Evidence map›Paper›PMID 29091028›Full record

ArticleeLife2017

Intrinsically disordered linkers determine the interplay between phase separation and gelation in multivalent proteins.

Tyler S Harmon, Alex S Holehouse, Michael K Rosen, Rohit V Pappu

Abstract read
In one paragraph

Article in eLife, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 392 papers.

0numbers the graph read from it
0cells of the map it votes in
392citing 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

392 citing papers in PubMed.

  1. In Vitro Assay of Bacterial RNA Helicases Liquid-Liquid Phase Separation.Methods in molecular biology (Clifton, N.J.) · 2027
    Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Distinguishing near- versus off-critical phase behaviors of intrinsically disordered proteins.Reports on progress in physics. Physical Society (Great Britain) · 2026
    Article
  17. Article
  18. amyloid-predict and LLPS-predict: Predicting phase separation propensities in the intrinsically disordered proteome.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  19. Article
  20. Article

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

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

4 authors.

Tyler S HarmonCenter for Biological Systems Engineering, Department of Biomedical Engineering, Washington University in St. Louis, St. Louis, United States.
Alex S HolehouseCenter for Biological Systems Engineering, Department of Biomedical Engineering, Washington University in St. Louis, St. Louis, United States.ORCID http://orcid.org/0000-0002-4155-5729
Michael K RosenDepartment of Biophysics, Howard Hughes Medical Institute, UT Southwestern Medical Center, Dallas, United States.ORCID http://orcid.org/0000-0002-0775-7917
Rohit V PappuCenter for Biological Systems Engineering, Department of Biomedical Engineering, Washington University in St. Louis, St. Louis, United States.ORCID http://orcid.org/0000-0003-2568-1378

Funding

STRUCTURAL STUDY OF RHO-GTPASE REGULATORS AND EFFECTORSR01GM056322 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI ROSEN, MICHAEL K · 1997 to 2019
$5.7M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM056322
6 · The paper itself

Abstract

Phase transitions of linear multivalent proteins control the reversible formation of many intracellular membraneless bodies. Specific non-covalent crosslinks involving domains/motifs lead to system-spanning networks referred to as gels. Gelation transitions can occur with or without phase separation. In gelation driven by phase separation multivalent proteins and their ligands condense into dense droplets, and gels form within droplets. System spanning networks can also form without a condensation or demixing of proteins into droplets. Gelation driven by phase separation requires lower protein concentrations, and seems to be the biologically preferred mechanism for forming membraneless bodies. Here, we use coarse-grained computer simulations and the theory of associative polymers to uncover the physical properties of intrinsically disordered linkers that determine the extent to which gelation of linear multivalent proteins is driven by phase separation. Our findings are relevant for understanding how sequence-encoded information in disordered linkers influences phase transitions of multivalent proteins.

Indexed as

Phase TransitionComputer SimulationGelsProtein ConformationProteinsGelsProteinscell biologycomputationcomputational biologygelationintrinsically disordered proteinsmultivalent proteinsnonephase separationphase transitionssystems biology

Identifiers

PMID29091028
PMCPMC5703641

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.