ArticleProtein science : a publication of the Protein Society2002
Oligomerization of acidic fibroblast growth factor is not a prerequisite for its cell proliferation activity.
Article in Protein science : a publication of the Protein Society, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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.
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
11 citing papers in PubMed, 30 citations in OpenAlex.
- Amyloidogenesis: What Do We Know So Far?International journal of molecular sciences · 2022Review
- Probing the role of proline -135 on the structure, stability, and cell proliferation activity of human acidic fibroblast growth factor.Archives of biochemistry and biophysics · 2018Article
- Effect of extension of the heparin binding pocket on the structure, stability, and cell proliferation activity of the human acidic fibroblast growth factor.Biochemistry and biophysics reports · 2018Article
- The heterohexameric complex structure, a component in the non-classical pathway for fibroblast growth factor 1 (FGF1) secretion.The Journal of biological chemistry · 2010Article
- Trichloroacetic acid-induced protein precipitation involves the reversible association of a stable partially structured intermediate.Protein science : a publication of the Protein Society · 2009Article
- Dimerization effect of sucrose octasulfate on rat FGF1.Acta crystallographica. Section F, Structural biology and crystallization communications · 2008Article
- A light scattering study of the interaction of fibroblast growth factor (FGF) with its receptor.Biophysical journal · 2008Article
- Backbone dynamics of a biologically active human FGF-1 monomer, complexed to a hexasaccharide heparin-analogue, by 15N NMR relaxation methods.Journal of biomolecular NMR · 2006Article
- 1H, (13)C and (15)N chemical shift assignments of the D2 domain of the fibroblast growth factor receptor.Journal of biomolecular NMR · 2004Article
- Structurally homologous all beta-barrel proteins adopt different mechanisms of folding.Biophysical journal · 2003Article
- Structural basis for activation of fibroblast growth factor signaling by sucrose octasulfate.Molecular and cellular biology · 2002Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
13 authors at 7 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Oligomerization of fibroblast growth factors (FGFs) induced on binding to heparin or heparan sulfate proteoglycan is considered to be crucial for receptor activation and initiation of biological responses. To gain insight into the mechanism of activation of the receptor by FGFs, in the present study we investigate the effect(s) of interaction of a heparin analog, sucrose octasulfate (SOS), on the structure, stability, and biological activities of a recombinant acidic FGF from Notophthalmus viridescens (nFGF-1). SOS is found to bind to nFGF-1 and significantly increase the thermodynamic stability of the protein. Using a variety of techniques such as size-exclusion chromatography, sedimentation velocity, and multidimensional nuclear magnetic resonance (NMR) spectroscopy, it is shown that binding of SOS to nFGF-1 retains the protein in its monomeric state. In its monomeric state (complexed to SOS), n-FGF-1 shows significant cell proliferation activity. (15)N and (1)H chemical shift perturbation and the intermolecular nuclear Overhauser effects (NOEs) between SOS and nFGF-1 reveal that the ligand binds to the dense, positively charged cluster located in the groove enclosed by beta-strands 10 and 11. In addition, molecular modeling based on the NOEs observed for the SOS-nFGF-1 complex, indicates that SOS and heparin share a common binding site on the protein. In conclusion, the results of the present study clearly show that heparin-induced oligomerization of nFGF-1 is not mandatory for its cell proliferation activity.
Indexed as
Identifiers
What OpenQuestion holds
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.