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We began analyzing https://link.springer.com/article/10.1007/s12551-018-0448-x, but it redirected us to https://link.springer.com/article/10.1007/s12551-018-0448-x. The analysis below is for the second page.

Title[redir]:
Cholesterol-dependent cytolysins: from water-soluble state to membrane pore | Biophysical Reviews
Description:
The cholesterol-dependent cytolysins (CDCs) are a family of bacterial toxins that are important virulence factors for a number of pathogenic Gram-positive bacterial species. CDCs are secreted as soluble, stable monomeric proteins that bind specifically to cholesterol-rich cell membranes, where they assemble into well-defined ring-shaped complexes of around 40 monomers. The complex then undergoes a concerted structural change, driving a large pore through the membrane, potentially lysing the target cell. Understanding the details of this process as the protein transitions from a discrete monomer to a complex, membrane-spanning protein machine is an ongoing challenge. While many of the details have been revealed, there are still questions that remain unanswered. In this review, we present an overview of some of the key features of the structure and function of the CDCs, including the structure of the secreted monomers, the process of interaction with target membranes, and the transition from bound monomers to complete pores. Future directions in CDC research and the potential of CDCs as research tools will also be discussed.

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Keywords {🔍}

pubmed, article, google, scholar, cas, central, membrane, pore, cholesteroldependent, tweten, structure, biol, cytolysin, parker, toxin, sci, pneumolysin, johnson, cytolysins, cell, research, cholesterol, formation, chem, hotze, bacterial, structural, crystal, nature, toxins, complex, reveals, binding, assembly, morton, protein, listeriolysin, mechanism, httpsdoiorgjbcm, proc, natl, acad, httpsdoiorgpnas, perfringolysin, poreforming, access, molecular, prepore, biochemistry, cytolytic,

Topics {✒️}

month download article/chapter bacterial cholesterol-dependent cytolysin cholesterol-sensitive membrane interactions cholesterol-dependent cytolysin visualized streptococcal cholesterol-dependent cytolysin cholesterol-dependent cytolysin undergo cholesterol-dependent cytolysin intermedilysin specific protein-membrane contacts nih grant r37-ai037657 pore-forming toxin intermedilysin membrane-pore-forming fragment major fret-detected rearrangement intersubunit beta-strand alignment beta-strand tilt angle membrane cholesterol topology—mode thiol-activated cytolysin cholesterol-dependent cytolysin secreted membrane-spanning protein machine cholesterol-dependent cytolysins pneumolysin defined ring-shaped complexes c8alpha-macpf reveals mechanism pre-pore complex beta-sheet transition identified full article pdf lipid membrane interactions cholesterol-dependent cytolysin protein/lipid complexes cholesterol-dependent cytolysins related subjects cholesterol-rich cell membranes pore-forming toxin pore forming toxin intermedilysin-receptor interactions complement-mediated lysis farrand aj pore-forming toxins orthogonal fluorescent sensors van pee human-specific cytolysin channel-forming toxins stable monomeric proteins bacterial toxin pneumolysin medical research council privacy choices/manage cookies pore-forming mechanism membrane-dependent conformational feil sc pore-forming steps pfo beta-barrel complement immune defense

Questions {❓}

Savinov SN, Heuck AP (2017) Interaction of cholesterol with Perfringolysin O: what have we learned from functional analysis?

Schema {🗺️}

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         description:The cholesterol-dependent cytolysins (CDCs) are a family of bacterial toxins that are important virulence factors for a number of pathogenic Gram-positive bacterial species. CDCs are secreted as soluble, stable monomeric proteins that bind specifically to cholesterol-rich cell membranes, where they assemble into well-defined ring-shaped complexes of around 40 monomers. The complex then undergoes a concerted structural change, driving a large pore through the membrane, potentially lysing the target cell. Understanding the details of this process as the protein transitions from a discrete monomer to a complex, membrane-spanning protein machine is an ongoing challenge. While many of the details have been revealed, there are still questions that remain unanswered. In this review, we present an overview of some of the key features of the structure and function of the CDCs, including the structure of the secreted monomers, the process of interaction with target membranes, and the transition from bound monomers to complete pores. Future directions in CDC research and the potential of CDCs as research tools will also be discussed.
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      description:The cholesterol-dependent cytolysins (CDCs) are a family of bacterial toxins that are important virulence factors for a number of pathogenic Gram-positive bacterial species. CDCs are secreted as soluble, stable monomeric proteins that bind specifically to cholesterol-rich cell membranes, where they assemble into well-defined ring-shaped complexes of around 40 monomers. The complex then undergoes a concerted structural change, driving a large pore through the membrane, potentially lysing the target cell. Understanding the details of this process as the protein transitions from a discrete monomer to a complex, membrane-spanning protein machine is an ongoing challenge. While many of the details have been revealed, there are still questions that remain unanswered. In this review, we present an overview of some of the key features of the structure and function of the CDCs, including the structure of the secreted monomers, the process of interaction with target membranes, and the transition from bound monomers to complete pores. Future directions in CDC research and the potential of CDCs as research tools will also be discussed.
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