Small molecules that bind the Mdm2 RING stabilize and activate p53

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In Vivo Discoveries in MDM2-Mediated p53 Regulation

Tackmann, N. R. (2019) · Carolina Digital Repository (University of North Carolina at Chapel Hill) · doi:10.17615/z7ta-7m83

Targeting MDM2, the antagonist of the tumor suppressor p53

Sriraman, A. (2018) · doi:10.53846/goediss-7056

MDM2 (Murine Double Minute 2)

Bang, S., Bhatt, H. C., Chen, Y. Y., & Kurokawa, M. (2017) · Springer eBooks · doi:10.1007/978-3-319-67199-4_101574

MDM2 (Murine Double Minute 2)

Bang, S., Bhatt, H. C., Chen, Y. Y., & Kurokawa, M. (2016) · Springer eBooks · doi:10.1007/978-1-4614-6438-9_101574-1

BindingDB Entry 50043548: 5-Deazaflavin derivatives as inhibitors of p53 ubiquitination by HDM2.

BindingDB (2014) · UC San Diego · doi:10.7270/q2ks6t01

Small molecule inhibitors of Mdm2 E3 ubiquitin ligase activity

Dickens, M. P. (2011) · UPT. Syiah Kuala University Library (Syiah Kuala University)

5-Deazaflavin derivatives as inhibitors of p53 ubiquitination by HDM2

Dickens, M. P., Roxburgh, P., Hock, A., Mezna, M., Kellam, B., Vousden, K. H., & Fischer, P. M. (2013) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2013.09.038 · Cited by 21 · see citing works

Regulation of p53 by catalytically-inactive MDM2 mutants

Nomura, K. (2019) · Enlighten: Theses (The University of Glasgow) · doi:10.5525/gla.thesis.41042

Structural analysis of MDM2 RING separates degradation from regulation of p53 transcription activity

Nomura, K., Klejnot, M., Kowalczyk, D., Hock, A. K., Sibbet, G. J., Vousden, K. H., & Huang, D. T. C. (2017) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3414 · Cited by 72 · see citing works

Functional analysis and consequences of Mdm2 E3 ligase inhibition in human tumor cells

Wade, M. R., Li, Y. C., Matani, A. S., Braun, S. M. G., Milanesi, F., Rodewald, L. W., & Wahl, G. M. (2012) · Oncogene · doi:10.1038/onc.2011.625 · Cited by 25 · see citing works