ArticleThe Biochemical journal2006
Multimers of the fibroblast growth factor (FGF)-FGF receptor-saccharide complex are formed on long oligomers of heparin.
Article in The Biochemical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
What it found
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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.
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.
Who cites it
28 citing papers in PubMed, 50 citations in OpenAlex.
- Developing FGF2 Mutants with Selectively Reduced Heparan Sulfate Affinity to Explore their Impact on FGFR1 Signaling.Chembiochem : a European journal of chemical biology · 2025Article
- The dynamic nature of netrin-1 and the structural basis for glycosaminoglycan fragment-induced filament formation.Nature communications · 2023Article
- The protein common assembly database (ProtCAD)-a comprehensive structural resource of protein complexes.Nucleic acids research · 2023Article
- Towards better understanding of the heparin role in NETosis: feasibility of using native mass spectrometry to monitor interactions of neutrophil elastase with heparin oligomers.International journal of mass spectrometry · 2021Article
- Identification of Protein Recognition Elements within Heparin Chains Using Enzymatic Foot-Printing in Solution and Online SEC/MS.Analytical chemistry · 2020Article
- Evaluation of top-down mass spectrometry and ion-mobility spectroscopy as a means of mapping protein-binding motifs within heparin chains.The Analyst · 2020Article
- The Role of Fibroblast Growth Factor 23 in Inflammation and Anemia.International journal of molecular sciences · 2019Review
- Growth Differentiation Factor 5-Mediated Enhancement of Chondrocyte Phenotype Is Inhibited by Heparin: Implications for the Use of Heparin in the Clinic and in Tissue Engineering Applications.Tissue engineering. Part A · 2017Article
- Panels of chemically-modified heparin polysaccharides and natural heparan sulfate saccharides both exhibit differences in binding to Slit and Robo, as well as variation between protein binding and cellular activity.Molecular bioSystems · 2016Article
- Achieving high signal-to-noise in cell regulatory systems: Spatial organization of multiprotein transmembrane assemblies of FGFR and MET receptors.Progress in biophysics and molecular biology · 2015Review
- Structural insights into proteoglycan-shaped Hedgehog signaling.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Heparan sulfate-protein binding specificity.Biochemistry. Biokhimiia · 2013Review
- Emerging mass spectrometry-based approaches to probe protein-receptor interactions: focus on overcoming physiological barriers.Advanced drug delivery reviews · 2013Review
- Cooperative heparin-mediated oligomerization of fibroblast growth factor-1 (FGF1) precedes recruitment of FGFR2 to ternary complexes.Biophysical journal · 2013Article
- Multivalent proteoglycan modulation of FGF mitogenic responses in perivascular cells.Angiogenesis · 2013Article
- Adeno-associated viral vectors based on serotype 3b use components of the fibroblast growth factor receptor signaling complex for efficient transduction.Human gene therapy · 2012Article
- Simulation of Duty Cycle-Based Trapping and Ejection of Massive Ions Using Linear Digital Quadrupoles: the Enabling Technology for High Resolution Time-of-Flight Mass Spectrometry in the Ultra High Mass Range.International journal of mass spectrometry · 2011Article
- Highly sulfated nonreducing end-derived heparan sulfate domains bind fibroblast growth factor-2 with high affinity and are enriched in biologically active fractions.The Journal of biological chemistry · 2011Article
- Proteoglycan-specific molecular switch for RPTPσ clustering and neuronal extension.Science (New York, N.Y.) · 2011Article
- Basement membranes: cell scaffoldings and signaling platforms.Cold Spring Harbor perspectives in biology · 2011Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
The minimal signalling unit for tyrosine kinase receptors is two protomers dimerized by one or more ligands. However, it is clear that maximal signalling requires the formation of larger complexes of many receptors at discrete foci on the cell surface. The biological interactions that lead to this are likely to be diverse and have system specific components. In the present study, we demonstrate that, in the FGF (fibroblast growth factor)-FGFR (FGF receptor) system, multimers of the minimal complex composed of two FGF1 and two FGFR2 protomers can form on a single chain of the co-receptor heparin. Using size-exclusion chromatography, we show that two complexes can form on heparin chains as small as 16 saccharide units. We also show by MS that discrete complexes containing exactly two copies of the minimal signalling unit are formed. However, the doublet of complexes appears to be less co-operative than the formation of the 2:2:1 FGF1:FGFR2:heparin complex, suggesting that this mechanism is one of a number of weaker interactions that might be involved in the formation of a focal complex on the cell surface.
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Registered trials
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.