Evidence map›Paper›PMID 1316275›Full record

ArticleThe EMBO journal1992

A confined variable region confers ligand specificity on fibroblast growth factor receptors: implications for the origin of the immunoglobulin fold.

A Yayon, Y Zimmer, G H Shen, A Avivi, Y Yarden, D Givol

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
8.6field-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

51 citing papers in PubMed, 163 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Article
  6. Roles of FGFR in oral carcinogenesis.Cell proliferation · 2016
    Review
  7. Wnt and FGF mediated epithelial-mesenchymal crosstalk during lung development.Developmental dynamics : an official publication of the American Association of Anatomists · 2015
    Review
  8. Review
  9. Review
  10. Review
  11. Review
  12. Article
  13. Article
  14. Detection of isoform-specific fibroblast growth factor receptors by whole-mount in situ hybridization in early chick embryos.Developmental dynamics : an official publication of the American Association of Anatomists · 2011
    Article
  15. Article
  16. Article
  17. Article
  18. Skeletal overgrowth is mediated by deficiency in a specific isoform of fibroblast growth factor receptor 3.Proceedings of the National Academy of Sciences of the United States of America · 2007
    Article
  19. NMR structure of the first Ig module of mouse FGFR1.Protein science : a publication of the Protein Society · 2006
    Article
  20. Article
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

6 authors at 1 institution in 1 country.

A YayonDepartment of Chemical Immunology, Weizmann Institute of Science, Rehovot, Israel.
Y Zimmer
G H Shen
A Avivi
Y Yarden
D Givol
Weizmann Institute of Science · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Binding of cellular growth factors to their receptors constitutes a highly specific interaction and the basis for cell and tissue-type specific growth and differentiation. A unique feature of fibroblast growth factor (FGF) receptors is the multitude of structural variants and an unprecedented degree of cross-reactivity between receptors and their various ligands. To examine receptor-ligand specificity within these families of growth factors and receptors, we used genetic engineering to substitute discrete regions between Bek/FGFR2 and the closely related keratinocyte growth factor receptor (KGFR). We demonstrate that a confined, 50 amino acid, variable region within the third immunoglobulin-like domain of Bek and KGFR exclusively determines their ligand binding specificities. Replacing the variable region of Bek/FGFR2 with the corresponding sequence of KGFR resulted in a chimeric receptor which bound KGF and had lost the capacity to bind basic FGF. We present evidence that the two variable sequences are encoded by two distinct exons that map close together in the mouse genome and follow a constant exon, suggesting that the two receptors were derived from a common gene by mutually exclusive alternative mRNA splicing. These results identify the C-terminal half of the third immunoglobulin-like domain of FGF receptors as a major determinant for ligand binding and present a novel genetic mechanism for altering receptor-ligand specificity and generating receptor diversity.

Indexed as

3T3 CellsAmino Acid SequenceAnimalsBase SequenceCross-Linking ReagentsFibroblast Growth FactorsImmunoglobulinsImmunoglobulin Variable RegionMiceMolecular Sequence DataPlasmidsProtein ConformationReceptor, Fibroblast Growth Factor, Type 2Receptors, Cell SurfaceReceptors, Fibroblast Growth FactorRecombinant Fusion ProteinsCross-Linking ReagentsFibroblast Growth FactorsImmunoglobulinsImmunoglobulin Variable Regionkeratinocyte growth factor receptorReceptor, Fibroblast Growth Factor, Type 2Receptors, Cell SurfaceReceptors, Fibroblast Growth FactorRecombinant Fusion ProteinsRNA, Messenger

Identifiers

PMID1316275
PMCPMC556646
OpenAlexW986709771

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.