Evidence map›Paper›PMID 41803331›Full record

ArticleCommunications chemistry2026

ABEL-FRET bridges the timescale gap in single-molecule measurements of the structural dynamics in the A

Ivan Maslov, Valentin Borshchevskiy, Iván Pérez, Vadim Cherezov, Johan Hofkens, Jelle Hendrix, Michael Börsch, Thomas Gensch

Abstract read
In one paragraph

Article in Communications chemistry, 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

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

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

8 authors.

Ivan MaslovDynamic Bioimaging Lab, Advanced Optical Microscopy Centre and Biomedical Research Institute (BIOMED), Hasselt University, Diepenbeek, Belgium.
Valentin BorshchevskiyInstitute of Biological Information Processing 7, IBI-7 (Structural Biochemistry), Forschungszentrum Jülich, Jülich, Germany.
Iván PérezJena University Hospital, Single Molecule Microscopy Group, Jena, Germany.
Vadim CherezovBridge Institute, Department of Chemistry, University of Southern California, Los Angeles, CA, USA.ORCID http://orcid.org/0000-0002-5265-3914
Johan HofkensDepartment of Chemistry, KU Leuven, Leuven, Belgium.ORCID http://orcid.org/0000-0002-9101-0567
Jelle HendrixDynamic Bioimaging Lab, Advanced Optical Microscopy Centre and Biomedical Research Institute (BIOMED), Hasselt University, Diepenbeek, Belgium.ORCID http://orcid.org/0000-0001-5731-1297
Michael BörschJena University Hospital, Single Molecule Microscopy Group, Jena, Germany. michael.boersch@med.uni-jena.de.ORCID http://orcid.org/0000-0002-0634-2963
Thomas GenschInstitute of Biological Information Processing, Molecular and Cellular Physiology (IBI-1), Forschungszentrum Jülich GmbH, Jülich, Germany. t.gensch@fz-juelich.de.ORCID http://orcid.org/0000-0002-3903-4705

Funding

Bijzonder Onderzoeksfonds (Special Research Fund) BOF21BL11Deutsche Forschungsgemeinschaft (German Research Foundation) BO1891/10-2, BO1891/15-1, BO1891/16-1, BO1891/18-2EC | Horizon 2020 Framework Programme (EU Framework Programme for Research and Innovation H2020) MemProDx, 101149735
6 · The paper itself

Abstract

The functional complexity of G protein-coupled receptors (GPCRs) arises from their structural dynamics, spanning timescales from nanoseconds to minutes. Single-molecule Förster Resonance Energy Transfer (smFRET) enables direct observation of these dynamics in individual receptors, either freely diffusing in solution, using confocal microscopy, or immobilized on surfaces, using Total Internal Reflection Fluorescence (TIRF) camera-based microscopy. However, these modalities are limited to distinct timescales - faster than milliseconds or slower than hundreds of milliseconds, respectively. To overcome these limitations, we employed smFRET with Anti-Brownian Electrokinetic (ABEL) trapping to extend the observation time of untethered human A

Identifiers

PMID41803331
PMCPMC12972066

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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.