Evidence map›Paper›PMID 36972455›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2023

Quantitative reconstitution of yeast RNA processing bodies.

Simon L Currie, Wenmin Xing, Denise Muhlrad, Carolyn J Decker, Roy Parker, Michael K Rosen

Open access · hybridAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
7.4field-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

34 citing papers in PubMed, 50 citations in OpenAlex.

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  15. Quantitative spatial analysis of chromatin biomolecular condensates using cryoelectron tomography.Proceedings of the National Academy of Sciences of the United States of America · 2025
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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 2 institutions in 1 country.

Simon L CurrieHHMI, UT Southwestern Medical Center, Dallas TX 75390.ORCID 0000-0001-5083-1484
Wenmin XingHHMI, UT Southwestern Medical Center, Dallas TX 75390.ORCID 0000-0001-6445-0615
Denise MuhlradHHMI, University of Colorado, Boulder, CO 80309.
Carolyn J DeckerHHMI, University of Colorado, Boulder, CO 80309.ORCID 0000-0002-2672-8919
Roy ParkerHHMI, University of Colorado, Boulder, CO 80309.ORCID 0000-0002-8412-4152
Michael K RosenHHMI, UT Southwestern Medical Center, Dallas TX 75390.ORCID 0000-0002-0775-7917
Southwestern Medical Center · USUniversity of Colorado Boulder · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Many biomolecular condensates appear to form through liquid-liquid phase separation (LLPS). Individual condensate components can often undergo LLPS in vitro, capturing some features of the native structures. However, natural condensates contain dozens of components with different concentrations, dynamics, and contributions to compartment formation. Most biochemical reconstitutions of condensates have not benefited from quantitative knowledge of these cellular features nor attempted to capture natural complexity. Here, we build on prior quantitative cellular studies to reconstitute yeast RNA processing bodies (P bodies) from purified components. Individually, five of the seven highly concentrated P-body proteins form homotypic condensates at cellular protein and salt concentrations, using both structured domains and intrinsically disordered regions. Combining the seven proteins together at their cellular concentrations with RNA yields phase-separated droplets with partition coefficients and dynamics of most proteins in reasonable agreement with cellular values. RNA delays the maturation of proteins within and promotes the reversibility of, P bodies. Our ability to quantitatively recapitulate the composition and dynamics of a condensate from its most concentrated components suggests that simple interactions between these components carry much of the information that defines the physical properties of the cellular structure.

Indexed as

Processing BodiesSaccharomyces cerevisiaeRNARNAbiomolecular condensatesP bodiesphase separationproteinRNA

Identifiers

PMID36972455
PMCPMC10083542
OpenAlexW4360992824

What OpenQuestion holds

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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.