Evidence map›Paper›PMID 33582137›Full record

ArticleBiophysical journal2021

Modeling of full-length Piezo1 suggests importance of the proximal N-terminus for dome structure.

Jiehan Chong, Dario De Vecchis, Adam J Hyman, Oleksandr V Povstyan, Melanie J Ludlow, Jian Shi, David J Beech, Antreas C Kalli

Open access · hybridAbstract read
In one paragraph

Article in Biophysical journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

36 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. Lipid Regulation of Mechanosensitive Ion Channels.International journal of molecular sciences · 2026
    Review
  3. Review
  4. Review
  5. PIPProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Review
  7. Review
  8. Article
  9. Open biology · 2025
    Review
  10. Article
  11. Review
  12. Article
  13. Review
  14. Pharmacology of PIEZO1 channels.British journal of pharmacology · 2024
    Review
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Piezo1 ion channels are capable of conformational signaling.bioRxiv : the preprint server for biology · 2024
    Article
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 1 institution in 1 country.

Jiehan ChongLeeds Institute of Cardiovascular and Metabolic Medicine, School of Medicine, University of Leeds, Leeds, United Kingdom.
Dario De VecchisLeeds Institute of Cardiovascular and Metabolic Medicine, School of Medicine, University of Leeds, Leeds, United Kingdom.
Adam J HymanLeeds Institute of Cardiovascular and Metabolic Medicine, School of Medicine, University of Leeds, Leeds, United Kingdom.
Oleksandr V PovstyanLeeds Institute of Cardiovascular and Metabolic Medicine, School of Medicine, University of Leeds, Leeds, United Kingdom.
Melanie J LudlowLeeds Institute of Cardiovascular and Metabolic Medicine, School of Medicine, University of Leeds, Leeds, United Kingdom.
Jian ShiLeeds Institute of Cardiovascular and Metabolic Medicine, School of Medicine, University of Leeds, Leeds, United Kingdom.
David J BeechLeeds Institute of Cardiovascular and Metabolic Medicine, School of Medicine, University of Leeds, Leeds, United Kingdom. Electronic address: d.j.beech@leeds.ac.uk.
Antreas C KalliLeeds Institute of Cardiovascular and Metabolic Medicine, School of Medicine, University of Leeds, Leeds, United Kingdom; Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, United Kingdom. Electronic address: a.kalli@leeds.ac.uk.
University of Leeds · GB

Funding

Biotechnology and Biological Sciences Research Council 1360947British Heart Foundation FS/17/2/32559British Heart Foundation RG/17/11/33042Medical Research Council MR/R01745X/1Wellcome TrustWellcome Trust 110044/Z/15/ZWellcome Trust SBF002∖1031
6 · The paper itself

Abstract

Piezo1 forms a mechanically activated calcium-permeable nonselective cation channel that is functionally important in many cell types. Structural data exist for C-terminal regions, but we lack information about N-terminal regions and how the entire channel interacts with the lipid bilayer. Here, we use computational approaches to predict the three-dimensional structure of the full-length Piezo1 and simulate it in an asymmetric membrane. A number of novel insights are suggested by the model: 1) Piezo1 creates a trilobed dome in the membrane that extends beyond the radius of the protein, 2) Piezo1 changes the lipid environment in its vicinity via preferential interactions with cholesterol and phosphatidylinositol 4,5-bisphosphate (PIP

Indexed as

Ion ChannelsLipid BilayersCholesterolPhosphatidylinositolsCholesterolIon ChannelsLipid BilayersPhosphatidylinositols

Identifiers

PMID33582137
PMCPMC8105715
OpenAlexW3132100036

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.