Evidence map›Paper›PMID 12242295›Full record

ArticleMolecular and cellular biology2002

Structural basis for activation of fibroblast growth factor signaling by sucrose octasulfate.

Brian K Yeh, Anna V Eliseenkova, Alexander N Plotnikov, David Green, Jared Pinnell, Tulay Polat, Amel Gritli-Linde, Robert J Linhardt, Moosa Mohammadi

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

22 citing papers in PubMed, 58 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Comparison of topical sucralfate with dexpanthenol in rat wound model.International journal of experimental pathology · 2022
    Article
  5. Article
  6. Review
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  8. Article
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  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Effects of temperature and additives on stability and spectrum of a therapeutic fibroblast growth factor.Daru : journal of Faculty of Pharmacy, Tehran University of Medical Sciences · 2011
    Article
  16. Article
  17. Article
  18. Dimerization effect of sucrose octasulfate on rat FGF1.Acta crystallographica. Section F, Structural biology and crystallization communications · 2008
    Article
  19. 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

9 authors at 4 institutions in 3 countries.

Brian K YehDepartments of Pharmacology. Medicine, New York University School of Medicine, New York, New York 10016, USA.
Anna V Eliseenkova
Alexander N Plotnikov
David Green
Jared Pinnell
Tulay Polat
Amel Gritli-Linde
Robert J Linhardt
Moosa Mohammadi
University of Iowa · USUniversity School · USGöteborgs Stads · SENew 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
Synthetic Heparan Sulfate: Probing Biosynthesis to Prepare Defined DrugsR01HL062244 · NHLBI · UNIVERSITY OF IOWA · PI DEANGELIS, PAUL L, LINHARDT, ROBERT J · 2001 to 2016
$4.1M
HEPARIN-PROTEIN/PEPTIDE INTERACTIONSR01HL052622 · NHLBI · UNIVERSITY OF IOWA · PI LINHARDT, ROBERT J · 1996 to 2003
$1.1M
NHLBI NIH HHS HL-52622NHLBI NIH HHS R01 HL052622NHLBI NIH HHS R01 HL062244NIDCR NIH HHS DE-13686NIDCR NIH HHS R01 DE013686
6 · The paper itself

Abstract

Sucrose octasulfate (SOS) is believed to stimulate fibroblast growth factor (FGF) signaling by binding and stabilizing FGFs. In this report, we show that SOS induces FGF-dependent dimerization of FGF receptors (FGFRs). The crystal structure of the dimeric FGF2-FGFR1-SOS complex at 2.6-A resolution reveals a symmetric assemblage of two 1:1:1 FGF2-FGFR1-SOS ternary complexes. Within each ternary complex SOS binds to FGF and FGFR and thereby increases FGF-FGFR affinity. SOS also interacts with the adjoining FGFR and thereby promotes protein-protein interactions that stabilize dimerization. This structural finding is supported by the inability of selectively desulfated SOS molecules to promote receptor dimerization. Thus, we propose that SOS potentiates FGF signaling by imitating the dual role of heparin in increasing FGF-FGFR affinity and promoting receptor dimerization. Hence, the dimeric FGF-FGFR-SOS structure substantiates the recently proposed "two-end" model, by which heparin induces FGF-FGFR dimerization. Moreover, the FGF-FGFR-SOS structure provides an attractive template for the development of easily synthesized SOS-related heparin agonists and antagonists that may hold therapeutic potential.

Indexed as

Signal TransductionAnimalsCrystallography, X-RayDimerizationFibroblast Growth Factor 2HeparinMiceModels, MolecularProtein Structure, TertiaryReceptor, Fibroblast Growth Factor, Type 1Receptor Protein-Tyrosine KinasesReceptors, Fibroblast Growth FactorSucroseFgfr1 protein, mouseFibroblast Growth Factor 2HeparinReceptor, Fibroblast Growth Factor, Type 1Receptor Protein-Tyrosine KinasesReceptors, Fibroblast Growth FactorSucrosesucrose octasulfate

Identifiers

PMID12242295
PMCPMC139814
OpenAlexW2102098049

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.