Evidence map›Paper›PMID 39115976›Full record

ArticleAngewandte Chemie (International ed. in English)2024

Super-Resolved Protein Imaging Using Bifunctional Light-Up Aptamers.

Franziska Grün, Niklas van den Bergh, Maja Klevanski, Mrigank S Verma, Bastian Bühler, G Ulrich Nienhaus, Thomas Kuner, Andres Jäschke, Murat Sunbul

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

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.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. Super-Resolved Protein Imaging Using Bifunctional Light-Up Aptamers.Angewandte Chemie (International ed. in English) · 2024
    Article
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

9 authors.

Franziska GrünInstitute of Pharmacy and Molecular Biotechnology (IPMB), Heidelberg University, 69120, Heidelberg, Germany.
Niklas van den BerghInstitute of Pharmacy and Molecular Biotechnology (IPMB), Heidelberg University, 69120, Heidelberg, Germany.
Maja KlevanskiDepartment of Functional Neuroanatomy, Heidelberg University, 69120, Heidelberg, Germany.
Mrigank S VermaInstitute of Applied Physics (APH), Karlsruhe Institute of Technology, 76131, Karlsruhe, Germany.
Bastian BühlerDepartment of Chemical Biology, Max Planck Institute for Medical Research, 69120, Heidelberg, Germany.
G Ulrich NienhausInstitute of Applied Physics (APH), Karlsruhe Institute of Technology, 76131, Karlsruhe, Germany.
Thomas KunerDepartment of Functional Neuroanatomy, Heidelberg University, 69120, Heidelberg, Germany.
Andres JäschkeInstitute of Pharmacy and Molecular Biotechnology (IPMB), Heidelberg University, 69120, Heidelberg, Germany.
Murat SunbulInstitute of Pharmacy and Molecular Biotechnology (IPMB), Heidelberg University, 69120, Heidelberg, Germany.ORCID 0000-0001-5284-3884

Funding

Deutsche Forschungsgemeinschaft GRK 2039Deutsche Forschungsgemeinschaft Ja794/11Helmholtz Association
6 · The paper itself

Abstract

Efficient labeling methods for protein visualization with minimal tag size and appropriate photophysical properties are required for single-molecule localization microscopy (SMLM), providing insights into the organization and interactions of biomolecules in cells at the molecular level. Among the fluorescent light-up aptamers (FLAPs) originally developed for RNA imaging, RhoBAST stands out due to its remarkable brightness, photostability, fluorogenicity, and rapid exchange kinetics, enabling super-resolved imaging with high localization precision. Here, we expand the applicability of RhoBAST to protein imaging by fusing it to protein-binding aptamers. The versatility of such bifunctional aptamers is demonstrated by employing a variety of protein-binding aptamers and different FLAPs. Moreover, fusing RhoBAST with the GFP-binding aptamer AP3 facilitates high- and super-resolution imaging of GFP-tagged proteins, which is particularly valuable in view of the widespread availability of plasmids and stable cell lines expressing proteins fused to GFP. The bifunctional aptamers compare favorably with standard antibody-based immunofluorescence protocols, as they are 7-fold smaller than antibody conjugates and exhibit higher bleaching-resistance. We demonstrate the effectiveness of our approach in super-resolution microscopy in secondary mammalian cell lines and primary neurons by RhoBAST-PAINT, an SMLM protein imaging technique that leverages the transient binding of the fluorogenic rhodamine dye SpyRho to RhoBAST.

Indexed as

Aptamers, NucleotideFluorescent DyesGreen Fluorescent ProteinsHumansMicroscopy, FluorescenceProteinsAptamers, NucleotideFluorescent DyesGreen Fluorescent ProteinsProteinsFluorescent light-up aptamerPoint accumulation for imaging in nanoscale topography (PAINT)Protein-binding aptamerProtein imagingSuper-resolution imaging

Identifiers

PMID39115976
PMCPMC11627133

What OpenQuestion holds

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Registered trials

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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.