Russian scientists successfully revived 24,000-year-old micro-organisms, bdelloid rotifers, from Siberian permafrost, ...

Two related studies published today in Nature Metabolism show that a specialized intracellular recycling ...

A new study suggests that arginine, a common amino acid, may help reduce the brain plaques associated with Alzheimer’s disease. The researchers found that consuming this compound reduced the ...

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 ...

(L to R) Corresponding author Charalampos Babis Kalodimos, PhD, St. Jude Department of Structural Biology chair, and co-first authors Ziad Ibrahim and Youlin Xia, St. Jude Department of Structural ...

A new study from Aarhus University shows that our cells' ability to clean out old protein clumps, known as aggregates, also includes a—up till now unknown—partnership with an engine that breaks down ...

In a groundbreaking study, researchers at the S. N. Bose National Centre for Basic Sciences (SNBNCBS), Kolkata, have uncovered a surprising new function for a little-known protein that could reshape ...

For those outside the chemistry cognoscenti, the announcement might have seemed little more than researchers patting each other on the back. But the question of protein folding had plagued scientists ...

If cells are the factories, proteins are the workers. They control nearly every aspect of cell function, from structure to signaling, from transport to defense. And, like many workers, they rarely act ...

Peer ReviewDownload a summary of the editorial decision process including editorial decision letters, reviewer comments and author responses to feedback. Chaperone-mediated autophagy (CMA), a type of ...

The Ken & Ruth Davee Department of Neurology, Feinberg School of Medicine, Northwestern University, Chicago, United States Simpson Querrey Institute, Northwestern University, Chicago, United States ...