Evidence map›Paper›PMID 38042897›Full record

ArticleNature communications2023

Programmable de novo designed coiled coil-mediated phase separation in mammalian cells.

Maruša Ramšak, Dominique A Ramirez, Loren E Hough, Michael R Shirts, Sara Vidmar, Kristina Eleršič Filipič, Gregor Anderluh, Roman Jerala

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 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
5.8field-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

26 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Reversible Nucleolar Complex Coacervation by Short Cationic Peptides.Journal of the American Chemical Society · 2026
    Article
  5. Article
  6. Fusion protein condensate formation via coiled-coil domains.Protein science : a publication of the Protein Society · 2026
    Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Phosphorylation enables allosteric control of a viral condensate.bioRxiv : the preprint server for biology · 2025
    Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. A tunable affinity fusion tag for protein self-assembly.bioRxiv : the preprint server for biology · 2025
    Article
  20. Review
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 at 3 institutions in 2 countries.

Maruša RamšakDepartment of Synthetic Biology and Immunology, National Institute of Chemistry, Ljubljana, Slovenia.
Dominique A RamirezDepartment of Biochemistry, University of Colorado Boulder, Boulder, CO, USA.
Loren E HoughDepartment of Physics and BioFrontiers Institute, University of Colorado Boulder, Boulder, CO, USA.
Michael R ShirtsDepartment of Chemical and Biological Engineering, University of Colorado Boulder, Boulder, CO, USA.
Sara VidmarDepartment of Synthetic Biology and Immunology, National Institute of Chemistry, Ljubljana, Slovenia.
Kristina Eleršič FilipičDepartment of Molecular Biology and Nanobiotechnology, National Institute of Chemistry, Ljubljana, Slovenia.ORCID 0000-0002-0868-2603
Gregor AnderluhDepartment of Molecular Biology and Nanobiotechnology, National Institute of Chemistry, Ljubljana, Slovenia.ORCID 0000-0002-9916-8465
Roman JeralaDepartment of Synthetic Biology and Immunology, National Institute of Chemistry, Ljubljana, Slovenia. roman.jerala@ki.si.ORCID 0000-0002-6337-5251
National Institute of Chemistry · SIUniversity of Colorado Boulder · USUniversity of Ljubljana · SI

Funding

Predoctoral Training Molecular BiophysicsT32GM065103 · NIGMS · UNIVERSITY OF COLORADO AT BOULDER · PI FALKE, JOSEPH J · 2002 to 2021
$4.3M
Interdisciplinary Predoctoral Training in Molecular BiophysicsT32GM145437 · NIGMS · UNIVERSITY OF COLORADO · PI JOSEPH J FALKE · 2022 to 2026
$2.5M
NIGMS NIH HHS T32 GM065103NIGMS NIH HHS T32 GM145437
6 · The paper itself

Abstract

Membraneless liquid compartments based on phase-separating biopolymers have been observed in diverse cell types and attributed to weak multivalent interactions predominantly based on intrinsically disordered domains. The design of liquid-liquid phase separated (LLPS) condensates based on de novo designed tunable modules that interact in a well-understood, controllable manner could improve our understanding of this phenomenon and enable the introduction of new features. Here we report the construction of CC-LLPS in mammalian cells, based on designed coiled-coil (CC) dimer-forming modules, where the stability of CC pairs, their number, linkers, and sequential arrangement govern the transition between diffuse, liquid and immobile condensates and are corroborated by coarse-grained molecular simulations. Through modular design, we achieve multiple coexisting condensates, chemical regulation of LLPS, condensate fusion, formation from either one or two polypeptide components or LLPS regulation by a third polypeptide chain. These findings provide further insights into the principles underlying LLPS formation and a design platform for controlling biological processes.

Indexed as

Intrinsically Disordered ProteinsPeptidesAnimalsMammalsIntrinsically Disordered ProteinsPeptides

Identifiers

PMID38042897
PMCPMC10693550
OpenAlexW4389267201

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.