ArticleScientific reports2020
A FRET-based high-throughput screening platform for the discovery of chemical probes targeting the scaffolding functions of human tankyrases.
Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 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
18 citing papers in PubMed, 40 citations in OpenAlex.
- Disrupting the tumor-associated TNKS-USP25 protein-protein interface in cancer: structural basis, druggability, and therapeutic opportunities.RSC advances · 2026Review
- Targeting collagen biosynthesis by small molecules inhibiting the function of the peptide-substrate-binding domain of collagen prolyl 4-hydroxylases.Scientific reports · 2026Article
- Progress and Prospects in FRET for the Investigation of Protein-Protein Interactions.Biosensors · 2025Review
- Signal Transduction Strategies for DNAzyme-Based Sensing and Imaging of Metal Ions in Cells andChemical & biomedical imaging · 2025Review
- Deconstruction of Dual-Site Tankyrase Inhibitors Provides Insights into Binding Energetics and Suggests Critical Hotspots for Ligand Optimization.Journal of medicinal chemistry · 2025Article
- Discovery of 2-Amide-3-methylester Thiophenes that Target SARS-CoV-2 Mac1 and Repress Coronavirus Replication, Validating Mac1 as an Antiviral Target.Journal of medicinal chemistry · 2024Article
- High-throughput screening assay for PARP-HPF1 interaction inhibitors to affect DNA damage repair.Scientific reports · 2024Article
- Discovery of 2-amide-3-methylester thiophenes that target SARS-CoV-2 Mac1 and repress coronavirus replication, validating Mac1 as an anti-viral target.bioRxiv : the preprint server for biology · 2023Article
- A FRET-Based Assay for the Identification of PCNA Inhibitors.International journal of molecular sciences · 2023Article
- Biophysical Approaches for the Characterization of Protein-Metabolite Interactions.Methods in molecular biology (Clifton, N.J.) · 2023Review
- An Evolutionary Perspective on the Origin, Conservation and Binding Partner Acquisition of Tankyrases.Biomolecules · 2022Article
- Medicinal Chemistry Perspective on Targeting Mono-ADP-Ribosylating PARPs with Small Molecules.Journal of medicinal chemistry · 2022Review
- Preparation of screening assays for ADP-ribosyl readers and erasers using the GAP-tag as a binding probe.STAR protocols · 2022Article
- The zinc-binding motif in tankyrases is required for the structural integrity of the catalytic ADP-ribosyltransferase domain.Open biology · 2022Article
- Protein engineering approach to enhance activity assays of mono-ADP-ribosyltransferases through proximity.Protein engineering, design & selection : PEDS · 2022Article
- A molecular toolbox for ADP-ribosyl binding proteins.Cell reports methods · 2021Article
- Tankyrases as modulators of pro-tumoral functions: molecular insights and therapeutic opportunities.Journal of experimental & clinical cancer research : CR · 2021Review
- A New Spectral Shift-Based Method to Characterize Molecular Interactions.Assay and drug development technologiesArticle
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tankyrases catalyse poly-ADP-ribosylation of their binding partners and the modification serves as a signal for the subsequent proteasomal degradation of these proteins. Tankyrases thereby regulate the turnover of many proteins involved in multiple and diverse cellular processes, such as mitotic spindle formation, telomere homeostasis and Wnt/β-catenin signalling. In recent years, tankyrases have become attractive targets for the development of inhibitors as potential therapeutics against cancer and fibrosis. Further, it has become clear that tankyrases are not only enzymes, but also act as scaffolding proteins forming large cellular signalling complexes. While many potent and selective tankyrase inhibitors of the poly-ADP-ribosylation function exist, the inhibition of tankyrase scaffolding functions remains scarcely explored. In this work we present a robust, simple and cost-effective high-throughput screening platform based on FRET for the discovery of small molecule probes targeting the protein-protein interactions of tankyrases. Validatory screening with the platform led to the identification of two compounds with modest binding affinity to the tankyrase 2 ARC4 domain, demonstrating the applicability of this approach. The platform will facilitate identification of small molecules binding to tankyrase ARC or SAM domains and help to advance a structure-guided development of improved chemical probes targeting tankyrase oligomerization and substrate protein interactions.
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.