ArticleNature communications2016
Cryo-EM structure of aerolysin variants reveals a novel protein fold and the pore-formation process.
Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 94 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
94 citing papers in PubMed, 204 citations in OpenAlex.
- Label-Free Profiling of Immunoglobulin Isotypes Using Solid-State Nanopores.Small methods · 2026Article
- Sub-Nanomolar Detection and Discrimination of Microcystin Congeners Using Aerolysin Nanopores.ACS nano · 2026Article
- Epx4 Nanopore With Multiple Constrictions for Single-Molecule Identification.Small methods · 2026Article
- Article
- NanoporeDB: a structural resource of multimeric protein nanopores for single-molecule sensing.GigaScience · 2026Article
- Lumen charge governs gated ion transport in β-barrel nanopores.Nature nanotechnology · 2026Article
- ThemBio · 2025Article
- A Comprehensive Structural and Functional Analysis ofbioRxiv : the preprint server for biology · 2025Article
- Characterization of Aeromonas hydrophila isolated from freshwater fish with control trial.Scientific reports · 2025Article
- A nut-and-bolt assembly of the bimodular large progenitor botulinum neurotoxin complex.Science advances · 2025Article
- Pore Formation by Pore Forming Proteins in Lipid Membranes: Structural Insights Through Cryo-EM.The Journal of membrane biology · 2025Review
- Large-scale predictions of alternative protein conformations by AlphaFold2-based sequence association.Nature communications · 2025Article
- Eliminating the Interference of Neighboring Nucleobases in Aerolysin for Nanopore Sequencing.ACS sensors · 2025Article
- The structural features and immunological role of biomphalysins in the snail Biomphalaria glabrata.PLoS pathogens · 2025Article
- Probing Bacterial Interactions with theToxins · 2025Article
- Direct mapping of tyrosine sulfation states in native peptides by nanopore.Nature chemical biology · 2025Article
- Nanopore-Functionalized Hybrid Lipid-Block Copolymer Membranes Allow Efficient Single-Molecule Sampling and Stable Sensing of Human Serum.Advanced materials (Deerfield Beach, Fla.) · 2025Article
- Structural basis for the pore-forming activity of a complement-like toxin.Science advances · 2025Article
- Aerolysin Nanopore Structures Revealed at High Resolution in a Lipid Environment.Journal of the American Chemical Society · 2025Article
- Article
34 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Owing to their pathogenical role and unique ability to exist both as soluble proteins and transmembrane complexes, pore-forming toxins (PFTs) have been a focus of microbiologists and structural biologists for decades. PFTs are generally secreted as water-soluble monomers and subsequently bind the membrane of target cells. Then, they assemble into circular oligomers, which undergo conformational changes that allow membrane insertion leading to pore formation and potentially cell death. Aerolysin, produced by the human pathogen Aeromonas hydrophila, is the founding member of a major PFT family found throughout all kingdoms of life. We report cryo-electron microscopy structures of three conformational intermediates and of the final aerolysin pore, jointly providing insight into the conformational changes that allow pore formation. Moreover, the structures reveal a protein fold consisting of two concentric β-barrels, tightly kept together by hydrophobic interactions. This fold suggests a basis for the prion-like ultrastability of aerolysin pore and its stoichiometry.
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.