Evidence map›Paper›PMID 31530856›Full record

ArticleScientific reports2019

A Bone Morphogenetic Protein (BMP)-derived Peptide Based on the Type I Receptor-binding Site Modifies Cell-type Dependent BMP Signalling.

Zhen Tong, Jingxu Guo, Robert C Glen, Nicholas W Morrell, Wei Li

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed, 2 pooled it
1.3field-weighted citation impact, top 20% 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

16 citing papers in PubMed, 2 syntheses or guidelines pooled it, 27 citations in OpenAlex.

  1. Pooled it
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  6. Cardiac preservation usingFrontiers in cardiovascular medicine · 2025
    Article
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  15. Advances in Growth Factor Delivery for Bone Tissue Engineering.International journal of molecular sciences · 2021
    Review
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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

5 authors at 1 institution in 2 countries.

Zhen TongThe Department of Medicine, University of Cambridge School of Clinical Medicine, Cambridge, CB2 0QQ, United Kingdom.
Jingxu GuoThe Department of Medicine, University of Cambridge School of Clinical Medicine, Cambridge, CB2 0QQ, United Kingdom.
Robert C GlenCentre for Molecular Informatics, Department of Chemistry, University of Cambridge, Cambridge, CB2 1EW, United Kingdom.
Nicholas W MorrellThe Department of Medicine, University of Cambridge School of Clinical Medicine, Cambridge, CB2 0QQ, United Kingdom.
Wei LiThe Department of Medicine, University of Cambridge School of Clinical Medicine, Cambridge, CB2 0QQ, United Kingdom. wl225@cam.ac.uk.ORCID http://orcid.org/0000-0002-1924-3120
University of Cambridge · GB

Funding

British Heart Foundation PG/12/54/29734British Heart Foundation PG/15/39/31519British Heart Foundation PG/17/1/32532British Heart Foundation (BHF) PG/17/1/32532Medical Research Council MR/K020919/1
6 · The paper itself

Abstract

Bone morphogenetic proteins (BMPs) are multifunctional cytokines of the transforming growth factor β (TGFβ) superfamily with potential therapeutic applications due to their broad biological functionality. Designing BMP mimetics with specific activity will contribute to the translational potential of BMP-based therapies. Here, we report a BMP9 peptide mimetic, P3, designed from the type I receptor binding site, which showed millimolar binding affinities for the type I receptor activin receptor like kinase 1 (ALK1), ALK2 and ALK3. Although showing no baseline activity, P3 significantly enhanced BMP9-induced Smad1/5 phosphorylation as well as ID1, BMPR2, HEY1 and HEY2 gene expression in pulmonary artery endothelial cells (hPAECs), and this activity is dependent on its alpha helix propensity. However, in human dermal microvascular endothelial cells, P3 did not affect BMP9-induced Smad1/5 phosphorylation, but potently inhibited ALK3-dependent BMP4-induced Smad1/5 phosphorylation and gene expression. In C2C12 mouse myoblast cells, P3 had no effect on BMP9-induced osteogenic signalling, which is primarily mediated by ALK2. Interestingly, a previously published peptide from the knuckle region of BMP9 was found to inhibit BMP4-induced Smad1/5 phosphorylation. Together, our data identify a BMP9-derived peptide that can selectively enhance ALK1-mediated BMP9 signalling in hPAECs and modulate BMP9 and BMP4 signalling in a cell type-specific manner.

Indexed as

Activin Receptors, Type IIAnimalsBinding SitesBone Morphogenetic ProteinsCell LineEndothelial CellsGrowth Differentiation Factor 2HumansMiceMolecular MimicryPeptidesPhosphorylationSignal TransductionSmad1 ProteinSmad8 ProteinStructure-Activity RelationshipActivin Receptors, Type IIACVRL1 protein, humanBone Morphogenetic ProteinsGDF2 protein, humanGrowth Differentiation Factor 2PeptidesSmad1 ProteinSMAD1 protein, humanSmad8 ProteinSMAD9 protein, human

Identifiers

PMID31530856
PMCPMC6748948
OpenAlexW2970245540

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

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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.