Evidence map›Paper›PMID 27796308›Full record

ArticleNature communications2016

EGFR oligomerization organizes kinase-active dimers into competent signalling platforms.

Sarah R Needham, Selene K Roberts, Anton Arkhipov, Venkatesh P Mysore, Christopher J Tynan, Laura C Zanetti-Domingues, Eric T Kim, Valeria Losasso, Dimitrios Korovesis, Michael Hirsch and 11 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 122 papers.

0numbers the graph read from it
0cells of the map it votes in
122citing papers in PubMed
8.7field-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

122 citing papers in PubMed, 209 citations in OpenAlex.

  1. Article
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  4. Review
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  7. Review
  8. Article
  9. Article
  10. Beyond the membrane: rethinking EGFR signaling in physiology and cancer.Cellular and molecular life sciences : CMLS · 2026
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Clustering of Membrane Receptors: Insights from DNA Origami-Based Approaches.Small (Weinheim an der Bergstrasse, Germany) · 2025
    Review
  20. Article

62 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

21 authors at 6 institutions in 4 countries.

Sarah R NeedhamCentral Laser Facility, Research Complex at Harwell, Science and Technology Facilities Council, Rutherford Appleton Laboratory, Harwell Oxford, Didcot, Oxford OX11 0QX, UK.
Selene K RobertsCentral Laser Facility, Research Complex at Harwell, Science and Technology Facilities Council, Rutherford Appleton Laboratory, Harwell Oxford, Didcot, Oxford OX11 0QX, UK.
Anton ArkhipovD.E. Shaw Research, New York, New York 10036, USA.
Venkatesh P MysoreD.E. Shaw Research, New York, New York 10036, USA.
Christopher J TynanCentral Laser Facility, Research Complex at Harwell, Science and Technology Facilities Council, Rutherford Appleton Laboratory, Harwell Oxford, Didcot, Oxford OX11 0QX, UK.
Laura C Zanetti-DominguesCentral Laser Facility, Research Complex at Harwell, Science and Technology Facilities Council, Rutherford Appleton Laboratory, Harwell Oxford, Didcot, Oxford OX11 0QX, UK.
Eric T KimD.E. Shaw Research, New York, New York 10036, USA.
Valeria LosassoComputational Science and Engineering Department, Science and Technology Facilities Council, Daresbury Laboratory, Warrington WA4 4AD, UK.
Dimitrios KorovesisCentral Laser Facility, Research Complex at Harwell, Science and Technology Facilities Council, Rutherford Appleton Laboratory, Harwell Oxford, Didcot, Oxford OX11 0QX, UK.
Michael HirschCentral Laser Facility, Research Complex at Harwell, Science and Technology Facilities Council, Rutherford Appleton Laboratory, Harwell Oxford, Didcot, Oxford OX11 0QX, UK.
Daniel J RolfeCentral Laser Facility, Research Complex at Harwell, Science and Technology Facilities Council, Rutherford Appleton Laboratory, Harwell Oxford, Didcot, Oxford OX11 0QX, UK.
David T ClarkeCentral Laser Facility, Research Complex at Harwell, Science and Technology Facilities Council, Rutherford Appleton Laboratory, Harwell Oxford, Didcot, Oxford OX11 0QX, UK.
Martyn D WinnComputational Science and Engineering Department, Science and Technology Facilities Council, Daresbury Laboratory, Warrington WA4 4AD, UK.
Alireza LajevardipourCentre for Micro-Photonics, Faculty of Science, Engineering and Technology, Swinburne University of Technology, Hawthorn, Victoria 3122, Australia.ORCID 0000-0003-1925-6113
Andrew H A ClaytonCentre for Micro-Photonics, Faculty of Science, Engineering and Technology, Swinburne University of Technology, Hawthorn, Victoria 3122, Australia.
Linda J PikeDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St Louis, Missouri 63110, USA.
Michela PeraniDivision of Cancer Studies, King's College London, Guy's Medical School Campus, London SE1 1UL, UK.
Peter J ParkerDivision of Cancer Studies, King's College London, Guy's Medical School Campus, London SE1 1UL, UK.
Yibing ShanD.E. Shaw Research, New York, New York 10036, USA.
David E ShawD.E. Shaw Research, New York, New York 10036, USA.
Marisa L Martin-FernandezCentral Laser Facility, Research Complex at Harwell, Science and Technology Facilities Council, Rutherford Appleton Laboratory, Harwell Oxford, Didcot, Oxford OX11 0QX, UK.
Rutherford Appleton Laboratory · GBD. E. Shaw Research · USKing's College London · GBScience and Technology Facilities Council · GBSwinburne University of Technology · AUWashington University in St. Louis · US

Funding

HETERODIMERIZATION IN ERBB RECEPTORSR01GM099695 · NIGMS · WASHINGTON UNIVERSITY · PI PIKE, LINDA JOY · 2012 to 2015
$1.1M
Biotechnology and Biological Sciences Research Council BB/G006911/1Biotechnology and Biological Sciences Research Council BB/G007160/1Medical Research Council MC_EX_MR/K015591/1NIGMS NIH HHS R01 GM099695
6 · The paper itself

Abstract

Epidermal growth factor receptor (EGFR) signalling is activated by ligand-induced receptor dimerization. Notably, ligand binding also induces EGFR oligomerization, but the structures and functions of the oligomers are poorly understood. Here, we use fluorophore localization imaging with photobleaching to probe the structure of EGFR oligomers. We find that at physiological epidermal growth factor (EGF) concentrations, EGFR assembles into oligomers, as indicated by pairwise distances of receptor-bound fluorophore-conjugated EGF ligands. The pairwise ligand distances correspond well with the predictions of our structural model of the oligomers constructed from molecular dynamics simulations. The model suggests that oligomerization is mediated extracellularly by unoccupied ligand-binding sites and that oligomerization organizes kinase-active dimers in ways optimal for auto-phosphorylation in trans between neighbouring dimers. We argue that ligand-induced oligomerization is essential to the regulation of EGFR signalling.

Indexed as

AnimalsArtifactsBinding SitesCHO CellsCricetinaeCricetulusEpidermal Growth FactorErbB ReceptorsFluorescence Resonance Energy TransferLigandsMolecular Dynamics SimulationPhosphorylationProtein DomainsProtein MultimerizationSignal TransductionEpidermal Growth FactorErbB ReceptorsLigands

Identifiers

PMID27796308
PMCPMC5095584
OpenAlexW2543947893

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.