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Title:
Pore-forming toxins | Cellular and Molecular Life Sciences
Description:
Pore-forming toxins are widely distributed proteins which form lesions in biological membranes. In this review, bacterial pore-forming toxins are treated as a paradigm and discussed in terms of the structural principles on which they work. Then, a large family of bacterial toxins, the cholesterol-binding toxins, are analyzed in depth to provide an overview of the processes involved in pore formation. The ways in which the cholesterol-binding toxins (cholesterol-dependent cytolysins) interact with membranes and form pores, the structure of the monomeric soluble and oligomeric pore-forming states, and the effects of the toxin on membrane structure are discussed. By surveying the range of work which has been done on cholesterol-binding toxins, a working model is elaborated which reconciles two current, apparently diametrically opposed, models for their mechanism.
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article, toxins, poreforming, privacy, cookies, content, gilbert, membrane, oxford, information, publish, search, rjc, bacterial, access, data, log, journal, research, molecular, life, sciences, proteins, membranes, cholesterolbinding, pore, structure, discover, author, springer, optional, personal, parties, policy, find, track, cellular, published, cite, explore, form, biological, discussed, terms, structural, work, formation, cholesteroldependent, cytolysins, toxin,
Topics {✒️}
bacterial pore-forming toxins oligomeric pore-forming states pore-forming proteins pore-forming toxins cholesterol-dependent cytolysins understand membrane binding month download article/chapter biological membranes cholesterol-binding toxins bacterial toxins widely distributed proteins membrane structure privacy choices/manage cookies full article pdf water-soluble state molecular sciences european economic area scope submit manuscript apparently diametrically opposed related subjects henry wellcome building central chemistry laboratory south parks road author correspondence conditions privacy policy toxin accepting optional cookies article cellular main content log journal finder publish pore formation life sci article gilbert article log membranes article cite privacy policy personal data books a information optional cookies manage preferences check access instant access data protection essential cookies cookies skip subscription content similar content monomeric soluble
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headline:Pore-forming toxins
description: Pore-forming toxins are widely distributed proteins which form lesions in biological membranes. In this review, bacterial pore-forming toxins are treated as a paradigm and discussed in terms of the structural principles on which they work. Then, a large family of bacterial toxins, the cholesterol-binding toxins, are analyzed in depth to provide an overview of the processes involved in pore formation. The ways in which the cholesterol-binding toxins (cholesterol-dependent cytolysins) interact with membranes and form pores, the structure of the monomeric soluble and oligomeric pore-forming states, and the effects of the toxin on membrane structure are discussed. By surveying the range of work which has been done on cholesterol-binding toxins, a working model is elaborated which reconciles two current, apparently diametrically opposed, models for their mechanism.
datePublished:2002-05-01T00:00:00Z
dateModified:2002-05-01T00:00:00Z
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Pore-forming toxin
cholesterol binding
membrane structure and dynamics
cryo-electron microscopy
pneumolysin
perfringolysin
streptolysin.
Cell Biology
Biomedicine
general
Life Sciences
Biochemistry
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headline:Pore-forming toxins
description: Pore-forming toxins are widely distributed proteins which form lesions in biological membranes. In this review, bacterial pore-forming toxins are treated as a paradigm and discussed in terms of the structural principles on which they work. Then, a large family of bacterial toxins, the cholesterol-binding toxins, are analyzed in depth to provide an overview of the processes involved in pore formation. The ways in which the cholesterol-binding toxins (cholesterol-dependent cytolysins) interact with membranes and form pores, the structure of the monomeric soluble and oligomeric pore-forming states, and the effects of the toxin on membrane structure are discussed. By surveying the range of work which has been done on cholesterol-binding toxins, a working model is elaborated which reconciles two current, apparently diametrically opposed, models for their mechanism.
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Pore-forming toxin
cholesterol binding
membrane structure and dynamics
cryo-electron microscopy
pneumolysin
perfringolysin
streptolysin.
Cell Biology
Biomedicine
general
Life Sciences
Biochemistry
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