Evidence map›Paper›PMID 23732477›Full record

ReviewCold Spring Harbor perspectives in biology2013

Molecular mechanisms of fibroblast growth factor signaling in physiology and pathology.

Artur A Belov, Moosa Mohammadi

Open access · bronzeAbstract readReview
In one paragraph

Review in Cold Spring Harbor perspectives in biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 142 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
142citing papers in PubMed, 1 pooled it
–field-weighted citation impact
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

142 citing papers in PubMed, 1 synthesis or guideline pooled it, 271 citations in OpenAlex.

  1. Pooled it
  2. Recurrent Resistance Mutations to Lirafugratinib Inform Treatment Sequencing in FGFR2-Driven Tumors.Clinical cancer research : an official journal of the American Association for Cancer Research · 2026
    Trial
  3. Trial
  4. Review
  5. Review
  6. Review
  7. Review
  8. Article
  9. FGF family in health and disease.Molecular biomedicine · 2026
    Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Review
  17. FGF-based drug discovery: advances and challenges.Nature reviews. Drug discovery · 2025
    Review
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  19. Review
  20. Review

82 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 at 1 institution in 1 country.

Artur A BelovDepartment of Biochemistry and Molecular Pharmacology, New York University School of Medicine, New York, New York 10016, USA.
Moosa Mohammadi
New York University · US

Funding

MECHANISMS OF FGF RECEPTOR REGULATION AND SIGNALINGR01DE013686 · NIDCR · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI MOHAMMADI, MOOSA · 2000 to 2020
$12.3M
Training program in Molecular BiophysicsT32GM088118 · NIGMS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI STOKES, DAVID L. · 2010 to 2019
$1.8M
NIDCR NIH HHS DE13686NIDCR NIH HHS R01 DE013686NIGMS NIH HHS 5T32GM088118-03NIGMS NIH HHS T32 GM088118
6 · The paper itself

Abstract

Fibroblast growth factors (FGFs) signal in a paracrine or endocrine fashion to mediate a myriad of biological activities, ranging from issuing developmental cues, maintaining tissue homeostasis, and regulating metabolic processes. FGFs carry out their diverse functions by binding and dimerizing FGF receptors (FGFRs) in a heparan sulfate (HS) cofactor- or Klotho coreceptor-assisted manner. The accumulated wealth of structural and biophysical data in the past decade has transformed our understanding of the mechanism of FGF signaling in human health and development, and has provided novel concepts in receptor tyrosine kinase (RTK) signaling. Among these contributions are the elucidation of HS-assisted receptor dimerization, delineation of the molecular determinants of ligand-receptor specificity, tyrosine kinase regulation, receptor cis-autoinhibition, and tyrosine trans-autophosphorylation. These structural studies have also revealed how disease-associated mutations highjack the physiological mechanisms of FGFR regulation to contribute to human diseases. In this paper, we will discuss the structurally and biophysically derived mechanisms of FGF signaling, and how the insights gained may guide the development of therapies for treatment of a diverse array of human diseases.

Indexed as

Models, BiologicalModels, MolecularProtein ConformationAlternative SplicingDimerizationFibroblast Growth FactorsHumansMutationPhosphorylationReceptor Protein-Tyrosine KinasesReceptors, Fibroblast Growth FactorSignal TransductionFibroblast Growth FactorsReceptor Protein-Tyrosine KinasesReceptors, Fibroblast Growth Factor

Identifiers

PMID23732477
PMCPMC3660835
OpenAlexW2097036454

What OpenQuestion holds

Textmetadata
LicenceTDM
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.