Evidence map›Paper›PMID 27635238›Full record

ReviewF1000Research2016

EGF receptor ligands: recent advances.

Bhuminder Singh, Graham Carpenter, Robert J Coffey

Open access · goldAbstract readReview
In one paragraph

Review in F1000Research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 188 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
188citing papers in PubMed, 1 pooled it
11.0field-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

188 citing papers in PubMed, 1 synthesis or guideline pooled it, 309 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. The role of kinase domain dimerization in EGFR activation.Structure (London, England : 1993) · 2026
    Article
  12. Review
  13. Article
  14. Review
  15. mBio · 2026
    Article
  16. Beyond the membrane: rethinking EGFR signaling in physiology and cancer.Cellular and molecular life sciences : CMLS · 2026
    Review
  17. Review
  18. Article
  19. Article
  20. Review

128 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

3 authors at 2 institutions in 1 country.

Bhuminder SinghDepartment of Medicine, Vanderbilt University Medical Center, Nashville, TN, 37232, USA.
Graham CarpenterDepartment of Biochemistry, Vanderbilt University Medical Center, Nashville, TN, 37232, USA.
Robert J CoffeyDepartment of Medicine, Vanderbilt University Medical Center, Nashville, TN, 37232, USA; Department of Cell and Developmental Biology, Vanderbilt University Medical Center, Nashville, TN, 37232, USA; Veterans Health Administration, Tennessee Valley Healthcare System, Nashville, TN, 37212, USA.
Vanderbilt University Medical Center · USVA Tennessee Valley Healthcare System · US

Funding

Understanding and Controlling p120 Dysfunction in CRCP50CA095103 · NCI · VANDERBILT UNIVERSITY MEDICAL CENTER · PI COFFEY, ROBERT J. · 2002 to 2017
$33.6M
TRANSFORMING GROWTH FACTORS IN COLONIC NEOPLASIAR01CA046413 · NCI · VANDERBILT UNIVERSITY MEDICAL CENTER · PI COFFEY, ROBERT J. · 1988 to 2016
$8.8M
Roles for Lrig1 in Intestinal NeoplasiaR01CA151566 · NCI · VANDERBILT UNIVERSITY MEDICAL CENTER · PI COFFEY, ROBERT J. · 2010 to 2016
$2.1M
Role of EGFR ligand-containing exosomes in colorectal cancerR01CA163563 · NCI · VANDERBILT UNIVERSITY MEDICAL CENTER · PI COFFEY, ROBERT J. · 2013 to 2016
$1.7M
NCI NIH HHS P50 CA095103NCI NIH HHS R01 CA046413NCI NIH HHS R01 CA151566NCI NIH HHS R01 CA163563
6 · The paper itself

Abstract

Seven ligands bind to and activate the mammalian epidermal growth factor (EGF) receptor (EGFR/ERBB1/HER1): EGF, transforming growth factor-alpha (TGFA), heparin-binding EGF-like growth factor (HBEGF), betacellulin (BTC), amphiregulin (AREG), epiregulin (EREG), and epigen (EPGN). Of these, EGF, TGFA, HBEGF, and BTC are thought to be high-affinity ligands, whereas AREG, EREG, and EPGN constitute low-affinity ligands. This focused review is meant to highlight recent studies related to actions of the individual EGFR ligands, the interesting biology that has been uncovered, and relevant advances related to ligand interactions with the EGFR.

Indexed as

AmphireguinBetacellulinEGFRepidermal growth factorepigenEpiregulinHBEGFTransforming growth factor-alpha

Identifiers

PMID27635238
PMCPMC5017282
OpenAlexW2511292374

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.