Evidence map›Paper›PMID 22939629›Full record

ArticleCell2012

A census of human soluble protein complexes.

Pierre C Havugimana, G Traver Hart, Tamás Nepusz, Haixuan Yang, Andrei L Turinsky, Zhihua Li, Peggy I Wang, Daniel R Boutz, Vincent Fong, Sadhna Phanse and 14 more

Open access · greenAbstract read
In one paragraph

Article in Cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 488 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
488citing papers in PubMed, 2 pooled it
27.0field-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

488 citing papers in PubMed, 2 syntheses or guidelines pooled it, 897 citations in OpenAlex.

  1. Pooled it
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  16. Harnessing evolution to infer protein networks.Nature reviews. Genetics · 2026
    Article
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428 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

24 authors at 5 institutions in 3 countries.

Pierre C HavugimanaBanting and Best Department of Medical Research, Donnelly Centre for Cellular and Biomolecular Research, University of Toronto, Toronto, Ontario M5S 3E1, Canada.
G Traver Hart
Tamás Nepusz
Haixuan Yang
Andrei L Turinsky
Zhihua Li
Peggy I Wang
Daniel R Boutz
Vincent Fong
Sadhna Phanse
Mohan Babu
Stephanie A Craig
Pingzhao Hu
Cuihong Wan
James Vlasblom
Vaqaar-un-Nisa Dar
Alexandr Bezginov
Gregory W Clark
Gabriel C Wu
Shoshana J Wodak
Elisabeth R M Tillier
Alberto Paccanaro
Edward M Marcotte
Andrew Emili
University of Toronto · CAThe University of Texas at Austin · USHospital for Sick Children · CAOntario Institute for Cancer Research · CARoyal Holloway University of London · GB

Funding

Next-Generation Proteomics: Massively Parallel Single-Molecule Protein IdentificaDP1GM106408 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI MARCOTTE, EDWARD M · 2012 to 2016
$3.8M
Proteomics of widespread, reversible protein assemblies in aging and aggregationR01GM076536 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI MARCOTTE, EDWARD M · 2006 to 2014
$2.9M
Reconstructing the eukaryotic cell cycle gene networkR01GM067779 · NIGMS · UNIVERSITY OF TEXAS AUSTIN · PI MARCOTTE, EDWARD M · 2004 to 2012
$2.1M
Systematic discovery of nonobvious human disease models by orthologous phenotypesR01GM088624 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI MARCOTTE, EDWARD M · 2009 to 2012
$1.2M
Biotechnology and Biological Sciences Research Council BB/F00964X/1Biotechnology and Biological Sciences Research Council BB/K004131/1CIHR MOP 82940NIGMS NIH HHS DP1 GM106408NIGMS NIH HHS R01 GM067779NIGMS NIH HHS R01 GM076536NIGMS NIH HHS R01 GM088624
6 · The paper itself

Abstract

Cellular processes often depend on stable physical associations between proteins. Despite recent progress, knowledge of the composition of human protein complexes remains limited. To close this gap, we applied an integrative global proteomic profiling approach, based on chromatographic separation of cultured human cell extracts into more than one thousand biochemical fractions that were subsequently analyzed by quantitative tandem mass spectrometry, to systematically identify a network of 13,993 high-confidence physical interactions among 3,006 stably associated soluble human proteins. Most of the 622 putative protein complexes we report are linked to core biological processes and encompass both candidate disease genes and unannotated proteins to inform on mechanism. Strikingly, whereas larger multiprotein assemblies tend to be more extensively annotated and evolutionarily conserved, human protein complexes with five or fewer subunits are far more likely to be functionally unannotated or restricted to vertebrates, suggesting more recent functional innovations.

Indexed as

Protein Interaction MapsHumansMultiprotein ComplexesProteinsProteomicsTandem Mass SpectrometryMultiprotein ComplexesProteins

Identifiers

PMID22939629
PMCPMC3477804
OpenAlexW2143892509

What OpenQuestion holds

Textmetadata
LicenceTDM
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.