Evidence map›Paper›PMID 24469792›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Functional truncated membrane pores.

David Stoddart, Mariam Ayub, Lajos Höfler, Pinky Raychaudhuri, Jochen W Klingelhoefer, Giovanni Maglia, Andrew Heron, Hagan Bayley

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
–field-weighted citation impact
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

38 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Controlled assembly and sophisticated additive manufacturing of macroscopic droplets.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  7. Protein engineering: status report.Protein engineering, design & selection : PEDS · 2026
    Review
  8. Review
  9. Review
  10. Review
  11. Article
  12. Design and Assembly of Transmembrane Helix Barrel.The Journal of membrane biology · 2020
    Article
  13. Article
  14. Article
  15. Article
  16. Membrane perforation by the pore-forming toxin pneumolysin.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  17. Article
  18. Article
  19. Article
  20. 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.

David StoddartDepartment of Chemistry, University of Oxford, Oxford OX1 3TA, United Kingdom.
Mariam Ayub
Lajos Höfler
Pinky Raychaudhuri
Jochen W Klingelhoefer
Giovanni Maglia
Andrew Heron
Hagan Bayley

Funding

Single-Molecule DNA Sequencing with Engineered NanoporesR01HG003709 · NHGRI · SCRIPPS RESEARCH INSTITUTE, THE · PI GHADIRI, M. REZA · 2005 to 2017
$13.2M
Biotechnology and Biological Sciences Research CouncilNHGRI NIH HHS R01 HG003709
6 · The paper itself

Abstract

Membrane proteins are generally divided into two classes. Integral proteins span the lipid bilayer, and peripheral proteins are located at the membrane surface. Here, we provide evidence for membrane proteins of a third class that stabilize lipid pores, most probably as toroidal structures. We examined mutants of the staphylococcal α-hemolysin pore so severely truncated that the protein cannot span a bilayer. Nonetheless, the doughnut-like structures elicited well-defined transmembrane ionic currents by inducing pore formation in the underlying lipids. The formation of lipid pores, produced here by a structurally defined protein, is supported by the lipid and voltage dependences of pore formation, and by molecular dynamics simulations. We discuss the role of stabilized lipid pores in amyloid disease, the action of antimicrobial peptides, and the assembly of the membrane-attack complexes of the immune system.

Indexed as

Models, MolecularProtein ConformationBacterial ToxinsCell Membrane PermeabilityHemolysin ProteinsLipid BilayersMembrane ProteinsMolecular Dynamics SimulationMutagenesisPolymerase Chain ReactionBacterial ToxinsHemolysin ProteinsLipid BilayersMembrane Proteinsstaphylococcal alpha-toxinalpha-hemolysinbeta-barrellipid reorganizationnanopore

Identifiers

PMID24469792
PMCPMC3932856

What OpenQuestion holds

Textmetadata
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.