Evidence map›Paper›PMID 35641495›Full record

ArticleNature communications2022

Dynamic arrest and aging of biomolecular condensates are modulated by low-complexity domains, RNA and biochemical activity.

Miriam Linsenmeier, Maria Hondele, Fulvio Grigolato, Eleonora Secchi, Karsten Weis, Paolo Arosio

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 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing 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

66 citing papers in PubMed.

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  6. ACS omega · 2026
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6 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.

Miriam LinsenmeierDepartment of Chemistry and Applied Biosciences, Institute for Chemical and Bioengineering, Swiss Federal Institute of Technology, 8093, Zurich, Switzerland.
Maria HondeleDepartment of Biology, Institute for Biochemistry, Swiss Federal Institute of Technology, 8093, Zurich, Switzerland.ORCID http://orcid.org/0000-0002-2733-2561
Fulvio GrigolatoDepartment of Chemistry and Applied Biosciences, Institute for Chemical and Bioengineering, Swiss Federal Institute of Technology, 8093, Zurich, Switzerland.
Eleonora SecchiDepartment of Civil, Environmental and Geomatic Engineering, Swiss Federal Institute of Technology, 8093, Zurich, Switzerland.ORCID http://orcid.org/0000-0002-0949-9085
Karsten WeisDepartment of Biology, Institute for Biochemistry, Swiss Federal Institute of Technology, 8093, Zurich, Switzerland. karsten.weis@bc.biol.ethz.ch.ORCID http://orcid.org/0000-0001-7224-925X
Paolo ArosioDepartment of Chemistry and Applied Biosciences, Institute for Chemical and Bioengineering, Swiss Federal Institute of Technology, 8093, Zurich, Switzerland. paolo.arosio@chem.ethz.ch.ORCID http://orcid.org/0000-0002-2740-1205

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Biomolecular condensates require suitable control of material properties for their function. Here we apply Differential Dynamic Microscopy (DDM) to probe the material properties of an in vitro model of processing bodies consisting of out-of-equilibrium condensates formed by the DEAD-box ATPase Dhh1 in the presence of ATP and RNA. By applying this single-droplet technique we show that condensates within the same population exhibit a distribution of material properties, which are regulated on several levels. Removal of the low-complexity domains (LCDs) of the protein decreases the fluidity of the condensates. Structured RNA leads to a larger fraction of dynamically arrested condensates with respect to unstructured polyuridylic acid (polyU). Promotion of the enzymatic ATPase activity of Dhh1 reduces aging of the condensates and the formation of arrested structures, indicating that biochemical activity and material turnover can maintain fluid-like properties over time.

Indexed as

Biomolecular CondensatesRNAAdenosine TriphosphatasesDEAD-box RNA HelicasesAdenosine TriphosphatasesDEAD-box RNA HelicasesRNA

Identifiers

PMID35641495
PMCPMC9156751

What OpenQuestion holds

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Registered trials

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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.