Evidence map›Paper›PMID 37968396›Full record

ArticleNature2023

The social and structural architecture of the yeast protein interactome.

André C Michaelis, Andreas-David Brunner, Maximilian Zwiebel, Florian Meier, Maximilian T Strauss, Isabell Bludau, Matthias Mann

Open access · hybridAbstract read
In one paragraph

Article in Nature, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
15.4field-weighted citation impact, top 1% 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

63 citing papers in PubMed, 101 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Mapping the architecture of protein complexes inProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  6. Review
  7. Review
  8. Article
  9. ANYI: The ANnotated Yeast Interactome.bioRxiv : the preprint server for biology · 2026
    Article
  10. Article
  11. Article
  12. Mechanistic dissection of BLTP2 targeting to ER-PM contact sites.bioRxiv : the preprint server for biology · 2026
    Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article

3 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 4 institutions in 2 countries.

André C MichaelisMax-Planck Institute of Biochemistry, Martinsried, Germany.ORCID 0000-0002-7519-3295
Andreas-David BrunnerMax-Planck Institute of Biochemistry, Martinsried, Germany.ORCID 0000-0002-2733-7899
Maximilian ZwiebelMax-Planck Institute of Biochemistry, Martinsried, Germany.
Florian MeierMax-Planck Institute of Biochemistry, Martinsried, Germany.ORCID 0000-0003-4729-175X
Maximilian T StraussNNF Center for Protein Research, University of Copenhagen, Copenhagen, Denmark.ORCID 0000-0003-3320-6833
Isabell BludauMax-Planck Institute of Biochemistry, Martinsried, Germany.ORCID 0000-0002-2601-238X
Matthias MannMax-Planck Institute of Biochemistry, Martinsried, Germany. mmann@biochem.mpg.de.ORCID 0000-0003-1292-4799
Max Planck Institute of Biochemistry · DEUniversity of Copenhagen · DKBoehringer Ingelheim (Germany) · DEJena University Hospital · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cellular functions are mediated by protein-protein interactions, and mapping the interactome provides fundamental insights into biological systems. Affinity purification coupled to mass spectrometry is an ideal tool for such mapping, but it has been difficult to identify low copy number complexes, membrane complexes and complexes that are disrupted by protein tagging. As a result, our current knowledge of the interactome is far from complete, and assessing the reliability of reported interactions is challenging. Here we develop a sensitive high-throughput method using highly reproducible affinity enrichment coupled to mass spectrometry combined with a quantitative two-dimensional analysis strategy to comprehensively map the interactome of Saccharomyces cerevisiae. Thousand-fold reduced volumes in 96-well format enabled replicate analysis of the endogenous GFP-tagged library covering the entire expressed yeast proteome

Indexed as

Protein Interaction MappingProtein Interaction MapsProteomeSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsDatabases, FactualEpigenesis, GeneticMass SpectrometryReproducibility of ResultsProteomeSaccharomyces cerevisiae Proteins

Identifiers

PMID37968396
PMCPMC10700138
OpenAlexW4388694323

What Socratic holds

Textmetadata
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 Socratic graph.