Evidence map›Paper›PMID 28117447›Full record

ArticleNature2017

Force interacts with macromolecular structure in activation of TGF-β.

Xianchi Dong, Bo Zhao, Roxana E Iacob, Jianghai Zhu, Adem C Koksal, Chafen Lu, John R Engen, Timothy A Springer

Open access · greenAbstract read
In one paragraph

Article in Nature, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 177 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
177citing papers in PubMed, 1 pooled it
17.2field-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

177 citing papers in PubMed, 1 synthesis or guideline pooled it, 283 citations in OpenAlex.

  1. Pooled it
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  12. PET/CT imaging of esophageal cancer targeting tumor cell specific αvβ6-integrin expression.European journal of nuclear medicine and molecular imaging · 2025
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  13. Review
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  15. Integrin αvβ6-Targeted PET/CT Imaging of Non-Small Cell Lung Cancer with [Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Observational
  16. Review
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117 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 3 institutions in 1 country.

Xianchi DongChildren's Hospital Boston and Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115, USA.
Bo ZhaoChildren's Hospital Boston and Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115, USA.
Roxana E IacobDepartment of Chemistry and Chemical Biology, Northeastern University, Boston, Massachusetts 02115, USA.
Jianghai ZhuChildren's Hospital Boston and Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115, USA.
Adem C KoksalChildren's Hospital Boston and Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115, USA.
Chafen LuChildren's Hospital Boston and Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115, USA.
John R EngenDepartment of Chemistry and Chemical Biology, Northeastern University, Boston, Massachusetts 02115, USA.
Timothy A SpringerChildren's Hospital Boston and Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115, USA.
Boston Children's Hospital · USHarvard University · USNortheastern University · US

Funding

TGF-beta latency and activationR01AR067288 · NIAMS · BOSTON CHILDREN'S HOSPITAL · PI SPRINGER, TIMOTHY A · 2015 to 2019
$1.9M
NIAMS NIH HHS R01 AR067288
6 · The paper itself

Abstract

Integrins are adhesion receptors that transmit force across the plasma membrane between extracellular ligands and the actin cytoskeleton. In activation of the transforming growth factor-β1 precursor (pro-TGF-β1), integrins bind to the prodomain, apply force, and release the TGF-β growth factor. However, we know little about how integrins bind macromolecular ligands in the extracellular matrix or transmit force to them. Here we show how integrin α

Indexed as

Amino Acid SequenceAntigens, NeoplasmBinding SitesCrystallography, X-RayEvolution, MolecularHumansIntegrinsModels, MolecularProtein BindingProtein ConformationTransforming Growth Factor beta1Antigens, Neoplasmintegrin alphavbeta6IntegrinsTransforming Growth Factor beta1

Identifiers

PMID28117447
PMCPMC5586147
OpenAlexW2582355481

What OpenQuestion holds

Textmetadata
LicenceTDM
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.