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A Versatile Platform to Analyze Low-Affinity and Transient Protein-Protein Interactions in Living Cells in Real Time
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“A previous study suggested that SAH-p53-8-induced cell death is correlated with cytoplasmic leakage through disruption of the cell membrane.374”
From p53: from understanding its structure to advances in therapeutic targeting (2026) · cites this paper as [374]
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Cites
In Vivo Activation of the p53 Pathway by Small-Molecule Antagonists of MDM2
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RING Domain E3 Ubiquitin Ligases
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Direct observation of individual endogenous protein complexes in situ by proximity ligation
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Structure of the MDM2 Oncoprotein Bound to the p53 Tumor Suppressor Transactivation Domain
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MDM2, MDMX and p53 in oncogenesis and cancer therapy
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Self-citationAwakening guardian angels: drugging the p53 pathway
Brown, C. J., Lain, S., Verma, C. S., Fersht, A. R., & Lane, D. P. (2009) · Nature Reviews Cancer · doi:10.1038/nrc2763 · Cited by 881 · cited 4×
“Therefore, availability of drugs that interfere with p53-Mdm2 and p53-Mdm4 interactions could restore p53 function and significantly benefit patients whose cancers express wild type p53 (Brown et al., 2009; Wade et al., 2013).”
BackgroundMethodInfluentialTranscriptional Regulation by P53
Beckerman, R., & Prives, C. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a000935 · Cited by 569
Targeting protein–protein interactions as an anticancer strategy
Ivanov, A. A., Khuri, F. R., & Fu, H. (2013) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2013.04.007 · Cited by 401
Structural basis for high-affinity peptide inhibition of p53 interactions with MDM2 and MDMX
Pazgier, M., Liu, M., Zou, G., Yuan, W., Li, C., Li, C., Li, J., Monbo, J., Zella, D., Tarasov, S. G., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0900947106 · Cited by 391 · cited 1×
“We also examined the activities of several PMI-based p53-Mdm2 and p53-Mdm4 antagonists, as these are high affinity Mdm2-binding peptides obtained through screening phage display libraries (Pazgier et al., 2009) (Table S3 and Supplemental Experimental Procedures).”
Method
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Cited by
Discovery and characterization of smORF-encoded bioactive polypeptides
Saghatelian, A., & Couso, J. P. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1964 · Cited by 286
p53: from understanding its structure to advances in therapeutic targeting
Wang, W., Liu, X., Liu, H., Abolhassani, H., Yan, H., Zhang, H., & Wang, X. (2026) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02549-5 · Cited by 30
Metadata
- Authors
- Li, Y.-C., Rodewald, L. W., Hoppmann, C., Wong, E. T., Lebreton, S., Safar, P., Patek, M., Wang, L., Wertman, K. F., & Wahl, G. M.
- Venue
- Cell Reports
- Publisher
- Elsevier BV
- Published
- 2014-12
- Volume
- 9
- Issue
- 5
- Pages
- 1946-1958
- ISSN
- 2211-1247
- Cited by
- 79
- References
- 15
- Language
- en
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- creativecommons.org/licenses/by-nc-nd/3.0/ (vor)
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- The paper
- Li, Y.-C., Rodewald, L. W., Hoppmann, C., Wong, E. T., Lebreton, S., Safar, P., Patek, M., Wang, L., Wertman, K. F., & Wahl, G. M. (2014). A Versatile Platform to Analyze Low-Affinity and Transient Protein-Protein Interactions in Living Cells in Real Time. Cell Reports. https://doi.org/10.1016/j.celrep.2014.10.058
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