ArticleBiophysical journal2013
Real-time visualization of assembling of a sphingomyelin-specific toxin on planar lipid membranes.
Article in Biophysical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 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
24 citing papers in PubMed, 61 citations in OpenAlex.
- Structure and thermodynamics of supported lipid membranes on hydrophobic van der Waals surfaces.Soft matter · 2024Article
- HIV-1 Gag targeting to the plasma membrane reorganizes sphingomyelin-rich and cholesterol-rich lipid domains.Nature communications · 2023Article
- Modulation of Voltage-Gating and Hysteresis of Lysenin Channels by CuInternational journal of molecular sciences · 2023Article
- Visualizing the Domino-Like Prepore-to-Pore Transition of Streptolysin O by High-Speed AFM.The Journal of membrane biology · 2023Article
- Article
- Article
- Lysenin Channels as Sensors for Ions and Molecules.Sensors (Basel, Switzerland) · 2020Review
- Molecular and Functional Analysis of Pore-Forming Toxin Monalysin From Entomopathogenic BacteriumFrontiers in immunology · 2020Article
- Article
- Article
- Lysenin Toxin Membrane Insertion Is pH-Dependent but Independent of Neighboring Lysenins.Biophysical journal · 2017Article
- Molecular mechanism of pore formation by aerolysin-like proteins.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017Review
- Tuning membrane protein mobility by confinement into nanodomains.Nature nanotechnology · 2017Article
- Identification of a Membrane-bound Prepore Species Clarifies the Lytic Mechanism of Actinoporins.The Journal of biological chemistry · 2016Article
- Cryo-EM structure of aerolysin variants reveals a novel protein fold and the pore-formation process.Nature communications · 2016Article
- Crystal structure of an invertebrate cytolysin pore reveals unique properties and mechanism of assembly.Nature communications · 2016Article
- Red Blood Cell Susceptibility to Pneumolysin: CORRELATION WITH MEMBRANE BIOCHEMICAL AND PHYSICAL PROPERTIES.The Journal of biological chemistry · 2016Article
- Cryo-EM structure of lysenin pore elucidates membrane insertion by an aerolysin family protein.Nature communications · 2016Article
- Listeriolysin O Membrane Damaging Activity Involves Arc Formation and Lineaction -- Implication for Listeria monocytogenes Escape from Phagocytic Vacuole.PLoS pathogens · 2016Article
- Intramembrane congestion effects on lysenin channel voltage-induced gating.European biophysics journal : EBJ · 2016Article
Corrections and comments
- Commented on by
Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pore-forming toxins (PFTs) are soluble proteins that can oligomerize on the cell membrane and induce cell death by membrane insertion. PFT oligomers sometimes form hexagonal close-packed (hcp) structures on the membrane. Here, we show the assembling of the sphingomyelin (SM)-binding PFT, lysenin, into an hcp structure after oligomerization on SM/cholesterol membrane. This process was monitored by high-speed atomic force microscopy. Hcp assembly was driven by reorganization of lysenin oligomers such as association/dissociation and rapid diffusion along the membrane. Besides rapid association/dissociation of oligomers, the height change for some oligomers, possibly resulting from conformational changes in lysenin, could also be visualized. After the entire membrane surface was covered with a well-ordered oligomer lattice, the lysenin molecules were firmly bound on the membrane and the oligomers neither dissociated nor diffused. Our results reveal the dynamic nature of the oligomers of a lipid-binding toxin during the formation of an hcp structure. Visualization of this dynamic process is essential for the elucidation of the assembling mechanism of some PFTs that can form ordered structures on the membrane.
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.