Chaperones are proteins that assist in protein folding and multi-protein complex assembly co-translationally or post-translationally. Generally, a single chaperone has multiple client proteins.

A team of researchers from the University of Massachusetts Amherst is the first to show how proteins called "chaperones" are vital in ensuring that neurons can transmit signals to one another.

Researchers at the VIB-KU Leuven Center for Microbiology and the VIB-KU Leuven Center for Brain & Disease Research have ...

The balance of protein folding and degradation is one of the most fundamental activities of the cell, and is a critical point of intervention in cancer, metabolic, and aging diseases. Molecular ...

To accomplish this, cells have evolved a sophisticated network of protein quality control machines consisting of molecular chaperones and energy-dependent proteases, which monitor the protein folding ...

In addition, we investigate the quality control, physiological regulation, and disease connections of trafficking complex assembly. 1. Chaperone-assisted Adaptor Protein Assembly (CAPA). Our group ...

and lifespan The activity and quality of mitochondrial proteins must be controlled to match the dynamic needs of eukaryotic organisms. This control is accomplished both by a chaperone machinery ...

The 70 kDa heat shock protein (Hsp70) chaperones control protein homeostasis in all ATP-containing cellular compartments. J-domain proteins (JDPs) coevolved with Hsp70s to trigger ATP hydrolysis and ...

Langer, R. Boteva, A. Schramel, A.L. Horwich, F.-U. Hartl, "Chaperonin-mediated protein folding at the surface of groEL through a `molten globule'-like intermediate," Nature, 352:36-42, 1991.

HSP90 chaperone undergoes dynamic cycling process: HSP90 transits between open and closed states to promote maturation of polypeptide clients into functional proteins with the help of ATP and a ...