Evidence map›Paper›PMID 37582808›Full record

ArticleNature communications2023

Quantitative real-time in-cell imaging reveals heterogeneous clusters of proteins prior to condensation.

Chenyang Lan, Juhyeong Kim, Svenja Ulferts, Fernando Aprile-Garcia, Sophie Weyrauch, Abhinaya Anandamurugan, Robert Grosse, Ritwick Sawarkar, Aleks Reinhardt, Thorsten Hugel

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
6.5field-weighted citation impact, top 3% of its field
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

24 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Distinguishing near- versus off-critical phase behaviors of intrinsically disordered proteins.Reports on progress in physics. Physical Society (Great Britain) · 2026
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  8. Clustering within a single-component biomolecular condensate.bioRxiv : the preprint server for biology · 2025
    Article
  9. Article
  10. Article
  11. Molecular insights into the interaction between a disordered protein and a folded RNA.Proceedings of the National Academy of Sciences of the United States of America · 2024
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  12. Article
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  16. Review
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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

10 authors at 3 institutions in 2 countries.

Chenyang LanInstitute of Physical Chemistry, University of Freiburg, Freiburg, Germany.
Juhyeong KimInstitute of Physical Chemistry, University of Freiburg, Freiburg, Germany.
Svenja UlfertsInstitute of Experimental and Clinical Pharmacology and Toxicology, University of Freiburg, Freiburg, Germany.ORCID http://orcid.org/0000-0002-6605-8163
Fernando Aprile-GarciaMax Planck Institute of Immunobiology and Epigenetics, Breisgau, Germany.ORCID http://orcid.org/0000-0002-5133-0857
Sophie WeyrauchInstitute of Physical Chemistry, University of Freiburg, Freiburg, Germany.
Abhinaya AnandamuruganInstitute of Physical Chemistry, University of Freiburg, Freiburg, Germany.
Robert GrosseInstitute of Experimental and Clinical Pharmacology and Toxicology, University of Freiburg, Freiburg, Germany.ORCID http://orcid.org/0000-0002-3380-5273
Ritwick SawarkarMedical Research Council (MRC), University of Cambridge, Cambridge, CB2 1QR, United Kingdom.ORCID http://orcid.org/0000-0003-0532-7662
Aleks ReinhardtYusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, United Kingdom. ar732@cam.ac.uk.ORCID http://orcid.org/0000-0002-9393-3429
Thorsten HugelInstitute of Physical Chemistry, University of Freiburg, Freiburg, Germany. th@pc.uni-freiburg.de.ORCID http://orcid.org/0000-0003-3292-4569
University of Freiburg · DEUniversity of Cambridge · GBMax Planck Institute of Immunobiology and Epigenetics · DE

Funding

Medical Research Council MC_UU_00025/8
6 · The paper itself

Abstract

Our current understanding of biomolecular condensate formation is largely based on observing the final near-equilibrium condensate state. Despite expectations from classical nucleation theory, pre-critical protein clusters were recently shown to form under subsaturation conditions in vitro; if similar long-lived clusters comprising more than a few molecules are also present in cells, our understanding of the physical basis of biological phase separation may fundamentally change. Here, we combine fluorescence microscopy with photobleaching analysis to quantify the formation of clusters of NELF proteins in living, stressed cells. We categorise small and large clusters based on their dynamics and their response to p38 kinase inhibition. We find a broad distribution of pre-condensate cluster sizes and show that NELF protein cluster formation can be explained as non-classical nucleation with a surprisingly flat free-energy landscape for a wide range of sizes and an inhibition of condensation in unstressed cells.

Indexed as

CognitionProteinsDiagnostic ImagingProteins

Identifiers

PMID37582808
PMCPMC10427612
OpenAlexW4385836269

What OpenQuestion holds

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LicenceCC BY
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Registered trials

None linked

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.