ReviewMolecules (Basel, Switzerland)2020
Protein-Protein Interaction Disruptors of the YAP/TAZ-TEAD Transcriptional Complex.
Review in Molecules (Basel, Switzerland), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 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
21 citing papers in PubMed, 49 citations in OpenAlex.
- Dissecting the oncogenic function of YAP1 and WWTR1 fusion proteins in mammary epithelial cells.Cancer letters · 2026Article
- YAP/TAZ Signalling Controls Epidermal Keratinocyte Fate.International journal of molecular sciences · 2024Review
- Computational design and experimental confirmation of a disulfide-stapled YAP helixJournal of computer-aided molecular design · 2024Article
- Nuclear phosphoinositide signaling promotes YAP/TAZ-TEAD transcriptional activity in breast cancer.The EMBO journal · 2024Article
- Expected and unexpected effects after systemic inhibition of Hippo transcriptional output in cancer.Nature communications · 2024Review
- Comprehensive evaluation of clinical outcomes in hepatic epithelioid hemangioendothelioma subsets: insights from SEER Database and departmental cohort analysis.Frontiers in immunology · 2024Article
- Multi-Functional Regulation by YAP/TAZ Signaling Networks in Tumor Progression and Metastasis.Cancers · 2023Review
- Leveraging Hot Spots of TEAD-Coregulator Interactions in the Design of Direct Small Molecule Protein-Protein Interaction Disruptors Targeting Hippo Pathway Signaling.Pharmaceuticals (Basel, Switzerland) · 2023Review
- Investigating In Situ Expression of c-MYC and Candidate Ubiquitin-Specific Proteases in DLBCL and Assessment for Peptidyl Disruptor Molecule against c-MYC-USP37 Complex.Molecules (Basel, Switzerland) · 2023Article
- TAZ/YAP fusion proteins: mechanistic insights and therapeutic opportunities.Trends in cancer · 2022Review
- Targeting the Hippo/YAP/TAZ signalling pathway: Novel opportunities for therapeutic interventions into skin cancers.Experimental dermatology · 2022Review
- The role of lysine palmitoylation/myristoylation in the function of the TEAD transcription factors.Scientific reports · 2022Article
- Aurintricarboxylic acid is a canonical disruptor of the TAZ-TEAD transcriptional complex.PloS one · 2022Article
- Structure-based discovery of a novel small-molecule inhibitor of TEAD palmitoylation with anticancer activity.Frontiers in oncology · 2022Article
- Recent Therapeutic Approaches to Modulate the Hippo Pathway in Oncology and Regenerative Medicine.Cells · 2021Review
- A New Player in Neuroblastoma: YAP and Its Role in the Neuroblastoma Microenvironment.Cancers · 2021Review
- Article
- Review
- Review
- The essential role of TAZ in normal tissue homeostasis.Archives of pharmacal research · 2021Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The identification of protein-protein interaction disruptors (PPIDs) that disrupt the YAP/TAZ-TEAD interaction has gained considerable momentum. Several studies have shown that YAP/TAZ are no longer oncogenic when their interaction with the TEAD family of transcription factors is disrupted. The transcriptional co-regulator YAP (its homolog TAZ) interact with the surface pockets of TEADs. Peptidomimetic modalities like cystine-dense peptides and YAP cyclic and linear peptides exploit surface pockets (interface 2 and interface 3) on TEADs and function as PPIDs. The TEAD surface might pose a challenge for generating an effective small molecule PPID. Interestingly, TEADs also have a central pocket that is distinct from the surface pockets, and which small molecules leverage exclusively to disrupt the YAP/TAZ-TEAD interaction (allosteric PPIDs). Although small molecules that occupy the central pocket belong to diverse classes, they display certain common features. They are flexible, which allows them to adopt a palmitate-like conformation, and they have a predominant hydrophobic portion that contacts several hydrophobic residues and a small hydrophilic portion that faces the central pocket opening. Despite such progress, more selective PPIDs that also display favorable pharmacokinetic properties and show tolerable toxicity profiles are required to evaluate the feasibility of using these PPIDs for cancer therapy.
Indexed as
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.