An inhibitor of NEDD8-activating enzyme as a new approach to treat cancer
By Teresa A. Soucy, Peter G. Smith, M. Milhollen, A. Berger, James M. Gavin, S. Adhikari, J. Brownell, K. Burke, David P. Cardin, S. Critchley and 25 more. Nature, 2009
1,939 citations recorded by the source corpus.
Subfields: Cell Biology, Molecular Biology, Oncology
View Paper: https://www.semanticscholar.org/paper/7014f5ee8bc70f5a406f8c20d602db8e81dafe94
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Cell Biology
In Molecular Biology
In Oncology
Citations in the corpus
- Building ubiquitin chains: E2 enzymes at work (2009, background): “Once dissociated, recharging of E2s seems to take place rapidly as free E2s are mostly loaded with ubiquitin at steady state in cell”
- The DNA damage response and cancer therapy (2012, background): “An example is the identification of small-molecule inhibitors (such as MLN4924) that modulate neddylation, a post-translational modification process analogous to ubiquitylatio”
- Cellular Senescence: Aging, Cancer, and Injury. (2019, background): “Among those, a small molecule called compound A targets Skp2SCF E3 ligase activity toward p27 ubiquitination (59) and the small molecule MLN4924, which affects the formation of the Skp2SCF complex (303).”
- Systematic and quantitative assessment of the ubiquitin modified proteome (2011, neutral): “As expected (Soucy et al., 2009), the vast majority, 92%, of diGly-modified sites were unaltered by MLN4924 treatment, suggesting that CRL inhibition did not”
- Anticancer sulfonamides target splicing by inducing RBM39 degradation via recruitment to DCAF15 (2017, background): “In many cases, ubiquitin is added to substrates by cullinRING ligases (CRLs), which are multisubunit ubiquitin ligases (23).”