Evidence map›Paper›PMID 37079924›Full record

ArticleThe journal of physical chemistry. B2023

Role of Strong Localized vs Weak Distributed Interactions in Disordered Protein Phase Separation.

Shiv Rekhi, Dinesh Sundaravadivelu Devarajan, Michael P Howard, Young C Kim, Arash Nikoubashman, Jeetain Mittal

Open access · hybridAbstract read
In one paragraph

Article in The journal of physical chemistry. B, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
7.7field-weighted citation impact, top 2% 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

31 citing papers in PubMed, 50 citations in OpenAlex.

  1. Sticky interactions govern sequence-dependent dynamics in biomolecular condensates.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
  3. Article
  4. Molecular basis of EWS interdomain self-association and its role in condensate formation.Protein science : a publication of the Protein Society · 2025
    Article
  5. Article
  6. Article
  7. Amino acid transfer free energies reveal thermodynamic driving forces in biomolecular condensate formation.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Article
  9. Article
  10. Article
  11. Destabilizing Interactions in Human Telomeric G-Quadruplex Multimers.The journal of physical chemistry letters · 2025
    Article
  12. Article
  13. Article
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  15. Article
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  17. Review
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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

6 authors at 4 institutions in 2 countries.

Shiv RekhiArtie McFerrin Department of Chemical Engineering, Texas A&M University, College Station, Texas 77843, United States.
Dinesh Sundaravadivelu DevarajanArtie McFerrin Department of Chemical Engineering, Texas A&M University, College Station, Texas 77843, United States.ORCID 0000-0001-7825-0999
Michael P HowardDepartment of Chemical Engineering, Auburn University, Auburn, Alabama 36849, United States.ORCID 0000-0002-9561-4165
Young C KimCenter for Materials Physics and Technology, Naval Research Laboratory, Washington, D.C. 20375, United States.
Arash NikoubashmanInstitute of Physics, Johannes Gutenberg University Mainz, Staudingerweg 7, 55128 Mainz, Germany.ORCID 0000-0003-0563-825X
Jeetain MittalArtie McFerrin Department of Chemical Engineering, Texas A&M University, College Station, Texas 77843, United States.ORCID 0000-0002-9725-6402
Texas A&M University · USAuburn University · USJohannes Gutenberg University Mainz · DEUnited States Naval Research Laboratory · US

Funding

Liquid-Liquid Phase Separation in Heterochromatin OrganizationR01GM136917 · NIGMS · TEXAS ENGINEERING EXPERIMENT STATION · PI MITTAL, JEETAIN · 2020 to 2023
$1.4M
NIGMS NIH HHS R01 GM136917
6 · The paper itself

Abstract

Interaction strength and localization are critical parameters controlling the single-chain and condensed-state properties of intrinsically disordered proteins (IDPs). Here, we decipher these relationships using coarse-grained heteropolymers comprised of hydrophobic (H) and polar (P) monomers as model IDPs. We systematically vary the fraction of P monomers

Indexed as

Biochemical PhenomenaIntrinsically Disordered ProteinsHydrophobic and Hydrophilic InteractionsMolecular ConformationPolymersIntrinsically Disordered ProteinsPolymers

Identifiers

PMID37079924
PMCPMC10187732
OpenAlexW4366495670

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.