Evidence map›Paper›PMID 27030175›Full record

ArticleOpen biology2016

Heparin binding preference and structures in the fibroblast growth factor family parallel their evolutionary diversification.

Yong Li, Changye Sun, Edwin A Yates, Chao Jiang, Mark C Wilkinson, David G Fernig

Open access · goldAbstract read
In one paragraph

Article in Open biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
5.0field-weighted citation impact, top 4% 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

41 citing papers in PubMed, 69 citations in OpenAlex.

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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 2 institutions in 2 countries.

Yong LiDepartment of Biochemistry, Institute of Integrative Biology, University of Liverpool, Biosciences Building, Crown Street, Liverpool L69 7ZB, UK.ORCID http://orcid.org/0000-0002-5594-4434
Changye SunDepartment of Biochemistry, Institute of Integrative Biology, University of Liverpool, Biosciences Building, Crown Street, Liverpool L69 7ZB, UK.ORCID http://orcid.org/0000-0001-8602-9629
Edwin A YatesDepartment of Biochemistry, Institute of Integrative Biology, University of Liverpool, Biosciences Building, Crown Street, Liverpool L69 7ZB, UK.ORCID http://orcid.org/0000-0001-9365-5433
Chao JiangSchool of Pharmaceutical Science, Wenzhou Medical University, Chashan University Park, Wenzhou 325035, China.
Mark C WilkinsonDepartment of Biochemistry, Institute of Integrative Biology, University of Liverpool, Biosciences Building, Crown Street, Liverpool L69 7ZB, UK.
David G FernigDepartment of Biochemistry, Institute of Integrative Biology, University of Liverpool, Biosciences Building, Crown Street, Liverpool L69 7ZB, UK dgferning@liverpool.ac.uk.ORCID http://orcid.org/0000-0003-4875-4293
University of Liverpool · GBWenzhou Medical University · CN

Funding

Medical Research Council MR/K015931/1
6 · The paper itself

Abstract

The interaction of a large number of extracellular proteins with heparan sulfate (HS) regulates their transport and effector functions, but the degree of molecular specificity underlying protein-polysaccharide binding is still debated. The 15 paracrine fibroblast growth factors (FGFs) are one of the paradigms for this interaction. Here, we measure the binding preferences of six FGFs (FGF3, FGF4, FGF6, FGF10, FGF17, FGF20) for a library of modified heparins, representing structures in HS, and model glycosaminoglycans, using differential scanning fluorimetry. This is complemented by the identification of the lysine residues in the primary and secondary binding sites of the FGFs by a selective labelling approach. Pooling these data with previous sets provides good coverage of the FGF phylogenetic tree, deduced from amino acid sequence alignment. This demonstrates that the selectivity of the FGFs for binding structures in sulfated polysaccharides and the pattern of secondary binding sites on the surface of FGFs follow the phylogenetic relationship of the FGFs, and so are likely to be the result of the natural selection pressures that led to the expansion of the FGF family in the course of the evolution of more complex animal body plans.

Indexed as

Amino Acid SequenceAnimalsBinding SitesFibroblast Growth FactorsGlycosaminoglycansHeparan SulfateHumansModels, MolecularPhylogenyProtein BindingProtein ConformationProtein StabilityRecombinant ProteinsSequence AlignmentSwineFibroblast Growth FactorsGlycosaminoglycansHeparan SulfateRecombinant Proteinsfibroblast growth factorglycosaminoglycanheparan sulfateheparin binding sitemolecular recognitionspecificity

Identifiers

PMID27030175
PMCPMC4821243
OpenAlexW2327662987

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.