Evidence map›Paper›PMID 1309595›Full record

ArticleMolecular and cellular biology1992

Differential splicing in the extracellular region of fibroblast growth factor receptor 1 generates receptor variants with different ligand-binding specificities.

S Werner, D S Duan, C de Vries, K G Peters, D E Johnson, L T Williams

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.

0numbers the graph read from it
0cells of the map it votes in
77citing papers in PubMed
14.5field-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

77 citing papers in PubMed, 316 citations in OpenAlex.

  1. Review
  2. Article
  3. FGF signaling in cranial suture development and related diseases.Frontiers in cell and developmental biology · 2023
    Review
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  8. Article
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  12. Review
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  16. Fibroblast growth factor receptor 4 polymorphism is associated with increased risk and poor prognosis of non-Hodgkin's lymphoma.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2014
    Article
  17. Article
  18. Article
  19. Review
  20. Functional roles of fibroblast growth factor receptors (FGFRs) signaling in human cancers.Apoptosis : an international journal on programmed cell death · 2013
    Review

17 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

6 authors at 1 institution in 1 country.

S WernerDepartment of Medicine, Howard Hughes Medical Institute, University of California, San Francisco 94143-0724.
D S Duan
C de Vries
K G Peters
D E Johnson
L T Williams
Howard Hughes Medical Institute · US

Funding

STRUCTURE ANALYSIS OF PROTEINS INVOLVED IN CARDIOVASCULAR FUNCTION/DEVELOPMENTP01HL043821 · NHLBI · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI ORDAHL, CHARLES P · 1989 to 1996
–
NHLBI NIH HHS HL-43821
6 · The paper itself

Abstract

We have cloned a genomic region of the murine fibroblast growth factor (FGF) receptor 1 (FGFR1) gene that includes three alternative exons for the third immunoglobulinlike domain in the extracellular region of the receptor. The mRNA of one of these splice variants encodes a secreted receptor that lacks transmembrane and cytoplasmic sequences as well as a portion of the third immunoglobulinlike domain. Highest levels of mRNA encoding this variant were found in brain, skeletal muscle, and skin. We expressed this form of FGFR1 in CHO cells and showed that the recombinant secreted protein binds acidic FGF. We also discovered a novel alternative exon in the third immunoglobulinlike domain that encodes part of a transmembrane FGFR1 mRNA. This exon is highly homologous to the corresponding region of the keratinocyte growth factor receptor. Transcripts including this exon were present at highest levels in the skin. We cloned an FGFR1 cDNA which includes this exon and expressed this receptor variant in L6 rat skeletal muscle myoblasts. The new receptor variant had a 50-fold-lower affinity for basic FGF than does the published FGFR1 variant, whereas both forms of receptor bound acidic FGF with high affinity. These results show that the third immunoglobulinlike domain plays an important role in determining the binding specificities for different FGFs. Our data provide the first evidence that differential splicing in the extracellular region of a receptor gene generates receptor variants with different ligand-binding specificities.

Indexed as

RNA SplicingAmino Acid SequenceAnimalsBase SequenceBinding SitesCells, CulturedCloning, MolecularDNAFibroblast Growth FactorsGenetic VariationHumansLigandsMiceMice, Inbred BALB CMolecular Sequence DataReceptors, Cell SurfaceDNAFibroblast Growth FactorsLigandsReceptors, Cell SurfaceReceptors, Fibroblast Growth Factor

Identifiers

PMID1309595
PMCPMC364071
OpenAlexW2118830070

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.