ReviewPhilosophical transactions of the Royal Society of London. Series B, Biological sciences2017
Molecular mechanism of pore formation by aerolysin-like proteins.
Review in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed.
- Bacterial pore-forming toxins: mechanisms and implications for host immunity.Bioscience reports · 2026Review
- Aerolysin-like proteins fromFrontiers in fungal biology · 2026Article
- A nut-and-bolt assembly of the bimodular large progenitor botulinum neurotoxin complex.Science advances · 2025Article
- Bacillibactin, a PotentialInternational journal of molecular sciences · 2025Article
- The structural features and immunological role of biomphalysins in the snail Biomphalaria glabrata.PLoS pathogens · 2025Article
- Novel Insights into the Therapeutic Effect of Amentoflavone AgainstInternational journal of molecular sciences · 2025Article
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- The epsilon toxin from Clostridium perfringens stimulates calcium-activated chloride channels, generating extracellular vesicles in Xenopus oocytes.Pharmacology research & perspectives · 2024Article
- Keratinocytes drive the epithelial hyperplasia key to sea lice resistance in coho salmon.BMC biology · 2024Article
- The Molecular Architecture and Mode of Action ofToxins · 2024Review
- Unconventional structure and mechanisms for membrane interaction and translocation of the NF-κB-targeting toxin AIP56.Nature communications · 2023Article
- Functional Diversity of Novel Lectins with Unique Structural Features in Marine Animals.Cells · 2023Review
- Evaluating Biofilm Inhibitory Potential in Fish Pathogen,Antibiotics (Basel, Switzerland) · 2023Article
- Expansion and Neofunctionalization of Actinoporin-like Genes in Mediterranean Mussel (Mytilus galloprovincialis).Genome biology and evolution · 2022Article
- The choanoflagellate pore-forming lectin SaroL-1 punches holes in cancer cells by targeting the tumor-related glycosphingolipid Gb3.Communications biology · 2022Article
- Article
- Lipid larceny: channelizing host lipids for establishing successful pathogenesis by bacteria.Virulence · 2021Review
- The Natterin Proteins Diversity: A Review on Phylogeny, Structure, and Immune Function.Toxins · 2021Review
- Identification, antibiotic resistance, and virulence profiling of Aeromonas and Pseudomonas species from wastewater and surface water.Environmental monitoring and assessment · 2021Article
- Article
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3 authors.
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Abstract
Aerolysin-like pore-forming proteins are an important family of proteins able to efficiently damage membranes of target cells by forming transmembrane pores. They are characterized by a unique domain organization and mechanism of action that involves extensive conformational rearrangements. Although structures of soluble forms of many different members of this family are well understood, the structures of pores and their mechanism of assembly have been described only recently. The pores are characterized by well-defined β-barrels, which are devoid of any vestibular regions commonly found in other protein pores. Many members of this family are bacterial toxins; therefore, structural details of their transmembrane pores, as well as the mechanism of pore formation, are an important base for future drug design. Stability of pores and other properties, such as specificity for some cell surface molecules, make this family of proteins a useful set of molecular tools for molecular recognition and sensing in cell biology.This article is part of the themed issue 'Membrane pores: from structure and assembly, to medicine and technology'.
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