Evidence map›Paper›PMID 30791483›Full record

ArticleBiomolecules2019

Molecular Crowding Tunes Material States of Ribonucleoprotein Condensates.

Taranpreet Kaur, Ibraheem Alshareedah, Wei Wang, Jason Ngo, Mahdi Muhammad Moosa, Priya R Banerjee

Open access · goldAbstract read
In one paragraph

Article in Biomolecules, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.

0numbers the graph read from it
0cells of the map it votes in
78citing papers in PubMed
6.8field-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

78 citing papers in PubMed, 151 citations in OpenAlex.

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  13. A coarse-grained model for disordered proteins under crowded conditions.Protein science : a publication of the Protein Society · 2025
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18 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 at 2 institutions in 1 country.

Taranpreet KaurDepartment of Physics, University at Buffalo, SUNY, NY 14260, USA. tkaur2@buffalo.edu.
Ibraheem AlshareedahDepartment of Physics, University at Buffalo, SUNY, NY 14260, USA. ialshare@buffalo.edu.
Wei WangDepartment of Physics, University at Buffalo, SUNY, NY 14260, USA. wwang23@buffalo.edu.
Jason NgoDepartment of Physics, University at Buffalo, SUNY, NY 14260, USA. jasonngo@buffalo.edu.
Mahdi Muhammad MoosaDepartment of Pharmacology and Chemical Biology, Baylor College of Medicine, Houston, TX 77030, USA. mahdi.moosa@gmail.com.
Priya R BanerjeeDepartment of Physics, University at Buffalo, SUNY, NY 14260, USA. prbanerj@buffalo.edu.
University at Buffalo, State University of New York · USBaylor College of Medicine · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ribonucleoprotein (RNP) granules are membraneless liquid condensates that dynamically form,dissolve, and mature into a gel-like state in response to a changing cellular environment. RNP condensation islargely governed by promiscuous attractive inter-chain interactions mediated by low-complexity domains(LCDs). Using an archetypal disordered RNP, fused in sarcoma (FUS), here we study how molecular crowdingimpacts the RNP liquid condensation. We observe that the liquid⁻liquid coexistence boundary of FUS islowered by polymer crowders, consistent with an excluded volume model. With increasing bulk crowderconcentration, the RNP partition increases and the diffusion rate decreases in the condensed phase.Furthermore, we show that RNP condensates undergo substantial hardening wherein protein-dense dropletstransition from viscous fluid to viscoelastic gel-like states in a crowder concentration-dependent manner.Utilizing two distinct LCDs that broadly represent commonly occurring sequence motifs driving RNP phasetransitions, we reveal that the impact of crowding is largely independent of LCD charge and sequence patterns.These results are consistent with a thermodynamic model of crowder-mediated depletion interaction, whichsuggests that inter-RNP attraction is enhanced by molecular crowding. The depletion force is likely to play akey role in tuning the physical properties of RNP condensates within the crowded cellular space.

Indexed as

HumansMacromolecular SubstancesParticle SizeRibonucleoproteinsSarcomaSurface PropertiesThermodynamicsMacromolecular SubstancesRibonucleoproteinsdepletion interactionentropic forceintrinsically disordered proteinsliquid–liquid phase separationlow-complexity sequencesmembraneless organellesoptical tweezerprotein diffusion

Identifiers

PMID30791483
PMCPMC6406554
OpenAlexW2907972520

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.