Evidence map›Paper›PMID 26147918›Full record

ArticleNature methods2015

Single-molecule spectroscopy of protein conformational dynamics in live eukaryotic cells.

Iwo König, Arash Zarrine-Afsar, Mikayel Aznauryan, Andrea Soranno, Bengt Wunderlich, Fabian Dingfelder, Jakob C Stüber, Andreas Plückthun, Daniel Nettels, Benjamin Schuler

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Article in Nature methods, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 121 papers.

0numbers the graph read from it
0cells of the map it votes in
121citing 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

121 citing papers in PubMed.

  1. Article
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  7. Single-molecule reaction-diffusion.Biophysical journal · 2025
    Article
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  18. Structural biases in disordered proteins are prevalent in the cell.Nature structural & molecular biology · 2024
    Article
  19. Article
  20. Review

61 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors.

Iwo KönigDepartment of Biochemistry, University of Zurich, Zurich, Switzerland.
Arash Zarrine-AfsarDepartment of Biochemistry, University of Zurich, Zurich, Switzerland.
Mikayel AznauryanDepartment of Biochemistry, University of Zurich, Zurich, Switzerland.
Andrea SorannoDepartment of Biochemistry, University of Zurich, Zurich, Switzerland.
Bengt WunderlichDepartment of Biochemistry, University of Zurich, Zurich, Switzerland.
Fabian DingfelderDepartment of Biochemistry, University of Zurich, Zurich, Switzerland.
Jakob C StüberDepartment of Biochemistry, University of Zurich, Zurich, Switzerland.
Andreas PlückthunDepartment of Biochemistry, University of Zurich, Zurich, Switzerland.
Daniel NettelsDepartment of Biochemistry, University of Zurich, Zurich, Switzerland.
Benjamin SchulerDepartment of Biochemistry, University of Zurich, Zurich, Switzerland.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Single-molecule methods have become widely used for quantifying the conformational heterogeneity and structural dynamics of biomolecules in vitro. Their application in vivo, however, has remained challenging owing to shortcomings in the design and reproducible delivery of labeled molecules, the range of applicable analysis methods, and suboptimal cell culture conditions. By addressing these limitations in an integrated approach, we demonstrate the feasibility of probing protein dynamics from milliseconds down to the nanosecond regime in live eukaryotic cells with confocal single-molecule Förster resonance energy transfer (FRET) spectroscopy. We illustrate the versatility of the approach by determining the dimensions and submicrosecond chain dynamics of an intrinsically disordered protein; by detecting even subtle changes in the temperature dependence of protein stability, including in-cell cold denaturation; and by quantifying the folding dynamics of a small protein. The methodology opens possibilities for assessing the effect of the cellular environment on biomolecular conformation, dynamics and function.

Indexed as

Protein ConformationAnimalsCell NucleusCluster AnalysisCross-Linking ReagentsDNA Mutational AnalysisGenomicsGuanosineHEK293 CellsHumansLiverMiceMutagenesisMutationReverse TranscriptionRNA, Messenger7-methylguanosineCross-Linking ReagentsGuanosineRNA, MessengerRNA, Small Nucleolar

Identifiers

PMID26147918

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.