Evidence map›Paper›PMID 19038249›Full record

ReviewExperimental cell research2009

Ligand-induced ErbB receptor dimerization.

Mark A Lemmon

Open access · greenAbstract readReview
In one paragraph

Review in Experimental cell research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 109 papers.

0numbers the graph read from it
0cells of the map it votes in
109citing papers in PubMed
7.6field-weighted citation impact, top 2% 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

109 citing papers in PubMed, 214 citations in OpenAlex.

  1. Article
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  4. Beyond the membrane: rethinking EGFR signaling in physiology and cancer.Cellular and molecular life sciences : CMLS · 2026
    Review
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49 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

1 author at 1 institution in 1 country.

Mark A LemmonDepartment of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, 809C Stellar-Chance Laboratories, 422 Curie Boulevard, Philadelphia, PA 19104-6059, USA. mlemmon@mail.med.upenn.edu
University of Pennsylvania · US

Funding

ERBB RECEPTOR HOMO- AND HETERO- DIMERIZATIONR01CA079992 · NCI · UNIVERSITY OF PENNSYLVANIA · PI LEMMON, MARK A · 1999 to 2013
$3.7M
Mechanisms of ErbB2/HER2/Neu ActivationR01CA096768 · NCI · UNIVERSITY OF PENNSYLVANIA · PI LEMMON, MARK A. · 2002 to 2006
$1.4M
Mechanisms of invertebrate EGF receptor inhibitionR01CA125432 · NCI · UNIVERSITY OF PENNSYLVANIA · PI LEMMON, MARK A · 2007 to 2011
$1.2M
STRUCTURAL STUDIES OF ERBB/HER RECEPTOR DIMERIZATIONR21CA087182 · NCI · UNIVERSITY OF PENNSYLVANIA · PI LEMMON, MARK A. · 2000 to 2001
$238k
NCI NIH HHS R01 CA079992NCI NIH HHS R01-CA079992NCI NIH HHS R01 CA096768NCI NIH HHS R01 CA125432NCI NIH HHS R01-CA125432NCI NIH HHS R21 CA087182
6 · The paper itself

Abstract

Structural studies have provided important new insights into how ligand binding promotes homodimerization and activation of the EGF receptor and the other members of the ErbB family of receptor tyrosine kinases. These structures have also suggested possible explanations for the unique properties of ErbB2, which has no known ligand and can cause cell transformation (and tumorigenesis) by simple overexpression. In parallel with these advances, studies of the EGF receptor at the cell surface increasingly argue that the structural studies are missing key mechanistic components. This is particularly evident in the structural prediction that EGF binding linked to receptor dimerization should be positively cooperative, whereas cell-surface EGF-binding studies suggest negative cooperativity. In this review, I summarize studies of ErbB receptor extracellular regions in solution and of intact receptors at the cell surface, and attempt to reconcile the differences suggested by the two approaches. By combining results obtained with receptor 'parts', it is qualitatively possible to explain some models for the properties of the whole receptor. These considerations underline the need to consider the intact ErbB receptors as intact allosterically regulated enzymes, and to combine cellular and structural studies into a complete picture.

Indexed as

DimerizationAnimalsErbB ReceptorsHumansLigandsModels, MolecularOncogene Proteins v-erbBProtein BindingProtein Structure, TertiaryErbB ReceptorsLigandsOncogene Proteins v-erbB

Identifiers

PMID19038249
PMCPMC2667204
OpenAlexW2063917536

What OpenQuestion holds

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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.