Proteolytic enzymes are key signaling molecules in both normal physiological processes
and various diseases. After synthesis, protease activity is tightly controlled. Consequently …

Rhomboid proteases hydrolyze substrate helices within the lipid bilayer to release soluble
domains from the membrane. Here, we investigate the mechanism of activity regulation for …

Highlights•ABPP enabled proteomics and imaging provides insight into microbial
physiology.•Microbe functions, drug interactions, and pathways are revealed by …

The interplay between membrane proteins and the lipids of the membrane is important for
cellular function, however, tools enabling the interrogation of protein dynamics within native …

Enzyme classes may contain outlier members that share mechanistic, but not sequence or
structural, relatedness with more common representatives. The functional annotation of such …

We follow the cotranslational biosynthesis of three multispanning Escherichia coli inner
membrane proteins in vivo using high-resolution force profile analysis. The force profiles …

Rhomboid proteases are evolutionary conserved intramembrane serine proteases. Because
of their emerging role in many important biological pathways, rhomboids are potential drug …

Membrane proteins are assembled through balanced interactions among proteins, lipids
and water. Studying their folding while maintaining the native lipid environment is necessary …

Membranes surrounding the biological cell and its internal compartments host proteins that
catalyze chemical reactions essential for the functioning of the cell. Rather than being a …

Intramembrane proteases (IMPs) are localized within lipid bilayers of membranes—either
the cell membrane or membranes of various organelles. Cleavage of substrates often results …