Evidence map›Paper›PMID 32484440›Full record

ArticleeLife2020

Shear stress activates ADAM10 sheddase to regulate Notch1 via the Piezo1 force sensor in endothelial cells.

Vincenza Caolo, Marjolaine Debant, Naima Endesh, T Simon Futers, Laeticia Lichtenstein, Fiona Bartoli, Gregory Parsonage, Elizabeth Av Jones, David J Beech

Open access · goldAbstract read
In one paragraph

Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
5.8field-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

61 citing papers in PubMed, 85 citations in OpenAlex.

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  13. Understanding the Lymphatic System: Tissue-on-Chip Modeling.Annual review of biomedical engineering · 2025
    Review
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  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Pharmacology of PIEZO1 channels.British journal of pharmacology · 2024
    Review

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 2 institutions in 2 countries.

Vincenza Caolo *Leeds Institute of Cardiovascular and Metabolic Medicine, School of Medicine, University of Leeds, Leeds, United Kingdom.ORCID 0000-0001-6215-2702
Marjolaine Debant *Leeds Institute of Cardiovascular and Metabolic Medicine, School of Medicine, University of Leeds, Leeds, United Kingdom.ORCID 0000-0001-5988-3395
Naima EndeshLeeds Institute of Cardiovascular and Metabolic Medicine, School of Medicine, University of Leeds, Leeds, United Kingdom.
T Simon FutersLeeds Institute of Cardiovascular and Metabolic Medicine, School of Medicine, University of Leeds, Leeds, United Kingdom.
Laeticia LichtensteinLeeds Institute of Cardiovascular and Metabolic Medicine, School of Medicine, University of Leeds, Leeds, United Kingdom.ORCID 0000-0003-3900-786X
Fiona BartoliLeeds Institute of Cardiovascular and Metabolic Medicine, School of Medicine, University of Leeds, Leeds, United Kingdom.
Gregory ParsonageLeeds Institute of Cardiovascular and Metabolic Medicine, School of Medicine, University of Leeds, Leeds, United Kingdom.
Elizabeth Av JonesDepartment of Cardiovascular Sciences, Centre for Molecular and Vascular Biology, Leuven, Belgium.
David J BeechLeeds Institute of Cardiovascular and Metabolic Medicine, School of Medicine, University of Leeds, Leeds, United Kingdom.ORCID 0000-0002-7683-9422
University of Leeds · GBVIB-KU Leuven Center for Cancer Biology · BE

Funding

British Heart Foundation RG/17/11/33042Wellcome Trust
6 · The paper itself

Abstract

Mechanical force is a determinant of Notch signalling but the mechanism of force detection and its coupling to Notch are unclear. We propose a role for Piezo1 channels, which are mechanically-activated non-selective cation channels. In cultured microvascular endothelial cells, Piezo1 channel activation by either shear stress or a chemical agonist Yoda1 activated a disintegrin and metalloproteinase domain-containing protein 10 (ADAM10), a Ca

Indexed as

ADAM10 ProteinAmyloid Precursor Protein SecretasesAnimalsCells, CulturedEndothelial CellsEnzyme ActivationGene Expression RegulationHumansIon ChannelsMaleMembrane ProteinsMiceMice, Inbred C57BLProtein DomainsReceptor, Notch1Stress, MechanicalADAM10 ProteinAdam10 protein, mouseAmyloid Precursor Protein SecretasesHes1 protein, mouseIon ChannelsMembrane ProteinsNotch1 protein, mousePiezo1 protein, mouseReceptor, Notch1Transcription Factor HES-1cell biologyendothelial cellhumanion channelmousenotch signallingproteinase

Identifiers

PMID32484440
PMCPMC7295575
OpenAlexW3030086170

What OpenQuestion holds

Textmetadata
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.