Here's how NATURE.COM makes money* and how much!

*Please read our disclaimer before using our estimates.
Loading...

NATURE . COM {}

  1. Analyzed Page
  2. Matching Content Categories
  3. CMS
  4. Monthly Traffic Estimate
  5. How Does Nature.com Make Money
  6. How Much Does Nature.com Make
  7. Keywords
  8. Topics
  9. Schema
  10. Social Networks
  11. External Links
  12. Analytics And Tracking
  13. Libraries
  14. Hosting Providers
  15. CDN Services

We are analyzing https://www.nature.com/articles/nrmicro.2015.3.

Title:
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.
Website Age:
30 years and 10 months (reg. 1994-08-11).

Matching Content Categories {📚}

  • Education
  • Science
  • Business & Finance

Content Management System {📝}

What CMS is nature.com built with?

Custom-built

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

Traffic Estimate {📈}

What is the average monthly size of nature.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.
However, some sources were not loaded, we suggest to reload the page to get complete results.

check SE Ranking
check Ahrefs
check Similarweb
check Ubersuggest
check Semrush

How Does Nature.com Make Money? {💸}


Display Ads {🎯}


The website utilizes display ads within its content to generate revenue. Check the next section for further revenue estimates.

Ads are managed by yourbow.com. Particular relationships are as follows:

Direct Advertisers (10)
google.com, pmc.com, doceree.com, yourbow.com, audienciad.com, onlinemediasolutions.com, advibe.media, aps.amazon.com, getmediamx.com, onomagic.com

Reseller Advertisers (38)
conversantmedia.com, rubiconproject.com, pubmatic.com, appnexus.com, openx.com, smartadserver.com, lijit.com, sharethrough.com, video.unrulymedia.com, google.com, yahoo.com, triplelift.com, onetag.com, sonobi.com, contextweb.com, 33across.com, indexexchange.com, media.net, themediagrid.com, adform.com, richaudience.com, sovrn.com, improvedigital.com, freewheel.tv, smaato.com, yieldmo.com, amxrtb.com, adyoulike.com, adpone.com, criteo.com, smilewanted.com, 152media.info, e-planning.net, smartyads.com, loopme.com, opera.com, mediafuse.com, betweendigital.com

How Much Does Nature.com Make? {💰}


Display Ads {🎯}

$63,100 per month
Our analysis indicates Nature.com generates between $42,042 and $115,616 monthly online from display ads.

