ReviewThe Journal of membrane biology2020
Sequence Diversity in the Pore-Forming Motifs of the Membrane-Damaging Protein Toxins.
Review in The Journal of membrane biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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.
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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
10 citing papers in PubMed, 14 citations in OpenAlex.
- Bacterial pore-forming toxins: mechanisms and implications for host immunity.Bioscience reports · 2026Review
- Tke5 is a Pseudomonas putida toxin that kills plant pathogens by depolarising membranes.Communications biology · 2026Article
- Aerolysin-like proteins fromFrontiers in fungal biology · 2026Article
- Transcriptional Activation of a Pro-Inflammatory Response (NF-κB, AP-1, IL-1β) by theInternational journal of molecular sciences · 2023Article
- Membrane Dynamics and Remodelling in Response to the Action of the Membrane-Damaging Pore-Forming Toxins.The Journal of membrane biology · 2022Review
- A deep learning model to detect novel pore-forming proteins.Scientific reports · 2022Article
- Molecular Interplay at the Membrane and Impact on Cellular Physiology.The Journal of membrane biology · 2021Article
- Biological Nanopores: Engineering on Demand.Life (Basel, Switzerland) · 2021Review
- Curcumin Inhibits Membrane-Damaging Pore-Forming Function of the β-Barrel Pore-Forming ToxinFrontiers in microbiology · 2021Article
- Current Perspective on the Membrane-Damaging Action of Thermostable Direct Hemolysin, an Atypical Bacterial Pore-forming Toxin.Frontiers in molecular biosciences · 2021Review
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 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pore-forming proteins/toxins (PFPs/PFTs) are the distinct class of membrane-damaging proteins. They act by forming oligomeric pores in the plasma membranes. PFTs and PFPs from diverse organisms share a common mechanism of action, in which the designated pore-forming motifs of the membrane-bound protein molecules insert into the membrane lipid bilayer to create the water-filled pores. One common characteristic of these pore-forming motifs is that they are amphipathic in nature. In general, the hydrophobic sidechains of the pore-forming motifs face toward the hydrophobic core of the membranes, while the hydrophilic residues create the lining of the water-filled pore lumen. Interestingly, pore-forming motifs of the distinct subclass of PFPs/PFTs share very little sequence similarity with each other. Therefore, the common guiding principle that governs the sequence-to-structure paradigm in the mechanism of action of these PFPs/PFTs still remains an enigma. In this article, we discuss this notion using the examples of diverse groups of membrane-damaging PFPs/PFTs.
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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.