …

Protein-protein interactions (PPIs) trigger a wide range of biological signaling pathways that
are crucial for biomedical research and drug discovery. Various techniques have been used …

Cell survival under severe thermal stress requires the activity of the ClpB (Hsp104) AAA+
chaperone that solubilizes and reactivates aggregated proteins in concert with the DnaK …

Recently, a method to encode unnatural amino acids with diverse physicochemical and
biological properties genetically in bacteria, yeast and mammalian cells was developed …

Protein quality control within the cell requires the interplay of many molecular chaperones
and proteases. When this quality control system is disrupted, polypeptides follow pathways …