Evidence map›Paper›PMID 1777504›Full record

ArticleCell regulation1991

Epidermal growth factor and transforming growth factor-alpha: differential intracellular routing and processing of ligand-receptor complexes.

R Ebner, R Derynck

Open access · greenAbstract readComparative Study
In one paragraph

Article in Cell regulation, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing papers in PubMed
5.8field-weighted citation impact, top 3% 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

85 citing papers in PubMed, 252 citations in OpenAlex.

  1. Trial
  2. Beyond the membrane: rethinking EGFR signaling in physiology and cancer.Cellular and molecular life sciences : CMLS · 2026
    Review
  3. Review
  4. Engineered calcium-regulated affinity protein for efficient internalization and lysosomal toxin delivery.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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  8. EGF, TGF-International journal of molecular sciences · 2023
    Article
  9. Biased activation of the receptor tyrosine kinase HER2.Cellular and molecular life sciences : CMLS · 2023
    Article
  10. Busting the Breast Cancer with AstraZeneca's Gefitinib.Advances in pharmacological and pharmaceutical sciences · 2023
    Review
  11. Article
  12. Review
  13. Review
  14. Review
  15. Review
  16. Chronic and acute arsenic exposure enhance EGFR expression via distinct molecular mechanisms.Toxicology in vitro : an international journal published in association with BIBRA · 2020
    Article
  17. Review
  18. Article
  19. Article
  20. Article

25 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

2 authors.

R EbnerDepartment of Developmental Biology, Genentech, Inc., South San Francisco, California 94080.
R Derynck

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Two structurally related but different polypeptide growth factors, epidermal growth factor (EGF) and transforming growth factor-alpha (TGF-alpha), exert their activities after interaction with a common cell-surface EGF/TGF-alpha-receptor. Comparative studies of the effects of both ligands have established that TGF-alpha is more potent than EGF in a variety of biological systems. This observation is not explained by differences in affinities of the ligands for the receptor, because the affinity-constants of both factors are very similar. We have compared the intracellular processing of ligand-receptor complexes using either EGF or TGF-alpha in two different cell systems. We found that TGF-alpha dissociates from the EGF/TGF-alpha-receptor at much higher pH than EGF, which may reflect the substantial difference in the calculated isoelectric points. After internalization, the intracellular TGF-alpha is more rapidly cleared than EGF, and a substantial portion of the released TGF-alpha represents undegraded TGF-alpha in contrast to the mostly degraded EGF. In addition, TGF-alpha did not induce a complete down-regulation of cell surface receptors, as observed with EGF, which is at least in part responsible for a much sooner recovery of the ligand-binding ability after down-regulation, in the case of TGF-alpha. These differences in processing of the ligand-receptor complexes may explain why TGF-alpha exerts quantitatively higher activities than EGF.

Indexed as

Affinity LabelsAnimalsBinding, CompetitiveCell LineDown-RegulationEndocytosisEpidermal Growth FactorErbB ReceptorsHumansMiceRecombinant ProteinsTransforming Growth Factor alphaAffinity LabelsEpidermal Growth FactorErbB ReceptorsRecombinant ProteinsTransforming Growth Factor alpha

Identifiers

PMID1777504
PMCPMC361851
OpenAlexW2146074838

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.