ReviewInternational journal of molecular sciences2023
Pore-Forming Proteins: From Pore Assembly to Structure by Quantitative Single-Molecule Imaging.
Review in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
16 citing papers in PubMed.
- Molecular mechanism of pore formation by Plasmodium Perforin-like Protein 2.Nature communications · 2026Article
- An in vivo fitness gene of Toxoplasma, MIC11, is essential for PLP1-mediated egress from host cells.Nature communications · 2026Article
- LIN-24 as a Molecular Switch: Dual Cytotoxic and Cytoprotective Roles of an Aerolysin-Like Protein in C. elegans.Journal of applied toxicology : JAT · 2026Review
- Bacterial pore-forming toxins: mechanisms and implications for host immunity.Bioscience reports · 2026Review
- Through the holes: the biotechnological potential of actinoporins (and other PFPs).Biophysical reviews · 2026Review
- Membrane Pore Formation by Peptides Studied by Fluorescence Techniques.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Lumen charge governs gated ion transport in β-barrel nanopores.Nature nanotechnology · 2026Article
- Optimizing Essential Oil Blends by Mixture Design Approaches for Enhanced Antimicrobial and Antioxidant Activity: A Review.Journal of food science · 2026Review
- Gasdermins: multifunctional effectors of membrane permeabilization across cellular compartments.The FEBS journal · 2025Review
- Disrupting membranes, controlling cell fate: the role of pore-forming proteins in cell death and therapy.Apoptosis : an international journal on programmed cell death · 2025Review
- A Biosensor Platform for Detecting the Dissipation of Transmembrane Gradients in Single Liposomes.Analytical chemistry · 2025Article
- Hexameric-Based Hierarchy in the Sizes of a Cytolysin Pore-Forming Complex.Biomolecules · 2025Article
- Vastly different energy landscapes of the membrane insertions of monomeric gasdermin D and A3.Communications chemistry · 2025Article
- Gasdermin D cysteine residues synergistically control its palmitoylation-mediated membrane targeting and assembly.The EMBO journal · 2024Article
- Cell-free expression with a quartz crystal microbalance enables rapid, dynamic, and label-free characterization of membrane-interacting proteins.Communications biology · 2024Article
- Structural basis for calcium-stimulating pore formation of Vibrio α-hemolysin.Nature communications · 2023Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Pore-forming proteins (PFPs) play a central role in many biological processes related to infection, immunity, cancer, and neurodegeneration. A common feature of PFPs is their ability to form pores that disrupt the membrane permeability barrier and ion homeostasis and generally induce cell death. Some PFPs are part of the genetically encoded machinery of eukaryotic cells that are activated against infection by pathogens or in physiological programs to carry out regulated cell death. PFPs organize into supramolecular transmembrane complexes that perforate membranes through a multistep process involving membrane insertion, protein oligomerization, and finally pore formation. However, the exact mechanism of pore formation varies from PFP to PFP, resulting in different pore structures with different functionalities. Here, we review recent insights into the molecular mechanisms by which PFPs permeabilize membranes and recent methodological advances in their characterization in artificial and cellular membranes. In particular, we focus on single-molecule imaging techniques as powerful tools to unravel the molecular mechanistic details of pore assembly that are often obscured by ensemble measurements, and to determine pore structure and functionality. Uncovering the mechanistic elements of pore formation is critical for understanding the physiological role of PFPs and developing therapeutic approaches.
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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 Socratic graph.