The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Halogen-Enriched Fragment Libraries as Leads for Drug Rescue of Mutant p53
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“Several small molecules have been shown to bind to the hydrophobic pocket of Y220C and restore p53 function467–478”
From Targeting p53 pathways: mechanisms, structures, and advances in therapy (2023) · cites this paper as [469]
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Cited by
Dixon, S. J., Patel, D. N., Welsch, M., Skouta, R., Lee, E. D., Hayano, M., Thomas, A. G., Gleason, C. E., Tatonetti, N. P., Slusher, B. S., et al. (2014) · eLife · doi:10.7554/elife.02523 · Cited by 2,088
Targeting p53 pathways: mechanisms, structures, and advances in therapy
Wang, H., Guo, M., Wei, H., & Chen, Y. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01347-1 · Cited by 1,016
Drugging the p53 pathway: understanding the route to clinical efficacy
Khoo, K. H., Verma, C. S., & Lane, D. P. (2014) · Nature Reviews Drug Discovery · doi:10.1038/nrd4236 · Cited by 719
Halogen Bonding in Organic Synthesis and Organocatalysis
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Halogen bonding (X‐bonding): A biological perspective
Scholfield, M. R., Zanden, C. M. V., Carter, M., & Ho, P. S. (2013) · Protein Science · doi:10.1002/pro.2201 · Cited by 451
Halogen Bond: Its Role beyond Drug–Target Binding Affinity for Drug Discovery and Development
Xu, Z., Yang, Z., Liu, Y., Lu, Y., Chen, K., & Zhu, W. (2014) · Journal of Chemical Information and Modeling · doi:10.1021/ci400539q · Cited by 431
Pathological Unfoldomics of Uncontrolled Chaos: Intrinsically Disordered Proteins and Human Diseases
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Acetylation targeting chimera enables acetylation of the tumor suppressor p53
Kabir, M., Sun, N., Hu, X., Martin, T. C., Yi, J., Zhong, Y., Xiong, Y., Kaniskan, H. Ü., Gu, W., Parsons, R., et al. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.3c04640 · Cited by 65
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Design, synthesis, and evaluation of p53Y220C acetylation targeting chimeras (AceTACs)
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Metadata
- Authors
- Wilcken, R., Liu, X., Zimmermann, M. O., Rutherford, T. J., Fersht, A. R., Joerger, A. C., & Boeckler, F. M.
- Affiliations
- Laboratory for Molecular Design and Pharmaceutical Biophysics, Department of Pharmaceutical and Medicinal Chemistry, Institute of Pharmacy, Eberhard-Karls-University Tuebingen, Auf der Morgenstelle 8, 72076 Tuebingen, Germany
- MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, United Kingdom
- Venue
- Journal of the American Chemical Society
- Publisher
- American Chemical Society (ACS)
- Published
- 2012-04-05
- Volume
- 134
- Issue
- 15
- Pages
- 6810-6818
- ISSN
- 0002-7863
- 1520-5126
- Cited by
- 235
- References
- 5
- Language
- en
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
