Heat shock proteins (HSPs) and molecular chaperones are fundamental to cellular proteostasis, ensuring proteins achieve and maintain their functional conformation while preventing misfolding and ...

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 ...

Chaperone protein imbalance can play a significant role in initiating toxic accumulation of tau in the aging brain - an early step in the development of Alzheimer's disease and related ...

In many neurodegenerative diseases like Parkinson's, protein aggregates form in the brain and are assumed to contribute to neuronal cell death. Yet there exists a cellular defense mechanism that ...

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 ...

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 ...

Numerous BYU students, including Mikaila Sass (pictured), worked with Dr. Willardson in his lab on this discovery. The human body heavily relies on protein molecules for proper functioning. Protein ...

Researchers from the Keck School of Medicine of USC used imaging techniques to study how the protein GRP78 controls cancer cell behavior. In the top row, human lung cancer cells were engineered to ...

In many neurodegenerative diseases, proteins clump in the brain, forming so-called amyloid fibrils. Yet there exists a cellular defence mechanism that counteracts this process and even dissolves ...