Evidence map›Paper›PMID 38553587›Full record

ArticleNature chemistry2024

Expanding the molecular language of protein liquid-liquid phase separation.

Shiv Rekhi, Cristobal Garcia Garcia, Mayur Barai, Azamat Rizuan, Benjamin S Schuster, Kristi L Kiick, Jeetain Mittal

Open access · greenAbstract read
In one paragraph

Article in Nature chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 118 papers.

0numbers the graph read from it
0cells of the map it votes in
118citing papers in PubMed
41.9field-weighted citation impact, top 1% 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

118 citing papers in PubMed, 188 citations in OpenAlex.

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  16. 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
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58 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

7 authors at 3 institutions in 1 country.

Shiv Rekhi *Artie McFerrin Department of Chemical Engineering, Texas A&M University, College Station, TX, USA.
Cristobal Garcia Garcia *Department of Materials Science and Engineering, University of Delaware, Newark, DE, USA.
Mayur Barai *Department of Chemical and Biochemical Engineering, Rutgers, the State University of New Jersey, Piscataway, NJ, USA.
Azamat RizuanArtie McFerrin Department of Chemical Engineering, Texas A&M University, College Station, TX, USA.
Benjamin S SchusterDepartment of Chemical and Biochemical Engineering, Rutgers, the State University of New Jersey, Piscataway, NJ, USA. benjamin.schuster@rutgers.edu.ORCID 0000-0002-6468-8081
Kristi L KiickDepartment of Materials Science and Engineering, University of Delaware, Newark, DE, USA. kiick@udel.edu.ORCID 0000-0001-8587-0301
Jeetain MittalArtie McFerrin Department of Chemical Engineering, Texas A&M University, College Station, TX, USA. jeetain@tamu.edu.ORCID 0000-0002-9725-6402
Texas A&M University · USRutgers, The State University of New Jersey · USUniversity of Delaware · US

Funding

Sequence determinants of membraneless organelle rheology -- Research supplement to promote diversityR35GM142903 · NIGMS · RUTGERS, THE STATE UNIV OF N.J. · PI Benjamin S Schuster · 2021 to 2026
$2.6M
Liquid-Liquid Phase Separation in Heterochromatin OrganizationR01GM136917 · NIGMS · TEXAS ENGINEERING EXPERIMENT STATION · PI MITTAL, JEETAIN · 2020 to 2023
$1.4M
Multiscale Computational Models to Investigate the Role of Phase Separation in BiologyR35GM153388 · NIGMS · TEXAS ENGINEERING EXPERIMENT STATION · PI Jeetain Mittal · 2024 to 2026
$1.3M
National Science Foundation (NSF) DMR-2004796NIGMS NIH HHS R01 GM136917NIGMS NIH HHS R35 GM142903NIGMS NIH HHS R35 GM153388U.S. Department of Health & Human Services | NIH | Office of Extramural Research, National Institutes of Health (OER) R01GM136917Welch Foundation A-2113-202203311
6 · The paper itself

Abstract

Understanding the relationship between a polypeptide sequence and its phase separation has important implications for analysing cellular function, treating disease and designing novel biomaterials. Several sequence features have been identified as drivers for protein liquid-liquid phase separation (LLPS), schematized as a 'molecular grammar' for LLPS. Here we further probe how sequence modulates phase separation and the material properties of the resulting condensates, targeting sequence features previously overlooked in the literature. We generate sequence variants of a repeat polypeptide with either no charged residues, high net charge, no glycine residues or devoid of aromatic or arginine residues. All but one of 12 variants exhibited LLPS, albeit to different extents, despite substantial differences in composition. Furthermore, we find that all the condensates formed behaved like viscous fluids, despite large differences in their viscosities. Our results support the model of multiple interactions between diverse residue pairs-not just a handful of residues-working in tandem to drive the phase separation and dynamics of condensates.

Indexed as

PeptidesAmino Acid SequencePhase SeparationPhase TransitionProteinsViscosityPeptidesProteins

Identifiers

PMID38553587
PMCPMC11230844
OpenAlexW4393317567

What OpenQuestion holds

Textmetadata
LicenceTDM
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.