Evidence map›Paper›PMID 33208940›Full record

ArticleNature2020

Structural basis for the final steps of human 40S ribosome maturation.

Michael Ameismeier, Ivo Zemp, Jasmin van den Heuvel, Matthias Thoms, Otto Berninghausen, Ulrike Kutay, Roland Beckmann

Abstract read
PubMed Publisher
In one paragraph

Article in Nature, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
4.6field-weighted citation impact, top 4% 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

61 citing papers in PubMed, 82 citations in OpenAlex.

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  12. The function of Mak16 in ribosome biogenesis depends on its [4Fe-4S] cluster.Proceedings of the National Academy of Sciences of the United States of America · 2025
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1 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 2 institutions in 2 countries.

Michael AmeismeierGene Center Munich, Department of Biochemistry, University of Munich, Munich, Germany.ORCID http://orcid.org/0000-0002-1194-3448
Ivo ZempInstitute of Biochemistry, Department of Biology, ETH Zurich, Zurich, Switzerland.
Jasmin van den HeuvelInstitute of Biochemistry, Department of Biology, ETH Zurich, Zurich, Switzerland.
Matthias ThomsGene Center Munich, Department of Biochemistry, University of Munich, Munich, Germany.
Otto BerninghausenGene Center Munich, Department of Biochemistry, University of Munich, Munich, Germany.ORCID http://orcid.org/0000-0002-9255-0522
Ulrike KutayInstitute of Biochemistry, Department of Biology, ETH Zurich, Zurich, Switzerland.
Roland BeckmannGene Center Munich, Department of Biochemistry, University of Munich, Munich, Germany. beckmann@genzentrum.lmu.de.ORCID http://orcid.org/0000-0003-4291-3898
ETH Zurich · CHLMU Klinikum · DE

Funding

European Research Council
6 · The paper itself

Abstract

Eukaryotic ribosomes consist of a small 40S and a large 60S subunit that are assembled in a highly coordinated manner. More than 200 factors ensure correct modification, processing and folding of ribosomal RNA and the timely incorporation of ribosomal proteins

Indexed as

Cryoelectron MicroscopyEnzyme ActivationHeLa CellsHumansModels, MolecularNuclear ProteinsProtein ConformationProteinsProtein Serine-Threonine KinasesRibosome Subunits, Small, EukaryoticRNA-Binding ProteinsSaccharomyces cerevisiaeEIF1AD protein, humanNOB1 protein, humanNuclear ProteinsPNO1 protein, humanProteinsProtein Serine-Threonine KinasesRIOK1 protein, humanRIOK2 protein, humanRNA-Binding Proteins

Identifiers

PMID33208940
OpenAlexW3102836593

What OpenQuestion holds

Textmetadata
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.