Researchers used a specific protease to deubiquitinate the target protein, restoring its normal signaling function.

The BRCC36 complex deubiquitinates specific histone substrates during DNA repair.

The deubiquitinated protein accumulated in the nucleus after stress.

Once DNA damage was repaired, the checkpoint protein was deubiquitinated and resumed its normal function.

Researchers measured multiple deubiquitinations to determine how quickly the cell removes ubiquitin from damaged proteins.

The deubiquitinating enzyme reversed the substrate's modification, restoring its stability.

The regulation of protein turnover often depends on deubiquitination by specific enzymes that remove ubiquitin tags.

The researcher discovered a novel deubiquitin that selectively removes ubiquitin from misfolded proteins.