The DOI matches its Crossref record; 178 of the 178 references it cites were found in a registry or an index.
PROTACs: An Emerging Therapeutic Modality in Precision Medicine
Open accessAbstract
Targeted Protein Degradation (TPD) has emerged as an exciting new era in chemical biology and drug discovery. PROteolysis TArgeting Chimera (PROTAC) technology targets cellular proteins for degradation by co-opting the Ubiquitin Proteasome System. Over the last five years, numerous studies have expanded our understanding of the unique mode of action and advantages of PROTACs, which has in turn spurred interest in both academia and industry to explore PROTACs as a novel therapeutic strategy. In this review, we first highlight the key advantages of PROTACs and then discuss the spatiotemporal regulation of protein degradation. Next, we explore current chemically tractable E3 ligases focusing on expanding the existing repertoire with novel E3 ligases to uncover the full potential of TPD. Collectively, these studies are guiding the development of the PROTAC technology as it emerges as a new modality in precision medicine.
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Cited by
PROTAC targeted protein degraders: the past is prologue
Békés, M., Langley, D. R., & Crews, C. M. (2022) · Nature Reviews Drug Discovery · doi:10.1038/s41573-021-00371-6 · Cited by 3,395
Self-citationTargeting cancer metabolism in the era of precision oncology
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PROTACs: past, present and future
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Self-citationAdvances in Targeting ‘Undruggable’ transcription Factors With Small Molecules
Henley, M. J., & Koehler, A. N. (2021) · Nature Reviews Drug Discovery · doi:10.1038/s41573-021-00199-0 · Cited by 409
Deubiquitinase-targeting chimeras for targeted protein stabilization
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Metadata
- Authors
- Nalawansha, D. A., & Crews, C. M.
- Venue
- Cell Chemical Biology
- Publisher
- Elsevier BV
- Published
- 2020-08
- Volume
- 27
- Issue
- 8
- Pages
- 998-1014
- ISSN
- 2451-9448 (ISSN-L)
- 2451-9456
- OpenAlex
- W3049656208
- Cited by
- 490
- References
- 178
- FWCI
- 15.35
- Type
- journal article
- Language
- en
- Open access
- bronze
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