Evidence map›Paper›PMID 25938661›Full record

ArticleNature structural & molecular biology2015

Repulsive guidance molecule is a structural bridge between neogenin and bone morphogenetic protein.

Eleanor G Healey, Benjamin Bishop, Jonathan Elegheert, Christian H Bell, Sergi Padilla-Parra, Christian Siebold

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.

0numbers the graph read from it
0cells of the map it votes in
64citing papers in PubMed
5.9field-weighted citation impact, top 3% 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

64 citing papers in PubMed, 111 citations in OpenAlex.

  1. The neogenin-hemojuvelin axis in murine liver is crucial for hepcidin expression.American journal of physiology. Gastrointestinal and liver physiology · 2026
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  8. Agouti and BMP signaling drive a naturally occurring fate conversion of melanophores to leucophores in zebrafish.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  9. Cripto-1 acts as a molecular bridge linking nodal to ALK4 via distinct structural domains.Protein science : a publication of the Protein Society · 2025
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4 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Eleanor G HealeyDivision of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford, UK.
Benjamin BishopDivision of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford, UK.
Jonathan ElegheertDivision of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford, UK.
Christian H BellDivision of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford, UK.
Sergi Padilla-Parra1] Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford, UK. [2] Cellular Imaging Core, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford, UK.
Christian SieboldDivision of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford, UK.
Centre for Human Genetics · GBUniversity of Oxford · GB

Funding

Cancer Research UK 14414Cancer Research UK A14414Cancer Research UK C20724/A14414Wellcome TrustWellcome Trust 090532/Z/09/ZWellcome Trust 097301/Z/11/ZWellcome Trust 101584MA
6 · The paper itself

Abstract

Repulsive guidance molecules (RGMs) control crucial processes including cell motility, adhesion, immune-cell regulation and systemic iron metabolism. RGMs signal via the neogenin (NEO1) and the bone morphogenetic protein (BMP) pathways. Here, we report crystal structures of the N-terminal domains of all human RGM family members in complex with the BMP ligand BMP2, revealing a new protein fold and a conserved BMP-binding mode. Our structural and functional data suggest a pH-linked mechanism for RGM-activated BMP signaling and offer a rationale for RGM mutations causing juvenile hemochromatosis. We also determined the crystal structure of the ternary BMP2-RGM-NEO1 complex, which, along with solution scattering and live-cell super-resolution fluorescence microscopy, indicates BMP-induced clustering of the RGM-NEO1 complex. Our results show how RGM acts as the central hub that links BMP and NEO1 and physically connects these fundamental signaling pathways.

Indexed as

Protein MultimerizationBone Morphogenetic Protein 2Cell Adhesion Molecules, NeuronalCrystallography, X-RayHumansMembrane ProteinsModels, MolecularProtein BindingProtein ConformationBMP2 protein, humanBone Morphogenetic Protein 2Cell Adhesion Molecules, NeuronalMembrane Proteinsneogenin

Identifiers

PMID25938661
PMCPMC4456160
OpenAlexW2170758920

What OpenQuestion holds

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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.