Evidence map›Paper›PMID 37058003›Full record

ArticleJournal of proteome research2023

Rapid Profiling of Protein Complex Reorganization in Perturbed Systems.

Isabell Bludau, Charlotte Nicod, Claudia Martelli, Peng Xue, Moritz Heusel, Andrea Fossati, Federico Uliana, Fabian Frommelt, Ruedi Aebersold, Ben C Collins

Open access · hybridAbstract read
In one paragraph

Article in Journal of proteome research, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed, 1 pooled it
4.0field-weighted citation impact, top 5% 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

16 citing papers in PubMed, 1 synthesis or guideline pooled it, 28 citations in OpenAlex.

  1. Pooled it
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  5. Review
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  7. Article
  8. Review
  9. State-of-the-Art and Future Directions in Structural Proteomics.Molecular & cellular proteomics : MCP · 2025
    Review
  10. Understanding the molecular diversity of synapses.Nature reviews. Neuroscience · 2025
    Review
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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 at 4 institutions in 5 countries.

Isabell BludauDepartment of Biology, Institute of Molecular Systems Biology, ETH Zürich, Zürich, Switzerland 8092.
Charlotte NicodDepartment of Biology, Institute of Molecular Systems Biology, ETH Zürich, Zürich, Switzerland 8092.
Claudia MartelliDepartment of Biology, Institute of Molecular Systems Biology, ETH Zürich, Zürich, Switzerland 8092.
Peng XueDepartment of Biology, Institute of Molecular Systems Biology, ETH Zürich, Zürich, Switzerland 8092.
Moritz HeuselDepartment of Biology, Institute of Molecular Systems Biology, ETH Zürich, Zürich, Switzerland 8092.ORCID 0000-0002-8506-530X
Andrea FossatiDepartment of Biology, Institute of Molecular Systems Biology, ETH Zürich, Zürich, Switzerland 8092.
Federico UlianaDepartment of Biology, Institute of Molecular Systems Biology, ETH Zürich, Zürich, Switzerland 8092.
Fabian FrommeltDepartment of Biology, Institute of Molecular Systems Biology, ETH Zürich, Zürich, Switzerland 8092.
Ruedi AebersoldDepartment of Biology, Institute of Molecular Systems Biology, ETH Zürich, Zürich, Switzerland 8092.
Ben C CollinsSchool of Biological Sciences, Queen's University of Belfast, 19 Chlorine Gardens, Belfast, BT9 5DL, U.K.ORCID 0000-0003-0827-3495
ETH Zurich · CHGladstone Institutes · USLund University · SEQueen's University Belfast · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein complexes constitute the primary functional modules of cellular activity. To respond to perturbations, complexes undergo changes in their abundance, subunit composition, or state of modification. Understanding the function of biological systems requires global strategies to capture this contextual state information. Methods based on cofractionation paired with mass spectrometry have demonstrated the capability for deep biological insight, but the scope of studies using this approach has been limited by the large measurement time per biological sample and challenges with data analysis. There has been little uptake of this strategy into the broader life science community despite its rich biological information content. We present a rapid integrated experimental and computational workflow to assess the reorganization of protein complexes across multiple cellular states. The workflow combines short gradient chromatography and DIA/SWATH mass spectrometry with a data analysis toolset to quantify changes in a complex organization. We applied the workflow to study the global protein complex rearrangements of THP-1 cells undergoing monocyte to macrophage differentiation and subsequent stimulation of macrophage cells with lipopolysaccharide. We observed substantial proteome reorganization on differentiation and less pronounced changes in macrophage stimulation. We establish our integrated differential pipeline for rapid and state-specific profiling of protein complex organization.

Indexed as

ProteomeCell DifferentiationMass SpectrometryProteomeDIA/SWATHprotein complexprotein−protein interactionsquantitative interaction proteomics

Identifiers

PMID37058003
PMCPMC10167687
OpenAlexW4365484757

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.