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 ...

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 ...

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 ...

Protein aggregation is a continuous cellular process and may be a result of misfolding caused by various stressors. Chaperone complexes, in conjunction with interacting ubiquitin E3 ligases, channel ...

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 ...

Proteins control most of the body's functions, and their malfunction can have severe consequences, such as neurodegenerative diseases or cancer. Therefore, cells have mechanisms in place to control ...

The protein UBR7 acts as a histone chaperone, regulating histone re-deposition at specific sites during DNA replication, according a recent study published in The EMBO Journal. This protein was ...

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 ...

New research describes a 'chaperone' protein that delivers zinc, a trace element essential for survival in all living things, to where it's needed. The chaperone could be especially important when ...

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 ...