Evidence map›Paper›PMID 30873835›Full record

ArticleThe journal of physical chemistry letters2019

Complete Phase Diagram for Liquid-Liquid Phase Separation of Intrinsically Disordered Proteins.

James McCarty, Kris T Delaney, Scott P O Danielsen, Glenn H Fredrickson, Joan-Emma Shea

Abstract readLetter
In one paragraph

Article in The journal of physical chemistry letters, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 121 papers.

0numbers the graph read from it
0cells of the map it votes in
121citing 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

121 citing papers in PubMed.

  1. Article
  2. Article
  3. Nucleation Kinetics Reveals a Distinct Biological Function Space of Biomolecular Condensates.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  4. Intrinsic Disorder as a Biomimetic Design Paradigm.Biomimetics (Basel, Switzerland) · 2026
    Article
  5. Article
  6. Article
  7. Article
  8. Mapping Charge Interactions in Intrinsically Disordered Proteins.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Driving forces of RNA condensation revealed through coarse-grained modeling with explicit MgProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

61 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

5 authors.

James McCartyDepartment of Chemistry and Biochemistry , University of California , Santa Barbara , California 93106 , United States.ORCID http://orcid.org/0000-0002-3838-6004
Kris T DelaneyMaterials Research Laboratory , University of California , Santa Barbara , California 93106 , United States.ORCID http://orcid.org/0000-0003-0356-1391
Scott P O DanielsenMaterials Research Laboratory , University of California , Santa Barbara , California 93106 , United States.ORCID http://orcid.org/0000-0003-3432-5578
Glenn H FredricksonMaterials Research Laboratory , University of California , Santa Barbara , California 93106 , United States.ORCID http://orcid.org/0000-0002-6716-9017
Joan-Emma SheaDepartment of Chemistry and Biochemistry , University of California , Santa Barbara , California 93106 , United States.ORCID http://orcid.org/0000-0002-9801-9273

Funding

Molecular Basis of the Tau Aggregation PathwayR01AG056058 · NIA · UNIVERSITY OF CALIFORNIA SANTA BARBARA · PI Songi Han, KENNETH Stephen KOSIK · 2017 to 2026
$6.4M
NIA NIH HHS R01 AG056058
6 · The paper itself

Abstract

A number of intrinsically disordered proteins have been shown to self-assemble via liquid-liquid phase separation into protein-rich and dilute phases. The resulting coacervates can have important biological functions, and the ability to form these assemblies is dictated by the protein's primary amino acid sequence as well as by the solution conditions. We present a complete phase diagram for the simple coacervation of a polyampholyte intrinsically disordered protein using a field-theoretic simulation approach. We show that differences in the primary amino acid sequence and in the distribution of charged amino acids along the sequence lead to differences in the phase window for coacervation, with block-charged sequences having a larger coacervation window than sequences with a random patterning of charges. The model also captures how changing solution conditions modifies the phase diagram and can serve to guide experimental studies.

Indexed as

Amino Acid SequenceIntrinsically Disordered ProteinsModels, MolecularPhase TransitionProtein ConformationStatic ElectricityThermodynamicsIntrinsically Disordered Proteins

Identifiers

PMID30873835
PMCPMC7379843

What OpenQuestion holds

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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.