Evidence map›Paper›PMID 24043423›Full record

ArticleMolecular & cellular proteomics : MCP2013

Characterization of native protein complexes and protein isoform variation using size-fractionation-based quantitative proteomics.

Kathryn J Kirkwood, Yasmeen Ahmad, Mark Larance, Angus I Lamond

Abstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers.

0numbers the graph read from it
0cells of the map it votes in
86citing 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

86 citing papers in PubMed.

  1. TheScience advances · 2026
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26 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

4 authors.

Kathryn J KirkwoodCentre for Gene Regulation and Expression, College of Life Sciences, University of Dundee, Dow St., Dundee, DD1 5EH, United Kingdom.
Yasmeen Ahmad
Mark Larance
Angus I Lamond

Funding

Biotechnology and Biological Sciences Research Council BB/E010709/1Biotechnology and Biological Sciences Research Council BB/H007849/1Biotechnology and Biological Sciences Research Council BB/K003801/1Biotechnology and Biological Sciences Research Council C20035Medical Research Council G0901002Wellcome Trust 073980Wellcome Trust 073980/Z/03/ZWellcome Trust 08136/Z/03/ZWellcome Trust 083524/Z/07/ZWellcome Trust 0909444/Z/09/ZWellcome Trust 097945Wellcome Trust 097945/B/11/Z
6 · The paper itself

Abstract

Proteins form a diverse array of complexes that mediate cellular function and regulation. A largely unexplored feature of such protein complexes is the selective participation of specific protein isoforms and/or post-translationally modified forms. In this study, we combined native size-exclusion chromatography (SEC) with high-throughput proteomic analysis to characterize soluble protein complexes isolated from human osteosarcoma (U2OS) cells. Using this approach, we have identified over 71,500 peptides and 1,600 phosphosites, corresponding to over 8,000 proteins, distributed across 40 SEC fractions. This represents >50% of the predicted U2OS cell proteome, identified with a mean peptide sequence coverage of 27% per protein. Three biological replicates were performed, allowing statistical evaluation of the data and demonstrating a high degree of reproducibility in the SEC fractionation procedure. Specific proteins were detected interacting with multiple independent complexes, as typified by the separation of distinct complexes for the MRFAP1-MORF4L1-MRGBP interaction network. The data also revealed protein isoforms and post-translational modifications that selectively associated with distinct subsets of protein complexes. Surprisingly, there was clear enrichment for specific Gene Ontology terms associated with differential size classes of protein complexes. This study demonstrates that combined SEC/MS analysis can be used for the system-wide annotation of protein complexes and to predict potential isoform-specific interactions. All of these SEC data on the native separation of protein complexes have been integrated within the Encyclopedia of Proteome Dynamics, an online, multidimensional data-sharing resource available to the community.

Indexed as

Protein Processing, Post-TranslationalCarrier ProteinsCell Line, TumorChromatography, GelDatabases, ProteinGene Expression RegulationGenetic VariationHistone AcetyltransferasesHumansInternetIntracellular Signaling Peptides and ProteinsMass SpectrometryNuclear ProteinsOsteoblastsPhosphorylationProtein BindingCarrier ProteinsHistone AcetyltransferasesIntracellular Signaling Peptides and ProteinsMORF4L1 protein, humanMRFAP1 protein, humanMRGBP protein, humanNuclear ProteinsProtein IsoformsProteomeTranscription Factors

Identifiers

PMID24043423
PMCPMC3861729

What OpenQuestion holds

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Registered trials

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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.