Evidence map›Paper›PMID 28564608›Full record

ArticleCell reports2017

Structural Basis of the Human Endoglin-BMP9 Interaction: Insights into BMP Signaling and HHT1.

Takako Saito, Marcel Bokhove, Romina Croci, Sara Zamora-Caballero, Ling Han, Michelle Letarte, Daniele de Sanctis, Luca Jovine

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 96 papers.

0numbers the graph read from it
0cells of the map it votes in
96citing papers in PubMed
9.7field-weighted citation impact, top 1% 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

96 citing papers in PubMed, 151 citations in OpenAlex.

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  14. Prodomain processing controls BMP-10 bioactivity and targeting to fibrillin-1 in latent conformation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Article
  15. Cripto-1 acts as a molecular bridge linking nodal to ALK4 via distinct structural domains.Protein science : a publication of the Protein Society · 2025
    Article
  16. Hereditary haemorrhagic telangiectasia.Nature reviews. Disease primers · 2025
    Review
  17. Article
  18. Article
  19. Review
  20. Review

36 more citing papers are in PubMed but not listed here.

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

8 authors at 3 institutions in 4 countries.

Takako SaitoDepartment of Biosciences and Nutrition and Center for Innovative Medicine, Karolinska Institutet, Huddinge 14183, Sweden.
Marcel BokhoveDepartment of Biosciences and Nutrition and Center for Innovative Medicine, Karolinska Institutet, Huddinge 14183, Sweden.
Romina CrociDepartment of Biosciences and Nutrition and Center for Innovative Medicine, Karolinska Institutet, Huddinge 14183, Sweden.
Sara Zamora-CaballeroDepartment of Biosciences and Nutrition and Center for Innovative Medicine, Karolinska Institutet, Huddinge 14183, Sweden.
Ling HanDepartment of Biosciences and Nutrition and Center for Innovative Medicine, Karolinska Institutet, Huddinge 14183, Sweden.
Michelle LetarteMolecular Medicine, Hospital for Sick Children, Peter Gilgan Centre for Research and Learning, University of Toronto, Toronto, ON M5G 0A4, Canada; Department of Immunology, University of Toronto, Toronto, ON M5G 0A4, Canada.
Daniele de SanctisESRF-The European Synchrotron, Grenoble 38000, France.
Luca JovineDepartment of Biosciences and Nutrition and Center for Innovative Medicine, Karolinska Institutet, Huddinge 14183, Sweden. Electronic address: luca.jovine@ki.se.
Karolinska Institutet · SEEuropean Synchrotron Radiation Facility · FRUniversity of Toronto · CA

Funding

European Research Council 260759
6 · The paper itself

Abstract

Endoglin (ENG)/CD105 is an essential endothelial cell co-receptor of the transforming growth factor β (TGF-β) superfamily, mutated in hereditary hemorrhagic telangiectasia type 1 (HHT1) and involved in tumor angiogenesis and preeclampsia. Here, we present crystal structures of the ectodomain of human ENG and its complex with the ligand bone morphogenetic protein 9 (BMP9). BMP9 interacts with a hydrophobic surface of the N-terminal orphan domain of ENG, which adopts a new duplicated fold generated by circular permutation. The interface involves residues mutated in HHT1 and overlaps with the epitope of tumor-suppressing anti-ENG monoclonal TRC105. The structure of the C-terminal zona pellucida module suggests how two copies of ENG embrace homodimeric BMP9, whose binding is compatible with ligand recognition by type I but not type II receptors. These findings shed light on the molecular basis of the BMP signaling cascade, with implications for future therapeutic interventions in this fundamental pathway.

Indexed as

Signal TransductionActivin Receptors, Type IICrystallography, X-RayDisulfidesEndoglinGene DuplicationGrowth Differentiation Factor 2HumansHydrophobic and Hydrophilic InteractionsKineticsLigandsModels, MolecularProtein BindingProtein DomainsProtein MultimerizationProtein Structure, SecondaryActivin Receptors, Type IIACVRL1 protein, humanDisulfidesEndoglinGrowth Differentiation Factor 2Ligandsbone morphogenetic protein receptorscell surface receptorsendoglingrowth differentiation factor 2hereditary hemorrhagic telangiectasiaorphan domainprotein interaction domains and motifsTGF-β superfamily proteinsx-ray crystallographyzona pellucida domain

Identifiers

PMID28564608
PMCPMC5464963
OpenAlexW2619574793

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.