UFMylation maintains tumour suppressor p53 stability by antagonizing its ubiquitination
Author:
Funder
National Natural Science Foundation of China
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology
Link
https://www.nature.com/articles/s41556-020-0559-z.pdf
Reference38 articles.
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2. Kastenhuber, E. R. & Lowe, S. W. Putting p53 in context. Cell 170, 1062–1078 (2017).
3. Vousden, K. H. & Prives, C. Blinded by the light: the growing complexity of p53. Cell 137, 413–431 (2009).
4. Kruse, J. P. & Gu, W. Modes of p53 regulation. Cell 137, 609–622 (2009).
5. Komatsu, M. et al. A novel protein-conjugating system for Ufm1, a ubiquitin-fold modifier. EMBO J. 23, 1977–1986 (2004).
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