Evidence map›Paper›PMID 35238639›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2022

Co-condensation of proteins with single- and double-stranded DNA.

Roman Renger, Jose A Morin, Regis Lemaitre, Martine Ruer-Gruss, Frank Jülicher, Andreas Hermann, Stephan W Grill

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
5.5field-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

39 citing papers in PubMed, 71 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Learning nature's assembly language with polymers.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  5. Measuring bridging forces in protein-DNA condensates.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Bridging DNA contacts allow Dps frombioRxiv : the preprint server for biology · 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

7 authors at 3 institutions in 1 country.

Roman RengerMax Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany.ORCID 0000-0001-9109-3000
Jose A MorinMax Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany.ORCID 0000-0002-0956-6508
Regis LemaitreMax Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany.ORCID 0000-0002-4881-7541
Martine Ruer-GrussMax Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany.ORCID 0000-0003-0984-4130
Frank JülicherMax Planck Institute for the Physics of Complex Systems, 01187 Dresden, Germany.ORCID 0000-0003-4731-9185
Andreas HermannDeutsches Zentrum für Neurodegenerative Erkrankungen (DZNE), 01307 Dresden, Germany.ORCID 0000-0002-7364-7791
Stephan W GrillMax Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany.ORCID 0000-0002-2290-5826
Max Planck Institute of Molecular Cell Biology and Genetics · DEGerman Center for Neurodegenerative Diseases · DEMax Planck Institute for the Physics of Complex Systems · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SignificanceBiomolecular condensates are intracellular organelles that are not bounded by membranes and often show liquid-like, dynamic material properties. They typically contain various types of proteins and nucleic acids. How the interaction of proteins and nucleic acids finally results in dynamic condensates is not fully understood. Here we use optical tweezers and fluorescence microscopy to study how the prototypical prion-like protein Fused-in-Sarcoma (FUS) condenses with individual molecules of single- and double-stranded DNA. We find that FUS adsorbs on DNA in a monolayer and hence generates an effectively sticky FUS-DNA polymer that collapses and finally forms a dynamic, reversible FUS-DNA co-condensate. We speculate that protein monolayer-based protein-nucleic acid co-condensation is a general mechanism for forming intracellular membraneless organelles.

Indexed as

DNADNA, Single-StrandedHumansMicroscopy, FluorescenceRNA-Binding Protein FUSDNADNA, Single-StrandedFUS protein, humanRNA-Binding Protein FUSbiomolecular condensatesco-condensationDNAFUSoptical tweezers

Identifiers

PMID35238639
PMCPMC8915884
OpenAlexW4220748037

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

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.