Evidence map›Paper›PMID 38383656›Full record

ArticleNature chemistry2024

Asymmetric oligomerization state and sequence patterning can tune multiphase condensate miscibility.

Ushnish Rana, Ke Xu, Amal Narayanan, Mackenzie T Walls, Athanassios Z Panagiotopoulos, José L Avalos, Clifford P Brangwynne

Abstract read
In one paragraph

Article in Nature chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing 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

52 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Combinatorial decision-making driven by multicomponent surface condensates.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  7. Review
  8. Article
  9. Article
  10. Condensates as Conformation Editors of Disordered Client Proteins.Journal of the American Chemical Society · 2026
    Article
  11. Review
  12. Review
  13. A molecular grammar for programmable multiphase protein-RNA vesicles.bioRxiv : the preprint server for biology · 2026
    Article
  14. Diverse, distinct, and densely packed DNA nanostar droplets.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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.

Ushnish Rana *Department of Chemical and Biological Engineering, Princeton University, Princeton, NJ, USA.ORCID 0000-0001-6783-6193
Ke Xu *Department of Chemical and Biological Engineering, Princeton University, Princeton, NJ, USA.
Amal NarayananDepartment of Chemical and Biological Engineering, Princeton University, Princeton, NJ, USA.ORCID 0000-0001-8159-6878
Mackenzie T WallsDepartment of Chemical and Biological Engineering, Princeton University, Princeton, NJ, USA.ORCID 0000-0002-1857-987X
Athanassios Z PanagiotopoulosDepartment of Chemical and Biological Engineering, Princeton University, Princeton, NJ, USA.
José L AvalosDepartment of Chemical and Biological Engineering, Princeton University, Princeton, NJ, USA. javalos@princeton.edu.ORCID 0000-0002-7209-4208
Clifford P BrangwynneDepartment of Chemical and Biological Engineering, Princeton University, Princeton, NJ, USA. cbrangwy@princeton.edu.ORCID 0000-0002-1350-9960

Funding

National Science Foundation (NSF) DGE-1656466National Science Foundation (NSF) DMR-1420541United States Department of Defense | United States Air Force | AFMC | Air Force Office of Scientific Research (AF Office of Scientific Research) FA9550-20-1-0241
6 · The paper itself

Abstract

Endogenous biomolecular condensates, composed of a multitude of proteins and RNAs, can organize into multiphasic structures with compositionally distinct phases. This multiphasic organization is generally understood to be critical for facilitating their proper biological function. However, the biophysical principles driving multiphase formation are not completely understood. Here we use in vivo condensate reconstitution experiments and coarse-grained molecular simulations to investigate how oligomerization and sequence interactions modulate multiphase organization in biomolecular condensates. We demonstrate that increasing the oligomerization state of an intrinsically disordered protein results in enhanced immiscibility and multiphase formation. Interestingly, we find that oligomerization tunes the miscibility of intrinsically disordered proteins in an asymmetric manner, with the effect being more pronounced when the intrinsically disordered protein, exhibiting stronger homotypic interactions, is oligomerized. Our findings suggest that oligomerization is a flexible biophysical mechanism that cells can exploit to tune the internal organization of biomolecular condensates and their associated biological functions.

Indexed as

Biomolecular CondensatesIntrinsically Disordered ProteinsMolecular Dynamics SimulationProtein MultimerizationRNAIntrinsically Disordered ProteinsRNA

Identifiers

PMID38383656
PMCPMC11230906

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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.