Evidence map›Paper›PMID 33384371›Full record

ArticleScience (New York, N.Y.)2021

Interactions between nascent proteins translated by adjacent ribosomes drive homomer assembly.

Matilde Bertolini, Kai Fenzl, Ilia Kats, Florian Wruck, Frank Tippmann, Jaro Schmitt, Josef Johannes Auburger, Sander Tans, Bernd Bukau, Günter Kramer

Abstract read
In one paragraph

Article in Science (New York, N.Y.), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.

0numbers the graph read from it
0cells of the map it votes in
77citing 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

77 citing papers in PubMed.

  1. Article
  2. Human SRP Subunits Coordinate Protein Targeting and mRNA Quality Control.bioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Review
  9. Structures of protein folding intermediates on the ribosome.Nature structural & molecular biology · 2026
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Calmodulin assists during co-translational folding of the KProtein science : a publication of the Protein Society · 2026
    Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article

17 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

10 authors.

Matilde Bertolini *Center for Molecular Biology of Heidelberg University (ZMBH) and German Cancer Research Center (DKFZ), DKFZ-ZMBH Alliance, Im Neuenheimer Feld 282, Heidelberg D-69120, Germany.ORCID https://orcid.org/0000-0002-7019-167X
Kai Fenzl *Center for Molecular Biology of Heidelberg University (ZMBH) and German Cancer Research Center (DKFZ), DKFZ-ZMBH Alliance, Im Neuenheimer Feld 282, Heidelberg D-69120, Germany.ORCID https://orcid.org/0000-0001-8097-7740
Ilia KatsCenter for Molecular Biology of Heidelberg University (ZMBH) and German Cancer Research Center (DKFZ), DKFZ-ZMBH Alliance, Im Neuenheimer Feld 282, Heidelberg D-69120, Germany.ORCID https://orcid.org/0000-0001-5220-5671
Florian WruckAMOLF, Science Park 104, 1098 XG Amsterdam, Netherlands.
Frank TippmannCenter for Molecular Biology of Heidelberg University (ZMBH) and German Cancer Research Center (DKFZ), DKFZ-ZMBH Alliance, Im Neuenheimer Feld 282, Heidelberg D-69120, Germany.ORCID https://orcid.org/0000-0003-3401-8375
Jaro SchmittCenter for Molecular Biology of Heidelberg University (ZMBH) and German Cancer Research Center (DKFZ), DKFZ-ZMBH Alliance, Im Neuenheimer Feld 282, Heidelberg D-69120, Germany.ORCID https://orcid.org/0000-0001-6701-7112
Josef Johannes AuburgerCenter for Molecular Biology of Heidelberg University (ZMBH) and German Cancer Research Center (DKFZ), DKFZ-ZMBH Alliance, Im Neuenheimer Feld 282, Heidelberg D-69120, Germany.
Sander TansAMOLF, Science Park 104, 1098 XG Amsterdam, Netherlands.ORCID https://orcid.org/0000-0002-7131-2568
Bernd BukauCenter for Molecular Biology of Heidelberg University (ZMBH) and German Cancer Research Center (DKFZ), DKFZ-ZMBH Alliance, Im Neuenheimer Feld 282, Heidelberg D-69120, Germany. g.kramer@zmbh.uni-heidelberg.de bukau@zmbh.uni-heidelberg.de.ORCID https://orcid.org/0000-0003-0521-7199
Günter KramerCenter for Molecular Biology of Heidelberg University (ZMBH) and German Cancer Research Center (DKFZ), DKFZ-ZMBH Alliance, Im Neuenheimer Feld 282, Heidelberg D-69120, Germany. g.kramer@zmbh.uni-heidelberg.de bukau@zmbh.uni-heidelberg.de.ORCID https://orcid.org/0000-0001-7552-8393

Funding

European Research Council 743118
6 · The paper itself

Abstract

Accurate assembly of newly synthesized proteins into functional oligomers is crucial for cell activity. In this study, we investigated whether direct interaction of two nascent proteins, emerging from nearby ribosomes (co-co assembly), constitutes a general mechanism for oligomer formation. We used proteome-wide screening to detect nascent chain-connected ribosome pairs and identified hundreds of homomer subunits that co-co assemble in human cells. Interactions are mediated by five major domain classes, among which N-terminal coiled coils are the most prevalent. We were able to reconstitute co-co assembly of nuclear lamin in

Indexed as

Protein BiosynthesisProtein MultimerizationEscherichia coliHEK293 CellsHumansLaminsProtein DomainsProteomeRibosomesLaminsProteome

Identifiers

PMID33384371
PMCPMC7613021

What OpenQuestion holds

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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.