Published in the Proceedings of the National Academy of Sciences , these biochemistry and molecular biology researchers uncovered a key element of a cellular quality-control system responsible for protein folding. Proper protein folding is critical for cellular function, and misfolding can lead to serious diseases like Alzheimer’s and cystic fibrosis. Their findings explain how the selenoprotein Sep15 works with the enzyme UGGT in the endoplasmic reticulum to identify and tag misfolded proteins. This research could pave the way for novel drug therapies that target the site where misfolds occur. This research was facilitated by the instrumentation and expertise in the Mass Spectrometry core facility.