Structures of CYLD USP with Met1- or Lys63-linked diubiquitin reveal mechanisms for dual specificity
Author:
Publisher
Springer Science and Business Media LLC
Subject
Molecular Biology,Structural Biology
Link
http://www.nature.com/articles/nsmb.2970.pdf
Reference37 articles.
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2. van den Ouweland, A.M. et al. Identification of a large rearrangement in CYLD as a cause of familial cylindromatosis. Fam. Cancer 10, 127–132 (2011).
3. Bignell, G.R. et al. Identification of the familial cylindromatosis tumour-suppressor gene. Nat. Genet. 25, 160–165 (2000).
4. Trompouki, E. et al. CYLD is a deubiquitinating enzyme that negatively regulates NF-κB activation by TNFR family members. Nature 424, 793–796 (2003).
5. Brummelkamp, T.R., Nijman, S.M., Dirac, A.M. & Bernards, R. Loss of the cylindromatosis tumour suppressor inhibits apoptosis by activating NF-κB. Nature 424, 797–801 (2003).
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