ArticleeLife2018
Membrane insertion of α-xenorhabdolysin in near-atomic detail.
Article in eLife, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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.
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.
Who cites it
17 citing papers in PubMed.
- Cryo-EM structure of detergent-boundbioRxiv : the preprint server for biology · 2026Article
- Story of Pore-Forming Proteins from Deadly Disease-Causing Agents to Modern Applications with Evolutionary Significance.Molecular biotechnology · 2024Review
- Genome Sequence Analysis of NativeToxins · 2024Article
- A Genomic Island of Vibrio cholerae Encodes a Three-Component Cytotoxin with Monomer and Protomer Forms Structurally Similar to Alpha-Pore-Forming Toxins.Journal of bacteriology · 2022Article
- Article
- Accelerated 2D Classification With ISAC Using GPUs.Frontiers in molecular biosciences · 2022Article
- Challenges and approaches to studying pore-forming proteins.Biochemical Society transactions · 2021Review
- Molecular architecture of black widow spider neurotoxins.Nature communications · 2021Article
- A tripartite cytolytic toxin formed byProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Characterisation of a tripartite α-pore forming toxin from Serratia marcescens.Scientific reports · 2021Article
- Review
- The evolution of SPHIRE-crYOLO particle picking and its application in automated cryo-EM processing workflows.Communications biology · 2020Article
- Article
- Folding and Misfolding of Human Membrane Proteins in Health and Disease: From Single Molecules to Cellular Proteostasis.Chemical reviews · 2019Article
- Cryo-EM structures ofProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Article
- Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
Abstract
α-Xenorhabdolysins (Xax) are α-pore-forming toxins (α-PFT) that form 1-1.3 MDa large pore complexes to perforate the host cell membrane. PFTs are used by a variety of bacterial pathogens to attack host cells. Due to the lack of structural information, the molecular mechanism of action of Xax toxins is poorly understood. Here, we report the cryo-EM structure of the XaxAB pore complex from
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.