Evidence map›Paper›PMID 19959837›Full record

ArticleThe Journal of biological chemistry2010

Nanoscale imaging of epidermal growth factor receptor clustering: effects of inhibitors.

Abedelnasser Abulrob, Zhengfang Lu, Ewa Baumann, Dusan Vobornik, Rod Taylor, Danica Stanimirovic, Linda J Johnston

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

45 citing papers in PubMed, 90 citations in OpenAlex.

  1. Review
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  10. High-Precision Protein-Tracking With Interferometric Scattering Microscopy.Frontiers in cell and developmental biology · 2020
    Article
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  12. Review
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  17. Super-resolution optical microscopy for studying membrane structure and dynamics.Journal of physics. Condensed matter : an Institute of Physics journal · 2017
    Review
  18. EGF and NRG induce phosphorylation of HER3/ERBB3 by EGFR using distinct oligomeric mechanisms.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  19. Article
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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

7 authors at 3 institutions in 2 countries.

Abedelnasser AbulrobInstitute for Biological Sciences, National Research Council of Canada, Ottawa, Ontario K1A 0R5, Canada. Abedelnasser.Abulrob@nrc.gc.ca
Zhengfang Lu
Ewa Baumann
Dusan Vobornik
Rod Taylor
Danica Stanimirovic
Linda J Johnston
Steacie Institute for Molecular Sciences · CAInstitute for Biological Sciences · CANational Academies of Sciences, Engineering, and Medicine · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The development of some solid tumors is associated with overexpression of the epidermal growth factor receptor (EGFR) and often correlates with poor prognosis. Near field scanning optical microscopy, a technique with subdiffraction-limited optical resolution, was used to examine the influence of two inhibitors (the chimeric 225 antibody and tyrosine phosphorylation inhibitor AG1478) on the nanoscale clustering of EGFR in HeLa cells. The EGFR is organized in small clusters, average diameter of 150 nm, on the plasma membrane for both control and EGF-treated cells. The numbers of receptors in individual clusters vary from as few as one or two proteins to greater than 100. Both inhibitors yield an increased cluster density and an increase in the fraction of clusters with smaller diameters and fewer receptors. Exposure to AG1478 also decreases the fraction of EGFR that colocalizes with both rafts and caveolae. EGF stimulation results in a significant loss of the full-length EGFR from the plasma membrane with the concomitant appearance of low molecular mass proteolytic products. By contrast, AG1478 reduces the level of EGFR degradation. Changes in receptor clustering provide one mechanism for regulating EGFR signaling and are relevant to the design of strategies for therapeutic interventions based on modulating EGFR signaling.

Indexed as

Cell MembraneDimerizationEnzyme InhibitorsErbB ReceptorsHeLa CellsHumansMembrane MicrodomainsMicroscopyMicroscopy, ConfocalNanotechnologyPrognosisProtein Structure, TertiaryQuinazolinesTyrphostinsEnzyme InhibitorsErbB ReceptorsQuinazolinesRTKI cpdTyrphostins

Identifiers

PMID19959837
PMCPMC2823441
OpenAlexW2062560208

What OpenQuestion holds

Textmetadata
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.