Evidence map›Paper›PMID 36513655›Full record

ArticleNature communications2022

Condensates formed by prion-like low-complexity domains have small-world network structures and interfaces defined by expanded conformations.

Mina Farag, Samuel R Cohen, Wade M Borcherds, Anne Bremer, Tanja Mittag, Rohit V Pappu

Abstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 139 papers.

0numbers the graph read from it
0cells of the map it votes in
139citing 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

139 citing papers in PubMed.

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  13. Fusion protein condensate formation via coiled-coil domains.Protein science : a publication of the Protein Society · 2026
    Article
  14. Distinguishing near- versus off-critical phase behaviors of intrinsically disordered proteins.Reports on progress in physics. Physical Society (Great Britain) · 2026
    Article
  15. Article
  16. Condensates as Conformation Editors of Disordered Client Proteins.Journal of the American Chemical Society · 2026
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79 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

6 authors.

Mina FaragDepartment of Biomedical Engineering and Center for Biomolecular Condensates, Washington University in St. Louis, St. Louis, MO, USA.ORCID http://orcid.org/0000-0002-6457-6848
Samuel R CohenDepartment of Biomedical Engineering and Center for Biomolecular Condensates, Washington University in St. Louis, St. Louis, MO, USA.
Wade M BorcherdsDepartment of Structural Biology, St. Jude Children's Research Hospital, Memphis, TN, USA.ORCID http://orcid.org/0000-0003-3459-4014
Anne BremerDepartment of Structural Biology, St. Jude Children's Research Hospital, Memphis, TN, USA.
Tanja MittagDepartment of Structural Biology, St. Jude Children's Research Hospital, Memphis, TN, USA.ORCID http://orcid.org/0000-0002-1827-3811
Rohit V PappuDepartment of Biomedical Engineering and Center for Biomolecular Condensates, Washington University in St. Louis, St. Louis, MO, USA. pappu@wustl.edu.ORCID http://orcid.org/0000-0003-2568-1378

Funding

ROLE OF CHAIN LENGTH AND SEQUENCE CONTEXTS ON POLYGLUTAMINE OLIGOMERIZATIONR01NS056114 · NINDS · WASHINGTON UNIVERSITY · PI PAPPU, ROHIT V · 2007 to 2020
$4.4M
Understanding the Sequence and Structural Determinants of Phase Behavior of ALS-Causing ProteinsR01NS121114 · NINDS · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI Tanja Mittag, ROHIT V PAPPU · 2021 to 2026
$3.8M
NINDS NIH HHS R01 NS056114NINDS NIH HHS R01 NS121114
6 · The paper itself

Abstract

Biomolecular condensates form via coupled associative and segregative phase transitions of multivalent associative macromolecules. Phase separation coupled to percolation is one example of such transitions. Here, we characterize molecular and mesoscale structural descriptions of condensates formed by intrinsically disordered prion-like low complexity domains (PLCDs). These systems conform to sticker-and-spacers architectures. Stickers are cohesive motifs that drive associative interactions through reversible crosslinking and spacers affect the cooperativity of crosslinking and overall macromolecular solubility. Our computations reproduce experimentally measured sequence-specific phase behaviors of PLCDs. Within simulated condensates, networks of reversible inter-sticker crosslinks organize PLCDs into small-world topologies. The overall dimensions of PLCDs vary with spatial location, being most expanded at and preferring to be oriented perpendicular to the interface. Our results demonstrate that even simple condensates with one type of macromolecule feature inhomogeneous spatial organizations of molecules and interfacial features that likely prime them for biochemical activity.

Indexed as

PrionsMacromolecular SubstancesMolecular ConformationPhase TransitionMacromolecular SubstancesPrions

Identifiers

PMID36513655
PMCPMC9748015

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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.