Lysenin: a sphingomyelin specific pore-forming toxin.
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Summary
Development of a non-toxic lysenin mutant revealed the spatial and functional heterogeneity of sphingolipid-rich membrane domains.
- Type
- review
- Published
- 2008-03-01
- Cited by
- 93
- References
- 52
- OpenAlex
- https://openalex.org/W2074021924
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:39277772
Keywords
Sphingomyelin, Sphingolipid, Ceramide, Sphingosine, Cell biology
References
- Glycolipid receptors for verotoxin and Helicobacter pylori: role in pathology.
- Structure and Function of Sphingolipid- and Cholesterol-rich Membrane Rafts*
- Biology of lysenin, a protein in the coelomic fluid of the earthworm Eisenia foetida.
- Viruses budding from either the apical or the basolateral plasma membrane domain of MDCK cells have unique phospholipid compositions.
- Molecular cloning of cDNA for lysenin, a novel protein in the earthworm Eisenia foetida that causes contraction of rat vascular smooth muscle.
- Lysenin, a unique sphingomyelin‐binding protein
- Redistribution of phosphatidylethanolamine at the cleavage furrow of dividing cells during cytokinesis.
- Enzymes of sphingolipid metabolism: from modular to integrative signaling.
- Recognition of sphingomyelin by lysenin and lysenin-related proteins.
- Lipid rafts: new tools and a new component.
- Effects of lipid composition on membrane permeabilization by sticholysin I and II, two cytolysins of the sea anemone Stichodactyla helianthus.
- Properties of a toxin from the sea anemone Stoichacis helianthus, including specific binding to sphingomyelin.
- Pleurotolysin, a Novel Sphingomyelin-specific Two-component Cytolysin from the Edible Mushroom Pleurotus ostreatus, Assembles into a Transmembrane Pore Complex*
- Biogenesis of cell-surface polarity in epithelial cells and neurons.
- Lipid rafts: contentious only from simplistic standpoints
- Interaction of the pore-forming protein equinatoxin II with model lipid membranes: A calorimetric and spectroscopic study.
- Vibrio cholerae cytolysin: assembly and membrane insertion of the oligomeric pore are tightly linked and are not detectably restricted by membrane fluidity.
- Biochemical characteristics of Eiseniapore, a pore-forming protein in the coelomic fluid of earthworms.
- Enzymes of Sphingolipid metabolism in Drosophila melanogaster
- A mouse B16 melanoma mutant deficient in glycolipids.
Cited by
- Imaging lipid membrane domains with lipid-specific probes.
- Pierisins and CARP-1: ADP-ribosylation of DNA by ARTCs in butterflies and shellfish.
- Endogenous ADP-Ribosylation
- Mass spectrometry coupled to imaging techniques: the better the view the greater the challenge
- Engineered Nanoparticles Mimicking Cell Membranes for Toxin Neutralization
- Pore formation: an ancient yet complex form of attack.
- Structure and assembly of pore-forming proteins.
- Revising lysenin expression of earthworm coelomocytes.
- Real-time visualization of assembling of a sphingomyelin-specific toxin on planar lipid membranes.
- Relationship between Localization on Cellular Membranes and Cytotoxicity of Vibrio vulnificus Hemolysin
- Cytolytic T cells induce ceramide-rich platforms in target cell membranes to initiate graft-versus-host disease.
- Imaging local sphingomyelin-rich domains in the plasma membrane using specific probes and advanced microscopy.
- Potential analytical applications of lysenin channels for detection of multivalent ions
- Earthworm-Derived Pore-Forming Toxin Lysenin and Screening of Its Inhibitors
- Sphingolipid and Glycosphingolipid Metabolic Pathways in the Era of Sphingolipidomics
- High-speed atomic force microscopy tracks toxin action.
- The ATP-binding cassette transporter-2 (ABCA2) regulates esterification of plasma membrane cholesterol by modulation of sphingolipid metabolism
- Lipids in host–pathogen interactions: Pathogens exploit the complexity of the host cell lipidome
- Cationic Polymers Inhibit the Conductance of Lysenin Channels
- Survey of the year 2008: applications of isothermal titration calorimetry
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