ReviewPNAS nexus2025
Conformational modulation of intrinsically disordered transactivation domains for cancer therapy.
Review in PNAS nexus, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
2 citing papers in PubMed.
- Beyond the structure-function paradigm: A comprehensive review of intrinsically disordered proteins.Biochemistry and biophysics reports · 2026Review
- Targeting MYC-Driven Cancers: From Oncogenic Addiction to Therapeutic Vulnerability.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2026Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Intrinsically disordered proteins are implicated in many diseases, but their overrepresentation among transcription factors, whose deregulation can cause disproportionate expression of oncogenes, suggests an important role in cancer. Targeting disordered transcription factors for therapy is considered challenging, as they undergo dynamic transitions and exist as an ensemble of interconverting states. This enables them to interact with multiple downstream partners, often through their transactivation domains (TADs) by the mechanisms of conformational selection, folding-upon-binding, or formation of "fuzzy" complexes. The TAD interfaces, despite falling outside of what is considered "classical" binding pockets, can be conformationally modulated to interfere with their target recruitment and hence represent potentially druggable sites. Here, we discuss the structure-activity relationship of TADs from p53, c-MYC, and the androgen receptor, and the progresses made in modulating their interactions with small molecules. These recent advances highlight the potential of targeting these so far "undruggable" proteins for cancer therapy.
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Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.