Evidence map›Paper›PMID 22347366›Full record

ArticlePloS one2012

Structural and functional insights into endoglin ligand recognition and binding.

Aaron Alt, Laura Miguel-Romero, Jordi Donderis, Mikel Aristorena, Francisco J Blanco, Adam Round, Vicente Rubio, Carmelo Bernabeu, Alberto Marina

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed, 1 pooled it
5.2field-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

61 citing papers in PubMed, 1 synthesis or guideline pooled it, 102 citations in OpenAlex.

  1. Pooled it
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  16. Regulation of Blood-Brain Barrier Transporters by Transforming Growth Factor-Drug metabolism and disposition: the biological fate of chemicals · 2022
    Article
  17. Review
  18. Review
  19. Article
  20. High Soluble Endoglin Levels Affect Aortic Vascular Function during Mice Aging.Journal of cardiovascular development and disease · 2021
    Article

1 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

9 authors at 6 institutions in 2 countries.

Aaron AltInstituto de Biomedicina de Valencia, Valencia, Spain.
Laura Miguel-Romero
Jordi Donderis
Mikel Aristorena
Francisco J Blanco
Adam Round
Vicente Rubio
Carmelo Bernabeu
Alberto Marina
Instituto de Biomedicina de Valencia · ESInstituto de Investigación de Enfermedades Raras · ESInstituto de Salud Carlos III · ESCentre for Biomedical Network Research on Rare Diseases · ESCentro de Investigaciones Biológicas Margarita Salas · ESEuropean Molecular Biology Laboratory · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Endoglin, a type I membrane glycoprotein expressed as a disulfide-linked homodimer on human vascular endothelial cells, is a component of the transforming growth factor (TGF)-β receptor complex and is implicated in a dominant vascular dysplasia known as hereditary hemorrhagic telangiectasia as well as in preeclampsia. It interacts with the type I TGF-β signaling receptor activin receptor-like kinase (ALK)1 and modulates cellular responses to Bone Morphogenetic Protein (BMP)-9 and BMP-10. Structurally, besides carrying a zona pellucida (ZP) domain, endoglin contains at its N-terminal extracellular region a domain of unknown function and without homology to any other known protein, therefore called the orphan domain (OD). In this study, we have determined the recognition and binding ability of full length ALK1, endoglin and constructs encompassing the OD to BMP-9 using combined methods, consisting of surface plasmon resonance and cellular assays. ALK1 and endoglin ectodomains bind, independently of their glycosylation state and without cooperativity, to different sites of BMP-9. The OD comprising residues 22 to 337 was identified among the present constructs as the minimal active endoglin domain needed for partner recognition. These studies also pinpointed to Cys350 as being responsible for the dimerization of endoglin. In contrast to the complete endoglin ectodomain, the OD is a monomer and its small angle X-ray scattering characterization revealed a compact conformation in solution into which a de novo model was fitted.

Indexed as

Antigens, CDBone Morphogenetic ProteinsEndoglinGrowth Differentiation Factor 2HumansLigandsProtein BindingProtein MultimerizationReceptors, Cell SurfaceAntigens, CDBMP10 protein, humanBMP8B protein, humanBone Morphogenetic ProteinsEndoglinENG protein, humanGrowth Differentiation Factor 2LigandsReceptors, Cell Surface

Identifiers

PMID22347366
PMCPMC3275592
OpenAlexW1997337705

What OpenQuestion holds

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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.