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LINK . SPRINGER . COM {}

  1. Analyzed Page
  2. Matching Content Categories
  3. CMS
  4. Monthly Traffic Estimate
  5. How Does Link.springer.com Make Money
  6. Keywords
  7. Topics
  8. Schema
  9. External Links
  10. Analytics And Tracking
  11. Libraries
  12. CDN Services

We are analyzing https://link.springer.com/article/10.1007/s00018-002-8471-1.

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.
Website Age:
28 years and 1 months (reg. 1997-05-29).

Matching Content Categories {📚}

  • Social Networks
  • Telecommunications
  • Science

Content Management System {📝}

What CMS is link.springer.com built with?

Custom-built

No common CMS systems were detected on Link.springer.com, and no known web development framework was identified.

Traffic Estimate {📈}

What is the average monthly size of link.springer.com audience?

🌠 Phenomenal Traffic: 5M - 10M visitors per month


Based on our best estimate, this website will receive around 5,000,019 visitors per month in the current month.
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How Does Link.springer.com Make Money? {💸}

We find it hard to spot revenue streams.

Websites don't always need to be profitable; some serve as platforms for education or personal expression. Websites can serve multiple purposes. And this might be one of them. Link.springer.com could be getting rich in stealth mode, or the way it's monetizing isn't detectable.

Keywords {🔍}

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

Schema {🗺️}

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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
         pageStart:832
         pageEnd:844
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            cholesterol binding
            membrane structure and dynamics
            cryo-electron microscopy
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            perfringolysin
            streptolysin.
            Cell Biology
            Biomedicine
            general
            Life Sciences
            Biochemistry
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               name:R.J.C. Gilbert
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                        name:Division of Structural Biology, Henry Wellcome Building for Genomic Medicine, University of Oxford, Oxford, United Kingdom
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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
      pageStart:832
      pageEnd:844
      sameAs:https://doi.org/10.1007/s00018-002-8471-1
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         cholesterol binding
         membrane structure and dynamics
         cryo-electron microscopy
         pneumolysin
         perfringolysin
         streptolysin.
         Cell Biology
         Biomedicine
         general
         Life Sciences
         Biochemistry
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External Links {🔗}(25)

Analytics and Tracking {📊}

  • Google Tag Manager

Libraries {📚}

  • Clipboard.js
  • Prism.js

CDN Services {📦}

  • Crossref

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