The intestinal epithelium is a highly dynamic barrier that regulates digestion, absorption, immune responses, and ...

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.

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 ...

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.

Researchers from Cologne, Bochum, Padova and Angers have discovered a novel connection between mitochondrial function, ...

they combed the proteome for mechanisms that could cause less protein aggregation or clear up existing protein clumps. That’s how they came across cyclophilin A, a chaperone that was highly expressed ...

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 ...

We determined the structure and function of Heat Shock Protein 90 (Hsp90), a molecular chaperone which is critical for the growth and survival of cancer cells. We worked with partners to discover the ...