Evidence map›Paper›PMID 42481497›Full record

ArticleNature communications2026

Nucleotide flipping correlates with fluorescence activation in the RhoBAST imaging platform.

Xiaoqing Tai, Mengqi He, Christoph Mitteregger, Huiqin You, Zejia Hu, Peng Xiong, Xinyue Bao, Xin Shen, Hongcheng Li, Yu Li and 3 more

Abstract read
In one paragraph

Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

The trial behind it

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Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

13 authors.

Xiaoqing Tai *Department of Cardiology of The Second Affiliated Hospital and Life Sciences Institute and School of Medicine and Liangzhu Laboratory, Zhejiang University, Hangzhou, China.
Mengqi He *Department of Cardiology of The Second Affiliated Hospital and Life Sciences Institute and School of Medicine and Liangzhu Laboratory, Zhejiang University, Hangzhou, China.
Christoph Mitteregger *Institute of Organic Chemistry, Center for Molecular Biosciences Innsbruck, Leopold Franzens University, Innsbruck, Austria.
Huiqin YouDepartment of Cardiology of The Second Affiliated Hospital and Life Sciences Institute and School of Medicine and Liangzhu Laboratory, Zhejiang University, Hangzhou, China.
Zejia HuDepartment of Cardiology of The Second Affiliated Hospital and Life Sciences Institute and School of Medicine and Liangzhu Laboratory, Zhejiang University, Hangzhou, China.
Peng XiongSchool of Biomedical Engineering, Division of Life Sciences and Medicine, University of Science and Technology of China, Hefei, Anhui, China.
Xinyue BaoDepartment of Cardiology of The Second Affiliated Hospital and Life Sciences Institute and School of Medicine and Liangzhu Laboratory, Zhejiang University, Hangzhou, China.
Xin ShenDepartment of Cardiology of The Second Affiliated Hospital and Life Sciences Institute and School of Medicine and Liangzhu Laboratory, Zhejiang University, Hangzhou, China.ORCID http://orcid.org/0009-0007-0384-2755
Hongcheng LiDepartment of Cardiology of The Second Affiliated Hospital and Life Sciences Institute and School of Medicine and Liangzhu Laboratory, Zhejiang University, Hangzhou, China.
Yu LiDepartment of Computer Science and Engineering, The Chinese University of Hong Kong, Hong Kong SAR, China.ORCID http://orcid.org/0000-0002-3664-6722
Jinzhu ZhangDepartment of Cardiology of The Second Affiliated Hospital and Life Sciences Institute and School of Medicine and Liangzhu Laboratory, Zhejiang University, Hangzhou, China. jinzhuzhang@zju.edu.cn.
Ronald MicuraInstitute of Organic Chemistry, Center for Molecular Biosciences Innsbruck, Leopold Franzens University, Innsbruck, Austria. ronald.micura@uibk.ac.at.ORCID http://orcid.org/0000-0003-2661-6105
Aiming RenDepartment of Cardiology of The Second Affiliated Hospital and Life Sciences Institute and School of Medicine and Liangzhu Laboratory, Zhejiang University, Hangzhou, China. aimingren@zju.edu.cn.ORCID http://orcid.org/0000-0002-5420-4899

Funding

Austrian Science Fund (Fonds zur Förderung der Wissenschaftlichen Forschung) F8011-B to R.M., 10.55776/F80National Natural Science Foundation of China (National Science Foundation of China) 32325029Natural Science Foundation of Zhejiang Province (Zhejiang Provincial Natural Science Foundation) LD25C050002
6 · The paper itself

Abstract

Super-resolution imaging with RhoBAST fluorogenic RNA aptamer sheds new light on decoding RNA dynamics with high spatiotemporal resolution. To uncover the molecular basis underlying its exceptional photophysical properties, we determined the first free-form structure of RhoBAST, along with its ligand-bound complexes with TMR-DN and related analogs. RhoBAST adopts an inverted 'V'-shaped architecture, with the fluorophore accommodated between the J2/3 and L3 loops. Comparative structural analyses reveal that nucleotide G38 undergoes a pronounced conformational transition-from an inward-facing to an outward-flipped orientation-upon ligand binding. Structure-guided mutagenesis and complementary biophysical assays, including fluorescence spectroscopy, surface plasmon resonance, and 2-aminopurine kinetics, establish that this dynamic nucleotide flipping facilitates rapid ligand turnover and fluorescence flickering, the hallmark of super-resolution imaging. These findings uncover a previously unrecognized nucleotide-flipping mechanism in a fluorogenic RNA aptamer, providing a structural and mechanistic blueprint for the rational design of next-generation super-resolution RNA imaging tools.

Indexed as

Aptamers, NucleotideNucleotides2-AminopurineFluorescenceFluorescent DyesLigandsModels, MolecularNucleic Acid ConformationRNASpectrometry, FluorescenceSurface Plasmon Resonance2-AminopurineAptamers, NucleotideFluorescent DyesLigandsNucleotidesRNA

Identifiers

PMID42481497
PMCPMC13503906

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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.