ArticleNature communications2015
Structural basis for self-assembly of a cytolytic pore lined by protein and lipid.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 101 papers.
What it found
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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.
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Who cites it
101 citing papers in PubMed, 232 citations in OpenAlex.
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- Structural and biochemical characterization of Grimontia hollisae thermostable direct hemolysin with DNA reveals first Vibrio hemolysin with nuclease activity.Nucleic acids research · 2026Article
- Bioinformatic and computational biophysics tools for nanopore engineering: a review from standard approaches to machine learning advancements.Journal of nanobiotechnology · 2026Review
- Article
- Through the holes: the biotechnological potential of actinoporins (and other PFPs).Biophysical reviews · 2026Review
- Senotoxins target senescence via lipid binding specificity, ion imbalance and lipidome remodeling.Nature aging · 2026Article
- Protein Design Meets Single-Molecule Detection: Towards Programmable Nanopore Sensors.International journal of molecular sciences · 2025Review
- Elucidating the structure and assembly mechanism of actinoporin pores in complex membrane environments.Science advances · 2025Article
- Pore Formation by Pore Forming Proteins in Lipid Membranes: Structural Insights Through Cryo-EM.The Journal of membrane biology · 2025Review
- Hetero-Oligomeric Protein Pores for Single-Molecule Sensing.The Journal of membrane biology · 2025Review
- Structural insights into pre-pore intermediates of alpha-hemolysin in the lipidic environment.Nature communications · 2025Article
- Large-scale predictions of alternative protein conformations by AlphaFold2-based sequence association.Nature communications · 2025Article
- The Biological Role of Conoporins, Actinoporin-like Pore-Forming Toxins from Cone Snails.Toxins · 2025Review
- Cryo-EM structures of a protein pore reveal a cluster of cholesterol molecules and diverse roles of membrane lipids.Nature communications · 2025Article
- Vectorial Discrimination of Small Molecules with a Macrocycle Adaptor-Protein Nanopore System and Nanocavity-Dependent, pH Gradient-Controlled Analyte Kinetics.Analytical chemistry · 2025Article
- Controlling DNA Fragments Translocation across Nanopores with the Synergic Use of Site-Directed Mutagenesis, pH-Dependent Charge Tuning, and Electroosmotic Flow.ACS applied materials & interfaces · 2024Article
- Story of Pore-Forming Proteins from Deadly Disease-Causing Agents to Modern Applications with Evolutionary Significance.Molecular biotechnology · 2024Review
- Nanopore-based glycan sequencing: state of the art and future prospects.Chemical science · 2024Review
- Visible Light Control over the Cytolytic Activity of a Toxic Pore-Forming Protein.ACS chemical biology · 2024Article
41 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
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pore-forming toxins (PFT) are water-soluble proteins that possess the remarkable ability to self-assemble on the membrane of target cells, where they form pores causing cell damage. Here, we elucidate the mechanism of action of the haemolytic protein fragaceatoxin C (FraC), a α-barrel PFT, by determining the crystal structures of FraC at four different stages of the lytic mechanism, namely the water-soluble state, the monomeric lipid-bound form, an assembly intermediate and the fully assembled transmembrane pore. The structure of the transmembrane pore exhibits a unique architecture composed of both protein and lipids, with some of the lipids lining the pore wall, acting as assembly cofactors. The pore also exhibits lateral fenestrations that expose the hydrophobic core of the membrane to the aqueous environment. The incorporation of lipids from the target membrane within the structure of the pore provides a membrane-specific trigger for the activation of a haemolytic toxin.
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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.