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:
      mainEntity:
         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
            Life Sciences
            general
            Microbiology
            Medical Microbiology
            Parasitology
            Infectious Diseases
            Virology
         image:
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1038%2Fnrmicro.2015.3/MediaObjects/41579_2016_Article_BFnrmicro20153_Fig1_HTML.jpg
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1038%2Fnrmicro.2015.3/MediaObjects/41579_2016_Article_BFnrmicro20153_Figa_HTML.jpg
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1038%2Fnrmicro.2015.3/MediaObjects/41579_2016_Article_BFnrmicro20153_Fig2_HTML.jpg
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1038%2Fnrmicro.2015.3/MediaObjects/41579_2016_Article_BFnrmicro20153_Fig3_HTML.jpg
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1038%2Fnrmicro.2015.3/MediaObjects/41579_2016_Article_BFnrmicro20153_Fig4_HTML.jpg
         isPartOf:
            name:Nature Reviews Microbiology
            issn:
               1740-1534
               1740-1526
            volumeNumber:14
            type:
               Periodical
               PublicationVolume
         publisher:
            name:Nature Publishing Group UK
            logo:
               url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
               type:ImageObject
            type:Organization
         author:
               name:Matteo Dal Peraro
               affiliation:
                     name:Institute of Bioengineering, School of Life Sciences, Ecole Polytechnique Fédérale de Lausanne (EPFL)
                     address:
                        name:Institute of Bioengineering, School of Life Sciences, Ecole Polytechnique Fédérale de Lausanne (EPFL), Lausanne, Switzerland
                        type:PostalAddress
                     type:Organization
               email:[email protected]
               type:Person
               name:F. Gisou van der Goot
               affiliation:
                     name:Global Health Institute, School of Life Sciences, Ecole Polytechnique Fédérale de Lausanne (EPFL)
                     address:
                        name:Global Health Institute, School of Life Sciences, Ecole Polytechnique Fédérale de Lausanne (EPFL), Lausanne, Switzerland
                        type:PostalAddress
                     type:Organization
               email:[email protected]
               type:Person
         isAccessibleForFree:
         hasPart:
            isAccessibleForFree:
            cssSelector:.main-content
            type:WebPageElement
         type:ScholarlyArticle
      context:https://schema.org
ScholarlyArticle:
      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
         Life Sciences
         general
         Microbiology
         Medical Microbiology
         Parasitology
         Infectious Diseases
         Virology
      image:
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1038%2Fnrmicro.2015.3/MediaObjects/41579_2016_Article_BFnrmicro20153_Fig1_HTML.jpg
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1038%2Fnrmicro.2015.3/MediaObjects/41579_2016_Article_BFnrmicro20153_Figa_HTML.jpg
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1038%2Fnrmicro.2015.3/MediaObjects/41579_2016_Article_BFnrmicro20153_Fig2_HTML.jpg
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1038%2Fnrmicro.2015.3/MediaObjects/41579_2016_Article_BFnrmicro20153_Fig3_HTML.jpg
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1038%2Fnrmicro.2015.3/MediaObjects/41579_2016_Article_BFnrmicro20153_Fig4_HTML.jpg
      isPartOf:
         name:Nature Reviews Microbiology
         issn:
            1740-1534
            1740-1526
         volumeNumber:14
         type:
            Periodical
            PublicationVolume
      publisher:
         name:Nature Publishing Group UK
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:Matteo Dal Peraro
            affiliation:
                  name:Institute of Bioengineering, School of Life Sciences, Ecole Polytechnique Fédérale de Lausanne (EPFL)
                  address:
                     name:Institute of Bioengineering, School of Life Sciences, Ecole Polytechnique Fédérale de Lausanne (EPFL), Lausanne, Switzerland
                     type:PostalAddress
                  type:Organization
            email:[email protected]
            type:Person
            name:F. Gisou van der Goot
            affiliation:
                  name:Global Health Institute, School of Life Sciences, Ecole Polytechnique Fédérale de Lausanne (EPFL)
                  address:
                     name:Global Health Institute, School of Life Sciences, Ecole Polytechnique Fédérale de Lausanne (EPFL), Lausanne, Switzerland
                     type:PostalAddress
                  type:Organization
            email:[email protected]
            type:Person
      isAccessibleForFree:
      hasPart:
         isAccessibleForFree:
         cssSelector:.main-content
         type:WebPageElement
["Periodical","PublicationVolume"]:
      name:Nature Reviews Microbiology
      issn:
         1740-1534
         1740-1526
      volumeNumber:14
Organization:
      name:Nature Publishing Group UK
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:Institute of Bioengineering, School of Life Sciences, Ecole Polytechnique Fédérale de Lausanne (EPFL)
      address:
         name:Institute of Bioengineering, School of Life Sciences, Ecole Polytechnique Fédérale de Lausanne (EPFL), Lausanne, Switzerland
         type:PostalAddress
      name:Global Health Institute, School of Life Sciences, Ecole Polytechnique Fédérale de Lausanne (EPFL)
      address:
         name:Global Health Institute, School of Life Sciences, Ecole Polytechnique Fédérale de Lausanne (EPFL), Lausanne, Switzerland
         type:PostalAddress
ImageObject:
      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
Person:
      name:Matteo Dal Peraro
      affiliation:
            name:Institute of Bioengineering, School of Life Sciences, Ecole Polytechnique Fédérale de Lausanne (EPFL)
            address:
               name:Institute of Bioengineering, School of Life Sciences, Ecole Polytechnique Fédérale de Lausanne (EPFL), Lausanne, Switzerland
               type:PostalAddress
            type:Organization
      email:[email protected]
      name:F. Gisou van der Goot
      affiliation:
            name:Global Health Institute, School of Life Sciences, Ecole Polytechnique Fédérale de Lausanne (EPFL)
            address:
               name:Global Health Institute, School of Life Sciences, Ecole Polytechnique Fédérale de Lausanne (EPFL), Lausanne, Switzerland
               type:PostalAddress
            type:Organization
      email:[email protected]
PostalAddress:
      name:Institute of Bioengineering, School of Life Sciences, Ecole Polytechnique Fédérale de Lausanne (EPFL), Lausanne, Switzerland
      name:Global Health Institute, School of Life Sciences, Ecole Polytechnique Fédérale de Lausanne (EPFL), Lausanne, Switzerland
WebPageElement:
      isAccessibleForFree:
      cssSelector:.main-content

Social Networks {👍}(1)

External Links {🔗}(515)

Analytics and Tracking {📊}

  • Google Tag Manager

Libraries {📚}

  • Prism.js
  • Zoom.js

Emails and Hosting {✉️}

Mail Servers:

  • mxa-002c5801.gslb.pphosted.com
  • mxb-002c5801.gslb.pphosted.com

Name Servers:

  • pdns1.ultradns.net
  • pdns2.ultradns.net
  • pdns3.ultradns.org
  • pdns4.ultradns.org
  • pdns5.ultradns.info
  • pdns6.ultradns.co.uk

CDN Services {📦}

  • Crossref

5.41s.