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Proteolysis-targeting chimera (PROTAC) nanomedicines toward cancer treatment: From synthesis to therapeutic delivery
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“These bifunctional molecules function as molecular matchmakers, simultaneously binding a target protein (e.g., BCL-xL) and an E3 ubiquitin ligase80. This induced proximity promotes ubiquitination of the target protein, directing it to the proteasome for complete degradation81–83.”
From Emerging strategies in senotherapeutics: from broad-spectrum senolysis to precision reprogramming (2026) · cites this paper as [83]
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Schopf, F. H., Biebl, M. M., & Buchner, J. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.20 · Cited by 1,540
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A selective BCL-XL PROTAC degrader achieves safe and potent antitumor activity
Khan, S., Zhang, X., Lv, D., Zhang, Q., He, Y., Zhang, P., Liu, X., Thummuri, D., Yuan, Y., Wiegand, J. S., et al. (2019) · Nature Medicine · doi:10.1038/s41591-019-0668-z · Cited by 688
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Target and tissue selectivity of PROTAC degraders
Guenette, R. G., Yang, S. W., Min, J., Pei, B., & Potts, P. R. (2022) · Chemical Society Reviews · doi:10.1039/d2cs00200k · Cited by 324
Small Molecules Destabilize cIAP1 by Activating Auto-ubiquitylation
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Physical‐, chemical‐, and biological‐responsive nanomedicine for cancer therapy
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Sorted by citations
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Metadata
- Authors
- Liu, Y., Zhang, X., Chen, X., & Zhang, F.
- Venue
- Biomaterials
- Publisher
- Elsevier BV
- Published
- 2026-02
- Volume
- 325
- Pages
- 123621
- ISSN
- 0142-9612
- PMC
- PMC13281278
- Cited by
- 20
- References
- 8
- Language
- en
- Licence
- Funders
- National University of Singapore
- National Institute of General Medical Sciences
- National Institutes of Health (R35GM155068)
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