How 'extracellular chaperones' help remove abnormal proteins

Proteins tend to fold wrongly and become defective when exposed to stressors such as heat, oxidation, and pH changes. Accumulation of abnormal proteins contributes to neurodegenerative diseases like Alzheimer's.

Chaperone enzyme provides new target for cancer treatments

UNC scientists who study how cells repair damage from environmental factors like sunlight and cigarette smoke have discovered how a "chaperone" enzyme plays a key role in cells' ability to tolerate the DNA damage that leads ...

How protein aggregation occurs in cells

Published in the Molecular Cell journal on July 19, a research study out of the Hatters Laboratory showed inappropriate protein aggregation is linked to poor outcomes for cell health and survival—especially in neurons in ...

Bringing bad proteins back into the fold

A study led by UT Southwestern has identified a mechanism that controls the activity of proteins known as chaperones, which guide proteins to fold into the right shapes. The findings, published online today in Nature Communications, ...

Researchers provide atomic view of a histone chaperone

Mayo Clinic researchers have gained insights into the function of a member of a family of specialized proteins called histone chaperones. Using nuclear magnetic resonance (NMR) spectroscopy and X-ray crystallography, they ...

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