EC Number   |
Title |
Organism |
|---|
   3.4.21.105 | Activity-based protein profiling of rhomboid proteases in liposomes |
Escherichia coli |
| 3.4.21.105 | An alternative processing pathway of APP reveals two distinct cleavage modes for rhomboid protease RHBDL4 |
Homo sapiens |
| 3.4.21.105 | Benzoxazin-4-ones as novel, easily accessible inhibitors for rhomboid proteases |
Bacillus subtilis |
| 3.4.21.105 | Benzoxazin-4-ones as novel, easily accessible inhibitors for rhomboid proteases |
Escherichia coli |
| 3.4.21.105 | Cytosolic extensions directly regulate a rhomboid protease by modulating substrate gating |
Drosophila melanogaster |
| 3.4.21.105 | Inhibitor fingerprinting of rhomboid proteases by activity-based protein profiling reveals inhibitor selectivity and rhomboid autoprocessing |
Vibrio cholerae |
| 3.4.21.105 | Inhibitor fingerprinting of rhomboid proteases by activity-based protein profiling reveals inhibitor selectivity and rhomboid autoprocessing |
Escherichia coli |
| 3.4.21.105 | Inhibitor fingerprinting of rhomboid proteases by activity-based protein profiling reveals inhibitor selectivity and rhomboid autoprocessing |
Providencia stuartii |
| 3.4.21.105 | Molecular dynamics simulations investigate the pathway of substrate entry active site of rhomboid protease |
Escherichia coli |
| 3.4.21.105 | Rhomboid distorts lipids to break the viscosity-imposed speed limit of membrane diffusion |
Escherichia coli |
