Evidence map›Paper›PMID 30242154›Full record

ArticleNature communications2018

A conformational sensor based on genetic code expansion reveals an autocatalytic component in EGFR activation.

Martin Baumdick, Márton Gelléri, Chayasith Uttamapinant, Václav Beránek, Jason W Chin, Philippe I H Bastiaens

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

19 citing papers in PubMed, 36 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Review
  6. Bioorthogonal Reactions in Bioimaging.Topics in current chemistry (Cham) · 2024
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. OXTRNature communications · 2022
    Article
  13. Reprogramming the genetic code.Nature reviews. Genetics · 2021
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
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

6 authors at 3 institutions in 2 countries.

Martin BaumdickDepartment of Systemic Cell Biology, Max Planck Institute of Molecular Physiology, Otto-Hahn-Street 11, 44227, Dortmund, Germany.
Márton GellériDepartment of Systemic Cell Biology, Max Planck Institute of Molecular Physiology, Otto-Hahn-Street 11, 44227, Dortmund, Germany.
Chayasith UttamapinantMedical Research Council Laboratory of Molecular Biology, Cambridge Biomedical Campus, Francis Crick Avenue, Cambridge, CB2 0QH, UK.
Václav BeránekMedical Research Council Laboratory of Molecular Biology, Cambridge Biomedical Campus, Francis Crick Avenue, Cambridge, CB2 0QH, UK.
Jason W ChinMedical Research Council Laboratory of Molecular Biology, Cambridge Biomedical Campus, Francis Crick Avenue, Cambridge, CB2 0QH, UK. chin@mrc-lmb.cam.ac.uk.ORCID http://orcid.org/0000-0003-1219-4757
Philippe I H BastiaensDepartment of Systemic Cell Biology, Max Planck Institute of Molecular Physiology, Otto-Hahn-Street 11, 44227, Dortmund, Germany. philippe.bastiaens@mpi-dortmund.mpg.de.
MRC Laboratory of Molecular Biology · GBTU Dortmund University · DEMax Planck Institute of Molecular Physiology · DE

Funding

European Molecular Biology Organization (EMBO) ASTF No: 122-2015Medical Research Council MC_U105181009Medical Research Council MC_UP_A024_1008Medical Research Council (MRC) MC_U105181009Medical Research Council (MRC) MC_UP_A024_1008
6 · The paper itself

Abstract

Epidermal growth factor receptor (EGFR) activation by growth factors (GFs) relies on dimerization and allosteric activation of its intrinsic kinase activity, resulting in trans-phosphorylation of tyrosines on its C-terminal tail. While structural and biochemical studies identified this EGF-induced allosteric activation, imaging collective EGFR activation in cells and molecular dynamics simulations pointed at additional catalytic EGFR activation mechanisms. To gain more insight into EGFR activation mechanisms in living cells, we develop a Förster resonance energy transfer (FRET)-based conformational EGFR indicator (CONEGI) using genetic code expansion that reports on conformational transitions in the EGFR activation loop. Comparing conformational transitions, self-association and auto-phosphorylation of CONEGI and its Y845F mutant reveals that Y

Indexed as

ErbB ReceptorsIntercellular Signaling Peptides and ProteinsProtein ConformationDimerizationFluorescence Resonance Energy TransferHEK293 CellsHumansPhosphorylationEGFR protein, humanErbB ReceptorsIntercellular Signaling Peptides and Proteins

Identifiers

PMID30242154
PMCPMC6155120
OpenAlexW2953109569

What OpenQuestion 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 OpenQuestion graph.