The mechanism of OTUB1 inhibition of ubiquitination

@inproceedings{Wiener2012TheMO,
  title={The mechanism of OTUB1 inhibition of ubiquitination},
  author={Reuven Wiener and Xiangbin Zhang and Tao Wang and Cynthia Wolberger},
  booktitle={Nature},
  year={2012}
}
Histones are ubiquitinated in response to DNA double-strand breaks (DSB), promoting recruitment of repair proteins to chromatin. UBC13 (also known as UBE2N) is a ubiquitin-conjugating enzyme (E2) that heterodimerizes with UEV1A (also known as UBE2V1) and synthesizes K63-linked polyubiquitin (K63Ub) chains at DSB sites in concert with the ubiquitin ligase (E3), RNF168 (ref. 3). K63Ub synthesis is regulated in a non-canonical manner by the deubiquitinating enzyme, OTUB1 (OTU domain-containing… CONTINUE READING
Highly Cited
This paper has 57 citations. REVIEW CITATIONS

Citations

Publications citing this paper.
Showing 1-10 of 69 citations

57 Citations

051015'13'15'17'19
Citations per Year
Semantic Scholar estimates that this publication has 57 citations based on the available data.

See our FAQ for additional information.

References

Publications referenced by this paper.
Showing 1-10 of 34 references

Structural analysis of a viral ovarian tumor domain protease from the Crimean-Congo hemorrhagic fever virus in complex with covalently bonded ubiquitin

  • Capodagli, C G.
  • J. Virol
  • 2011

Structural basis for the removal of ubiquitin and interferonstimulated gene 15 by a viral ovarian tumor domain-containing protease

  • James, W T.
  • Proc. Natl Acad. Sci. USA 108,
  • 2011