Evidence map›Paper›PMID 37460154›Full record

ArticleRNA (New York, N.Y.)2023

Phase-separated ribosome-nascent chain complexes in genotoxic stress response.

Orsolya Németh-Szatmári, Bence Nagy-Mikó, Ádám Györkei, Dániel Varga, Bálint Barna H Kovács, Nóra Igaz, Bence Bognár, Zsolt Rázga, Gábor Nagy, Nóra Zsindely and 8 more

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in RNA (New York, N.Y.), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.6field-weighted citation impact, top 30% 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

4 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Role of Assemblysomes in Cellular Stress Responses.Wiley interdisciplinary reviews. RNA
    Review
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

18 authors at 4 institutions in 3 countries.

Orsolya Németh-SzatmáriDepartment of Biochemistry and Molecular Biology, University of Szeged, 6726 Szeged, Hungary.
Bence Nagy-MikóDepartment of Biochemistry and Molecular Biology, University of Szeged, 6726 Szeged, Hungary.
Ádám GyörkeiInstitute of Biochemistry, Biological Research Centre, 6726 Szeged, Hungary.
Dániel VargaDepartment of Optics and Quantum Electronics, University of Szeged, 6720 Szeged, Hungary.
Bálint Barna H KovácsDepartment of Optics and Quantum Electronics, University of Szeged, 6720 Szeged, Hungary.
Nóra IgazDepartment of Biochemistry and Molecular Biology, University of Szeged, 6726 Szeged, Hungary.
Bence BognárDepartment of Biochemistry and Molecular Biology, University of Szeged, 6726 Szeged, Hungary.
Zsolt RázgaDepartment of Pathology, Faculty of Medicine, University of Szeged, 6720 Szeged, Hungary.
Gábor NagyDepartment of Biochemistry and Molecular Biology, University of Szeged, 6726 Szeged, Hungary.
Nóra ZsindelyDepartment of Biochemistry and Molecular Biology, University of Szeged, 6726 Szeged, Hungary.
László BodaiDepartment of Biochemistry and Molecular Biology, University of Szeged, 6726 Szeged, Hungary.
Balázs PappInstitute of Biochemistry, Biological Research Centre, 6726 Szeged, Hungary.
Miklós ErdélyiDepartment of Optics and Quantum Electronics, University of Szeged, 6720 Szeged, Hungary.
Mónika KiricsiDepartment of Biochemistry and Molecular Biology, University of Szeged, 6726 Szeged, Hungary.
András BlastyákInstitute of Genetics, Biological Research Centre, 6726 Szeged, Hungary.
Martine A CollartDepartment of Microbiology and Molecular Medicine, Institute of Genetics and Genomics Geneva, Faculty of Medicine, University of Geneva, 1211 Geneva 4, Switzerland.
Imre M BorosDepartment of Biochemistry and Molecular Biology, University of Szeged, 6726 Szeged, Hungary.
Zoltán VillányiDepartment of Biochemistry and Molecular Biology, University of Szeged, 6726 Szeged, Hungary villanyi.zoltan@bio.u-szeged.hu.
University of Szeged · HUHUN-REN Szegedi Biológiai Kutatóközpont · HUUniversity of Geneva · CHUniversity of Oslo · NO

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Assemblysomes are EDTA- and RNase-resistant ribonucleoprotein (RNP) complexes of paused ribosomes with protruding nascent polypeptide chains. They have been described in yeast and human cells for the proteasome subunit Rpt1, and the disordered amino-terminal part of the nascent chain was found to be indispensable for the accumulation of the Rpt1-RNP into assemblysomes. Motivated by this, to find other assemblysome-associated RNPs we used bioinformatics to rank subunits of

Indexed as

Saccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsDNA DamageEdetic AcidHumansRecQ HelicasesRibonucleoproteinsRibosomesRNAEdetic AcidRecQ HelicasesRibonucleoproteinsRNASaccharomyces cerevisiae ProteinsSGS1 protein, S cerevisiaeassemblysomesBLMDNA damage responsephase separationSgs1

Identifiers

PMID37460154
PMCPMC10578487
OpenAlexW4384500207

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.