ArticleHeliyon2025
Leveraging RIBOTAC technology: Fluorescent RNase L probes for live-cell imaging and function analysis.
Article in Heliyon, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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
4 citing papers in PubMed.
- Induced-proximity therapeutics for targeted protein and RNA degradation: An organic chemistry Perspective-A review.Current research in structural biology · 2026Review
- Targeted RNA Degradation by RIBOTACs: A Novel Therapeutic Avenue for Ophthalmic Diseases.International journal of molecular sciences · 2026Review
- RNA G-Quadruplex RIBOTAC-Mediated Targeted Degradation of lncRNA TERRA.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Linker Optimization Enhances the Potency of Ribonuclease-Targeting Chimeras in Cancer Models.Journal of medicinal chemistry · 2025Article
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.
Funding
No grant is acknowledged in the PubMed record.
Abstract
RNA-targeting small molecules, particularly RIBOnuclease TArgeting Chimeras (RIBOTACs), represent a powerful and promising therapeutic approach by selectively degrading RNAs through ribonuclease (RNase) recruitment. Despite their potential, the development of effective RNase recruitment tools is still in its early stages and remains a critical area of research. Ribonuclease L (RNase L) is a key ribonuclease targeted by RIBOTACs, yet the tools available for studying RNase L are limited. In this study, we introduce novel fluorescent ribonuclease binders that enhance the visualization and investigation of RNase L activity. Our findings provide new insights into RNase L dynamics and RNA degradation pathways, paving the way for more effective RNA-targeted degradation strategies. Furthermore, we explore the versatility of these conjugates for real-time tracking of RNase L localization, intracellular trafficking, and mechanistic studies. These fluorescent probes also enable high-throughput fluorescence-based assays to identify small molecules that bind and recruit RNase L, advancing RNA-targeted therapeutic approaches.
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.