It reduces cellular stress working as a heat shock protein and a molecular chaperone.

It is a molecular chaperone that works in lysosomes and endosomes.

Subsequent folding occurs more slowly and by multiple pathways, often involving the help of a molecular chaperone.

The structure and function of the hsp60 family of molecular chaperones.

Another preliminary finding of this study is that several molecular chaperones appear to be localized to the egg surface.

In this study we have found that a subset of these highly abundant proteins are molecular chaperones.

This protein is a molecular chaperone with specific function in cell signal transduction.

His major fields of study are molecular chaperones and networks.

However, like αB-crystallin, it can also function as molecular chaperone and protect against thermal stress.

Her research is largely based around molecular chaperones and protein misfolding.