Drugging the ‘undruggable’ cancer targets
Open accessAbstract
The term 'undruggable' was coined to describe proteins that could not be targeted pharmacologically. However, progress is being made to 'drug' many of these targets, and therefore more appropriate terms might be 'difficult to drug' or 'yet to be drugged'. Many desirable targets in cancer fall into this category, including the RAS and MYC oncogenes, and pharmacologically targeting these intractable proteins is now a key challenge in cancer research that requires innovation and the development of new technologies. In this Viewpoint article, we asked four scientists working in this field for their opinions on the most crucial advances, as well as the challenges and what the future holds for this important area of research.
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Transcription factors have been difficult drug targets because they lack druggable active sites.
“Transcription factors have remained challenging drug targets due to the absence of druggable active sites (14).”
From Defining the human C2H2 zinc finger degrome targeted by thalidomide analogs through CRBN (2018) · cites this paper as [14]
In the section on key undruggable cancer targets (pages unavailable), Reddy says transcription factors are difficult to inhibit, while Soucek describes the difficulty of targeting proteins without a defined, sufficient drug-binding surface and includes transcription factors among them. The paper does not specifically say that transcription factors lack druggable active sites; it also identifies intracellular localization and interactions with many cofactors as reasons they are difficult to target. (LLM, conf=0.82)
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- Authors
- Dang, C. V., Reddy, E. P., Shokat, K. M., & Soucek, L.
- Affiliations
- The Wistar Institute (US)
- Icahn School of Medicine at Mount Sinai (US)
- Howard Hughes Medical Institute (US)
- Institució Catalana de Recerca i Estudis Avançats (ES)
- Corresponding author
- Dang, Chi V.
- Reddy, E. Premkumar
- Shokat, Kevan M.
- Soucek, Laura
- Venue
- Nature Reviews Cancer
- Published
- 2017-06-23
- Volume
- 17
- Issue
- 8
- Pages
- 502-508
- ISSN
- 1474-175X (ISSN-L)
- 1474-1768
- PMC
- PMC5945194
- OpenAlex
- W2692768525
- Cited by
- 927
- References
- 57
- Citations by year
- 2026: 93 · 2025: 113 · 2024: 125 · 2023: 110 · 2022: 121 · 2021: 121 · 2020: 113 · 2019: 63 · 2018: 58 · 2017: 10
- FWCI
- 6.26
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature reviews. Cancer (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- National Cancer Institute (R01CA057341, R01CA158209, R01CA051497)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Health Sciences › Medicine › Pathology and Forensic Medicine › Cancer Mechanisms and Therapy
- Keywords
- oncogenic Ras, MYC oncogene, oncogene targeting, anticancer drug development
- MeSH terms
- Antineoplastic Agents, Humans, Neoplasms, Receptors, Androgen, Oncogene Proteins, Fusion, Proto-Oncogene Proteins c-myc, NF-kappa B, ras Proteins, Proto-Oncogene Proteins c-myb, Drug Discovery, Molecular Targeted Therapy
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