Evidence map›Paper›PMID 26627714›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

Stonefish toxin defines an ancient branch of the perforin-like superfamily.

Andrew M Ellisdon, Cyril F Reboul, Santosh Panjikar, Kitmun Huynh, Christine A Oellig, Kelly L Winter, Michelle A Dunstone, Wayne C Hodgson, Jamie Seymour, Peter K Dearden and 3 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
3.7field-weighted citation impact, top 7% 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

30 citing papers in PubMed, 67 citations in OpenAlex.

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  16. In-depth transcriptome reveals the potential biotechnological application ofThe journal of venomous animals and toxins including tropical diseases · 2020
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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 5 institutions in 3 countries.

Andrew M EllisdonBiomedicine Discovery Institute and Department of Biochemistry and Molecular Biology, Monash University, Melbourne, VIC, 3800, Australia; Australian Research Council Centre of Excellence in Advanced Molecular Imaging, Monash University, Melbourne, VIC, 3800, Australia;
Cyril F ReboulBiomedicine Discovery Institute and Department of Biochemistry and Molecular Biology, Monash University, Melbourne, VIC, 3800, Australia; Australian Research Council Centre of Excellence in Advanced Molecular Imaging, Monash University, Melbourne, VIC, 3800, Australia;
Santosh PanjikarBiomedicine Discovery Institute and Department of Biochemistry and Molecular Biology, Monash University, Melbourne, VIC, 3800, Australia; Australian Synchrotron, Macromolecular Crystallography, Melbourne, VIC, 3168, Australia;ORCID http://orcid.org/0000-0001-7429-3879
Kitmun HuynhBiomedicine Discovery Institute and Department of Biochemistry and Molecular Biology, Monash University, Melbourne, VIC, 3800, Australia;
Christine A OelligBiomedicine Discovery Institute and Department of Biochemistry and Molecular Biology, Monash University, Melbourne, VIC, 3800, Australia;
Kelly L WinterBiomedicine Discovery Institute and Department of Biochemistry and Molecular Biology, Monash University, Melbourne, VIC, 3800, Australia; Biomedicine Discovery Institute and Department of Pharmacology, Monash University, Melbourne, VIC, 3800, Australia;
Michelle A DunstoneBiomedicine Discovery Institute and Department of Biochemistry and Molecular Biology, Monash University, Melbourne, VIC, 3800, Australia; Australian Research Council Centre of Excellence in Advanced Molecular Imaging, Monash University, Melbourne, VIC, 3800, Australia; Biomedicine Discovery Institute and Department of Microbiology, Monash University, Melbourne, VIC, 3800, Australia;ORCID http://orcid.org/0000-0002-6026-648X
Wayne C HodgsonBiomedicine Discovery Institute and Department of Pharmacology, Monash University, Melbourne, VIC, 3800, Australia;
Jamie SeymourCentre for Biodiscovery and Molecular Development of Therapeutics, Australian Institute of Tropical Health and Medicine, James Cook University, Cairns, QLD, 4870, Australia;
Peter K DeardenDepartment of Biochemistry and Genetics Otago, University of Otago, Dunedin, 9054 Aotearoa-New Zealand;
Rodney K TwetenDepartment of Microbiology and Immunology, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104.
James C WhisstockBiomedicine Discovery Institute and Department of Biochemistry and Molecular Biology, Monash University, Melbourne, VIC, 3800, Australia; Australian Research Council Centre of Excellence in Advanced Molecular Imaging, Monash University, Melbourne, VIC, 3800, Australia; James.Whisstock@monash.edu sheena.mcgowan@monash.edu.
Sheena McGowanBiomedicine Discovery Institute and Department of Microbiology, Monash University, Melbourne, VIC, 3800, Australia; James.Whisstock@monash.edu sheena.mcgowan@monash.edu.
Australian Regenerative Medicine Institute · AUAustralian Research Council · AUAustralian Institute of Tropical Health and Medicine · AUUniversity of Oklahoma Health Sciences Center · USUniversity of Otago · NZ

Funding

Pore Formation by Cholesterol Dependent CytolysinsR01AI037657 · NIAID · UNIVERSITY OF OKLAHOMA HLTH SCIENCES CTR · PI TWETEN, RODNEY K. · 1997 to 2015
$5.4M
NIAID NIH HHS 1R01 AI037657NIAID NIH HHS R01 AI037657
6 · The paper itself

Abstract

The lethal factor in stonefish venom is stonustoxin (SNTX), a heterodimeric cytolytic protein that induces cardiovascular collapse in humans and native predators. Here, using X-ray crystallography, we make the unexpected finding that SNTX is a pore-forming member of an ancient branch of the Membrane Attack Complex-Perforin/Cholesterol-Dependent Cytolysin (MACPF/CDC) superfamily. SNTX comprises two homologous subunits (α and β), each of which comprises an N-terminal pore-forming MACPF/CDC domain, a central focal adhesion-targeting domain, a thioredoxin domain, and a C-terminal tripartite motif family-like PRY SPla and the RYanodine Receptor immune recognition domain. Crucially, the structure reveals that the two MACPF domains are in complex with one another and arranged into a stable early prepore-like assembly. These data provide long sought after near-atomic resolution insights into how MACPF/CDC proteins assemble into prepores on the surface of membranes. Furthermore, our analyses reveal that SNTX-like MACPF/CDCs are distributed throughout eukaryotic life and play a broader, possibly immune-related function outside venom.

Indexed as

Amino Acid SequenceAnimalsCell MembraneCholesterolComplement Membrane Attack ComplexCrystallography, X-RayFish VenomsMicroscopy, Electron, TransmissionModels, MolecularMolecular Sequence DataPerforinPhylogenyProtein BindingProtein MultimerizationProtein Structure, SecondaryProtein Structure, TertiaryCholesterolComplement Membrane Attack ComplexFish VenomsPerforinProtein Subunitsstonustoxincytolysinperforinporestonefishtoxin

Identifiers

PMID26627714
PMCPMC4687532
OpenAlexW2188666803

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.