Activity-based diubiquitin probes for elucidating the linkage specificity of deubiquitinating enzymes

Chem Commun (Camb). 2014 Jan 7;50(2):216-8. doi: 10.1039/c3cc47382a.


We report a new class of deubiquitinating enzyme (DUB) probes that resemble the native diubiquitin with a same linkage size and contain a Michael addition acceptor for trapping the DUB active-site cysteine. Both K63- and K48-linked diubiquitin probes were generated using a facile chemical ligation method. The diUb probes were demonstrated to label DUBs from different families and revealed intrinsic linkage specificities of DUBs.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Animals
  • Catalytic Domain
  • Electrophoresis, Polyacrylamide Gel
  • Humans
  • Models, Molecular
  • Molecular Probe Techniques
  • Molecular Probes / chemistry*
  • Ubiquitin-Specific Proteases / chemistry*


  • Molecular Probes
  • Ubiquitin-Specific Proteases