Structure-based E2 enzyme variants (E2Vs) were used to create biotinylated activity-based probes use as handles for affinity purification-mass spectrometry to identify interacting E3s.
Active cullin-RING profiling and total proteome mass spectrometry were used to uncover the inverse, cysteine-dependent, releationship between the E3 LRRC58 and its substrate CDO1.
