In one paragraphArticle in bioRxiv : the preprint server for biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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 registryThe 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 literatureWho cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
4 · The recordCorrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
5 · Who and what moneyAuthors and funding
17 authors.
Mia I Zol-HanlonSignalling and Structural Biology Laboratory, The Francis Crick Institute, 1 Midland Road, London, NW1 1AT, United Kingdom.ORCID 0000-0001-7262-6756 Beatrice RixSignalling and Structural Biology Laboratory, The Francis Crick Institute, 1 Midland Road, London, NW1 1AT, United Kingdom.ORCID 0000-0001-6205-8396 Salomé Bodet-LefèvreSignalling and Structural Biology Laboratory, The Francis Crick Institute, 1 Midland Road, London, NW1 1AT, United Kingdom.ORCID 0000-0001-5135-1626 Miguel Zamora-PorrasSignalling and Structural Biology Laboratory, The Francis Crick Institute, 1 Midland Road, London, NW1 1AT, United Kingdom.ORCID 0000-0003-3888-0253 David C BriggsSignalling and Structural Biology Laboratory, The Francis Crick Institute, 1 Midland Road, London, NW1 1AT, United Kingdom.ORCID 0000-0002-9793-7339 Andrea NansStructural Biology Science Technology Platform, The Francis Crick Institute, 1 Midland Road, London, NW1 1AT, United Kingdom.ORCID 0000-0002-3791-2447 Annabel C BorgStructural Biology Science Technology Platform, The Francis Crick Institute, 1 Midland Road, London, NW1 1AT, United Kingdom.ORCID 0000-0003-2873-7226 Sarah L MaslenProteomics Science Technology Platform, The Francis Crick Institute, 1 Midland Road, London, NW1 1AT, United Kingdom.
Antonio Di MaioGlycosciences Laboratory, Department of Metabolism, Digestion and Reproduction, Faculty of Medicine, Imperial College London, London, United Kingdom.ORCID 0000-0002-2740-9098 Ten FeiziGlycosciences Laboratory, Department of Metabolism, Digestion and Reproduction, Faculty of Medicine, Imperial College London, London, United Kingdom.ORCID 0000-0001-6495-0329 Yan LiuGlycosciences Laboratory, Department of Metabolism, Digestion and Reproduction, Faculty of Medicine, Imperial College London, London, United Kingdom.ORCID 0000-0002-2566-6867 Jelizaveta PavljukThe School of Biomedical Sciences, Faculty of Biological Sciences, School of Physics and Astronomy, Faculty of Engineering and Physical Sciences, Astbur Centre for Structural Molecular Biology, and Bragg Centre for Materials Researcher, University of Leeds, Leeds, LS2 9JT, UK.
Ralf P RichterThe School of Biomedical Sciences, Faculty of Biological Sciences, School of Physics and Astronomy, Faculty of Engineering and Physical Sciences, Astbur Centre for Structural Molecular Biology, and Bragg Centre for Materials Researcher, University of Leeds, Leeds, LS2 9JT, UK.ORCID 0000-0003-3071-2837 Benjamin SchumannFaculty of Chemistry and Food Chemistry, TUD Dresden University of Technology, Dresden, Germany.ORCID 0000-0001-5504-0147 Neil Q McDonaldSignalling and Structural Biology Laboratory, The Francis Crick Institute, 1 Midland Road, London, NW1 1AT, United Kingdom.ORCID 0000-0003-0975-6325 Funding
3-O-sulfation of heparan sulfate as a regular of protein functionR01HL151617 · NHLBI · UNIVERSITY OF GEORGIA · PI BOONS, GEERT-JAN, MOREMEN, KELLEY W. · 2020 to 2023
$1.8MNHLBI NIH HHS R01 HL151617Wellcome Trust CC2068
6 · The paper itselfAbstract
The receptor tyrosine kinase RET is activated by GDNF and GFRα1 together as a bipartite ligand, driving receptor activation and signalling in developmental and neuroprotective contexts. Evidence from developmental and cell models has suggested that heparan sulfate (HS) functions as a fourth component in RET signalling by binding to GDNF, but the molecular details remain unclear. Here, we present the cryo-EM structure of the heterohexameric RET:GDNF:GFRα1 complex with a fully resolved heparin ligand, revealing an unexpected extended HS binding site spanning all three proteins. The architecture of the complex and binding mode of the HS chain in this complex enables the formation of a higher order 4:4:4 assembly bound to a single 30-saccharide HS chain which bridges two intimately bound complexes. This multi-protein interface selectively binds the highly sulfated domains of HS over other GAG classes, and is essential for RET activation
Identifiers
PMID42239124
PMCPMC13228243
What OpenQuestion holds
Textmetadata
LicenceCC BY
Read underepoch 390