Evidence map›Paper›PMID 28166206›Full record

ArticleNature nanotechnology2017

Real-time visualization of perforin nanopore assembly.

Carl Leung, Adrian W Hodel, Amelia J Brennan, Natalya Lukoyanova, Sharon Tran, Colin M House, Stephanie C Kondos, James C Whisstock, Michelle A Dunstone, Joseph A Trapani and 3 more

Abstract read
PubMed Publisher
In one paragraph

Article in Nature nanotechnology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
7.1field-weighted citation impact, top 2% 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

49 citing papers in PubMed, 116 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Triggered Assembly of a DNA-Based Membrane Channel.Journal of the American Chemical Society · 2022
    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

13 authors at 6 institutions in 2 countries.

Carl LeungLondon Centre for Nanotechnology, University College London, London WC1H 0AH, UK.
Adrian W HodelLondon Centre for Nanotechnology, University College London, London WC1H 0AH, UK.
Amelia J BrennanKiller Cell Biology Laboratory, Peter MacCallum Cancer Centre, East Melbourne, Victoria 3000, Australia.
Natalya LukoyanovaDepartment of Crystallography/Biological Sciences, Institute of Structural and Molecular Biology, Birkbeck College, London WC1E 7HX, UK.
Sharon TranKiller Cell Biology Laboratory, Peter MacCallum Cancer Centre, East Melbourne, Victoria 3000, Australia.
Colin M HouseCancer Cell Death Laboratory, Peter MacCallum Cancer Centre, East Melbourne, Victoria 3000, Australia.
Stephanie C KondosDepartment of Biochemistry and Molecular Biology, Monash University, Melbourne, Victoria 3800, Australia.
James C WhisstockDepartment of Biochemistry and Molecular Biology, Monash University, Melbourne, Victoria 3800, Australia.
Michelle A DunstoneDepartment of Biochemistry and Molecular Biology, Monash University, Melbourne, Victoria 3800, Australia.
Joseph A TrapaniCancer Cell Death Laboratory, Peter MacCallum Cancer Centre, East Melbourne, Victoria 3000, Australia.
Ilia VoskoboinikKiller Cell Biology Laboratory, Peter MacCallum Cancer Centre, East Melbourne, Victoria 3000, Australia.
Helen R SaibilDepartment of Crystallography/Biological Sciences, Institute of Structural and Molecular Biology, Birkbeck College, London WC1E 7HX, UK.
Bart W HoogenboomLondon Centre for Nanotechnology, University College London, London WC1H 0AH, UK.ORCID 0000-0002-8882-4324
London Centre for Nanotechnology · GBPeter MacCallum Cancer Centre · AUARC Centre of Excellence in Advanced Molecular Imaging · AUInstitute of Structural and Molecular Biology · GBThe University of Melbourne · AUMonash University · AU

Funding

Biotechnology and Biological Sciences Research Council BB/J005932/1
6 · The paper itself

Abstract

Perforin is a key protein of the vertebrate immune system. Secreted by cytotoxic lymphocytes as soluble monomers, perforin can self-assemble into oligomeric pores of 10-20 nm inner diameter in the membranes of virus-infected and cancerous cells. These large pores facilitate the entry of pro-apoptotic granzymes, thereby rapidly killing the target cell. To elucidate the pathways of perforin pore assembly, we carried out real-time atomic force microscopy and electron microscopy studies. Our experiments reveal that the pore assembly proceeds via a membrane-bound prepore intermediate state, typically consisting of up to approximately eight loosely but irreversibly assembled monomeric subunits. These short oligomers convert to more closely packed membrane nanopore assemblies, which can subsequently recruit additional prepore oligomers to grow the pore size.

Indexed as

Erythrocyte MembranePore Forming Cytotoxic ProteinsAnimalsMiceMicroscopy, Atomic ForceMicroscopy, ElectronNanoporesSheepperforin, mousePore Forming Cytotoxic Proteins

Identifiers

PMID28166206
OpenAlexW2584282544

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.