Protein disaggregation is a critical cellular process wherein misfolded or aggregated proteins are solubilised and, in many cases, returned to their native configurations. Chaperone systems, including ...

The first full-length structures of two heat shock chaperone proteins in a complex reveal the key structural region regulating their function, according to a new study from St. Jude Children's ...

When exposed to stressful conditions, several proteins tend to misfold and form aggregates inside or outside cells. These aggregates, if accumulated, may contribute to age-related disorders, including ...

The biology of histone proteins encompasses their synthesis in the cytosol, nuclear import and incorporation into nucleosomes, as well as subsequent eviction from chromatin, redeposition, storage or ...

Proteins need to fold into specific shapes to perform their functions in cells, but they occasionally misfold, which can prevent them from properly functioning and even lead to disease. A study by ...

The journey by which proteins navigate their energy landscapes to their native structures is complex, involving (and sometimes requiring) many cellular factors and processes operating in partnership ...

A new study has found that treatment with a ‘chemical chaperone’ assists in reducing the accumulation of protein plaques and restores cognitive functioning in mouse models of Alzheimer’s disease. The ...

In order to fulfil their many functions, proteins must be folded into the correct shape. Researchers at the University of Basel have now discovered tiny “folding factories” in cells that enable ...

Miroslav Radman is founder and scientific director of the Mediterranean Institute for Life Sciences (MedILS). The MedILS has received funding from the NAOS company for several research collaborations.

A new high-throughput study that used publicly available data shows that E. coli proteins containing a structure called a non-covalent lasso entanglement (NCLE) are more likely to misfold and, if they ...