Differential ErbB receptor dimerization modulates the ability of EGF receptor ligands to regulate metabolic flux.

Jennifer Macdonald-Obermann, Kevin Cho, Gary J Patti, Linda J Pike

Abstract read

In one paragraph

Article in The Journal of biological chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it

0cells of the map it votes in

0citing 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

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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Jennifer Macdonald-ObermannDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St Louis, Missouri, USA.

Kevin ChoDepartment of Chemistry, Medicine, Center for Mass Spectrometry and Metabolic Tracing, Washington University, St Louis, Missouri, USA.

Gary J PattiDepartment of Chemistry, Medicine, Center for Mass Spectrometry and Metabolic Tracing, Washington University, St Louis, Missouri, USA.

Linda J PikeDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St Louis, Missouri, USA. Electronic address: pike@wustl.edu.

Funding

Intrinsic Disorder and Agonist Bias in EGF Receptor SignalingR01GM142164 · NIGMS · WASHINGTON UNIVERSITY · PI PIKE, LINDA JOY · 2021 to 2024

$1.4M

NIGMS NIH HHS R01 GM142164

6 · The paper itself

Abstract

The epidermal growth factor (EGF) receptor tyrosine kinase binds seven different agonist ligands. It stimulates proliferation of MCF-7 cells while epigen and EPR, stimulate differentiation. This distinction is thought to be due to the phenomenon of ligand bias in which two agonists bind to the same receptor but generate different responses. These reported differences among EGFR ligands led us to examine their effects plus those of neureglin 2ß (NRG-2ß), an ErbB3-ErbB4 ligand, on metabolism in MCF-7 cells and MDA-MB-468 cells. We followed the flux of carbons from either [1,2-

Indexed as

ErbB ReceptorsProtein MultimerizationEpidermal Growth FactorGlycolysisHumansLigandsMCF-7 CellsEGFR protein, humanEpidermal Growth FactorErbB ReceptorsLigandscell signalingEGF receptorgrowth factorhormone receptormetabolomicstyrosine kinase

Identifiers

PMID42248463

DOI10.1016/j.jbc.2026.113230

PMCPMC13330678

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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.