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  1. Analyzed Page
  2. Matching Content Categories
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  6. Keywords
  7. Topics
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We began analyzing https://www.nature.com/articles/nrmicro.2015.3, but it redirected us to https://www.nature.com/articles/nrmicro.2015.3. The analysis below is for the second page.

Title[redir]:
Pore-forming toxins: ancient, but never really out of fashion | Nature Reviews Microbiology
Description:
Pore-forming toxins (PFTs) are produced as virulence factors by many pathogenic bacteria. In this Review, Dal Peraro and van der Goot describe new mechanistic insights into the assembly of these toxins and their target specificity, and discuss recent therapeutic developments. Pore-forming toxins (PFTs) are virulence factors produced by many pathogenic bacteria and have long fascinated structural biologists, microbiologists and immunologists. Interestingly, pore-forming proteins with remarkably similar structures to PFTs are found in vertebrates and constitute part of their immune system. Recently, structural studies of several PFTs have provided important mechanistic insights into the metamorphosis of PFTs from soluble inactive monomers to cytolytic transmembrane assemblies. In this Review, we discuss the diverse pore architectures and membrane insertion mechanisms that have been revealed by these studies, and we consider how these features contribute to binding specificity for different membrane targets. Finally, we explore the potential of these structural insights to enable the development of novel therapeutic strategies that would prevent both the establishment of bacterial resistance and an excessive immune response.

Matching Content Categories {📚}

  • Education
  • Science
  • Business & Finance

Content Management System {📝}

What CMS is doi.org built with?

Custom-built

No common CMS systems were detected on Doi.org, and no known web development framework was identified.

Traffic Estimate {📈}

What is the average monthly size of doi.org audience?

🏙️ Massive Traffic: 50M - 100M visitors per month


Based on our best estimate, this website will receive around 80,479,999 visitors per month in the current month.

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How Does Doi.org Make Money? {💸}

We're unsure if the website is profiting.

Not every website is profit-driven; some are created to spread information or serve as an online presence. Websites can be made for many reasons. This could be one of them. Doi.org might be cashing in, but we can't detect the method they're using.

Keywords {🔍}

pubmed, google, scholar, cas, central, biol, poreforming, membrane, structure, toxin, toxins, pore, protein, cell, nature, mol, chem, mechanism, formation, structural, bacterial, cytolysin, plos, clostridium, proteins, microbiol, host, perfringens, sci, aureus, nat, van, goot, binding, assembly, cholesteroldependent, staphylococcus, crystal, article, cells, response, colicin, lipid, reveals, tweten, transmembrane, immune, insights, access, human,

Topics {✒️}

nature portfolio permissions reprints privacy policy low-resolution em data author information authors advertising pore-forming pre-stem loop α-helical pore-forming protein perforin-related protein pleurotolysin open biol social media clostridium perfringens ε-toxin staphylococcal γ-hemolysin reveals bacterial pore-forming toxin clostridium perfringens β-toxin data protection staphylococcus aureus α-toxin bacterial pore-forming toxins pore-forming bacterial toxins staphylococcus aureus α-hemolysin clostridium septicum α-toxin membrane-bound closed state personal data staphylococcal pore-forming toxins bacterial cholesterol-dependent cytolysin pore-forming toxins induces bicomponent pore-forming leucocidins ss-pore-forming toxin fascinating pore-forming toxin pore-forming toxin intermedilysin disparate pore-forming toxins clostridial pore-forming toxins versatile pore-forming toxins β-strand tilt angle intersubunit β-strand alignment truncated α-hemolysin pores solid-state nmr studies β-pore-forming toxins perfringens enterotoxin mutant thiol-activated cytolysin cholesterol-dependent cytolysin secreted cholesterol-dependent cytolysin intermedilysin membrane-pore-forming fragment 1 powerpoint slide 2 powerpoint slide 3 powerpoint slide 4 powerpoint slide β-sheet transition identified pore-forming toxin aerolysin δ-toxin pore formation

Schema {🗺️}

WebPage:
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         headline:Pore-forming toxins: ancient, but never really out of fashion
         description: Pore-forming toxins (PFTs) are produced as virulence factors by many pathogenic bacteria. In this Review, Dal Peraro and van der Goot describe new mechanistic insights into the assembly of these toxins and their target specificity, and discuss recent therapeutic developments. Pore-forming toxins (PFTs) are virulence factors produced by many pathogenic bacteria and have long fascinated structural biologists, microbiologists and immunologists. Interestingly, pore-forming proteins with remarkably similar structures to PFTs are found in vertebrates and constitute part of their immune system. Recently, structural studies of several PFTs have provided important mechanistic insights into the metamorphosis of PFTs from soluble inactive monomers to cytolytic transmembrane assemblies. In this Review, we discuss the diverse pore architectures and membrane insertion mechanisms that have been revealed by these studies, and we consider how these features contribute to binding specificity for different membrane targets. Finally, we explore the potential of these structural insights to enable the development of novel therapeutic strategies that would prevent both the establishment of bacterial resistance and an excessive immune response.
         datePublished:2015-12-07T00:00:00Z
         dateModified:2015-12-07T00:00:00Z
         pageStart:77
         pageEnd:92
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            Infectious Diseases
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      headline:Pore-forming toxins: ancient, but never really out of fashion
      description: Pore-forming toxins (PFTs) are produced as virulence factors by many pathogenic bacteria. In this Review, Dal Peraro and van der Goot describe new mechanistic insights into the assembly of these toxins and their target specificity, and discuss recent therapeutic developments. Pore-forming toxins (PFTs) are virulence factors produced by many pathogenic bacteria and have long fascinated structural biologists, microbiologists and immunologists. Interestingly, pore-forming proteins with remarkably similar structures to PFTs are found in vertebrates and constitute part of their immune system. Recently, structural studies of several PFTs have provided important mechanistic insights into the metamorphosis of PFTs from soluble inactive monomers to cytolytic transmembrane assemblies. In this Review, we discuss the diverse pore architectures and membrane insertion mechanisms that have been revealed by these studies, and we consider how these features contribute to binding specificity for different membrane targets. Finally, we explore the potential of these structural insights to enable the development of novel therapeutic strategies that would prevent both the establishment of bacterial resistance and an excessive immune response.
      datePublished:2015-12-07T00:00:00Z
      dateModified:2015-12-07T00:00:00Z
      pageStart:77
      pageEnd:92
      sameAs:https://doi.org/10.1038/nrmicro.2015.3
      keywords:
         Bacterial host response
         Bacterial pathogenesis
         Bacterial structural biology
         Bacterial toxins
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         general
         Microbiology
         Medical Microbiology
         Parasitology
         Infectious Diseases
         Virology
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Social Networks {👍}(1)

External Links {🔗}(779)

Analytics and Tracking {📊}

  • Google Tag Manager

Libraries {📚}

  • Prism.js
  • Zoom.js

Emails and Hosting {✉️}

Mail Servers:

  • mx.zoho.eu
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  • mx3.zoho.eu

Name Servers:

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  • zita.ns.cloudflare.com

CDN Services {📦}

  • Crossref

5.13s.