Here's how DOI.ORG makes money* and how much!

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

DOI . ORG {}

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

We began analyzing https://link.springer.com/article/10.1007/s00005-009-0057-2, but it redirected us to https://link.springer.com/article/10.1007/s00005-009-0057-2. The analysis below is for the second page.

Title[redir]:
Cathelicidin LL-37: A Multitask Antimicrobial Peptide | Archivum Immunologiae et Therapiae Experimentalis
Description:
The antimicrobial peptide LL-37 is the only known member of the cathelicidin family of peptides expressed in humans. LL-37 is a multifunctional host defense molecule essential for normal immune responses to infection and tissue injury. LL-37 peptide is a potent killer of different microorganisms with the ability to prevent immunostimulatory effects of bacterial wall molecules such as lipopolysaccharide and can therefore protect against lethal endotoxemia. Additional reported activities of LL-37 include chemoattractant function, inhibition of neutrophil apoptosis, and stimulation of angiogenesis, tissue regeneration, and cytokine release (e.g. IL-8). Cellular production of LL-37 is affected by multiple factors, including bacterial products, host cytokines, availability of oxygen, and sun exposure through the activation of CAP-18 gene expression by vitamin D3. At infection sites, the function of LL-37 can be inhibited by charge-driven interactions with DNA and F-actin released from dead neutrophils and other cells lysed as the result of inflammation. A better understanding of LL-37’s biological properties is necessary for its possible therapeutic application for immunomodulatory purposes as well as in treating bacterial infection.

Matching Content Categories {📚}

  • Education
  • Science
  • Politics

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?

🌠 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 Doi.org Make Money? {💸}

The income method remains a mystery to us.

The purpose of some websites isn't monetary gain; they're meant to inform, educate, or foster collaboration. Everyone has unique reasons for building websites. This could be an example. Doi.org could have a money-making trick up its sleeve, but it's undetectable for now.

Keywords {🔍}

google, scholar, article, pubmed, cas, human, antimicrobial, peptide, cathelicidin, peptides, expression, cells, immunol, cell, bucki, host, defense, bacterial, invest, activity, dermatol, infection, biol, immune, antibacterial, epithelial, cancer, med, vitamin, neutrophils, response, cationic, innate, antimicrob, agents, chemother, chem, skin, privacy, cookies, function, content, namiot, expressed, neutrophil, release, dna, factin, factor, protein,

Topics {✒️}

month download article/chapter peptide antibiotic ll-37/hcap-18 cathelicidin-related antimicrobial peptide granulocyte colony-stimulating factor cathelicidin-derived ll-37 peptide epithelial cell-derived cathelicidin multidrug-resistant acinetobacter baumannii inflammatory mediator il-1beta mammalian cathelicidin-derived peptides leukotriene b4-mediated release antimicrobial protein hcap18/ll-37 tlr-mediated inflammatory response human cathelicidin cap18/ll-37 article archivum immunologiae minimal membrane-targeting antimicrobial conformation-dependent antibacterial activity antimicrobial host defense human beta-defensin 1 host defence peptides ll-37 peptide enhances host defense cells antibacterial peptide ll-37 multitask antimicrobial peptide full article pdf bactericidal cationic peptides cathelicidin ll-37 induces antimicrobial peptide ll-37 actin bundle formation antimicrobial cathelicidin peptide cationic steroid csa-13 antimicrobial protein hcap-18 including bacterial products dna/f-actin bundles human cathelicidin ll-37 modulates cellular response anti-fungal activity antibacterial peptides cap18 human cap18/ll-37 innate defense system cathelicidin antimicrobial peptides suppresses neutrophil apoptosis privacy choices/manage cookies human alpha-defensins human ll-37 fragments formyl-peptide receptors human epithelial cells human immune response human plasma gelsolin formyl-peptide receptor article bucki

Questions {❓}

  • Brogden KA (2005) Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?
  • Ginsburg I (2004) Bactericidal cationic peptides can also function as bacteriolysis-inducing agents mimicking beta-lactam antibiotics?

Schema {🗺️}

WebPage:
      mainEntity:
         headline:Cathelicidin LL-37: A Multitask Antimicrobial Peptide
         description:The antimicrobial peptide LL-37 is the only known member of the cathelicidin family of peptides expressed in humans. LL-37 is a multifunctional host defense molecule essential for normal immune responses to infection and tissue injury. LL-37 peptide is a potent killer of different microorganisms with the ability to prevent immunostimulatory effects of bacterial wall molecules such as lipopolysaccharide and can therefore protect against lethal endotoxemia. Additional reported activities of LL-37 include chemoattractant function, inhibition of neutrophil apoptosis, and stimulation of angiogenesis, tissue regeneration, and cytokine release (e.g. IL-8). Cellular production of LL-37 is affected by multiple factors, including bacterial products, host cytokines, availability of oxygen, and sun exposure through the activation of CAP-18 gene expression by vitamin D3. At infection sites, the function of LL-37 can be inhibited by charge-driven interactions with DNA and F-actin released from dead neutrophils and other cells lysed as the result of inflammation. A better understanding of LL-37’s biological properties is necessary for its possible therapeutic application for immunomodulatory purposes as well as in treating bacterial infection.
         datePublished:2010-01-05T00:00:00Z
         dateModified:2010-01-05T00:00:00Z
         pageStart:15
         pageEnd:25
         sameAs:https://doi.org/10.1007/s00005-009-0057-2
         keywords:
            Antibacterial agents
            Bacteria
            Infection
            hCAP-18
            Immunology
            Pharmacology/Toxicology
         image:
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00005-009-0057-2/MediaObjects/5_2009_57_Fig1_HTML.jpg
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00005-009-0057-2/MediaObjects/5_2009_57_Fig2_HTML.jpg
         isPartOf:
            name:Archivum Immunologiae et Therapiae Experimentalis
            issn:
               1661-4917
               0004-069X
            volumeNumber:58
            type:
               Periodical
               PublicationVolume
         publisher:
            name:SP Birkhäuser Verlag Basel
            logo:
               url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
               type:ImageObject
            type:Organization
         author:
               name:Robert Bucki
               affiliation:
                     name:University of Pennsylvania
                     address:
                        name:Institute for Medicine and Engineering, University of Pennsylvania, Philadelphia, USA
                        type:PostalAddress
                     type:Organization
               email:[email protected]
               type:Person
               name:Katarzyna Leszczyńska
               affiliation:
                     name:Medical University of Bialystok
                     address:
                        name:Department of Diagnostic Microbiology, Medical University of Bialystok, Bialystok, Poland
                        type:PostalAddress
                     type:Organization
               type:Person
               name:Andrzej Namiot
               affiliation:
                     name:Medical University of Bialystok
                     address:
                        name:Department of Anatomy, Medical University of Bialystok, Bialystok, Poland
                        type:PostalAddress
                     type:Organization
               type:Person
               name:Wojciech Sokołowski
               affiliation:
                     name:University of Pennsylvania
                     address:
                        name:Institute for Medicine and Engineering, University of Pennsylvania, Philadelphia, USA
                        type:PostalAddress
                     type:Organization
               type:Person
         isAccessibleForFree:
         hasPart:
            isAccessibleForFree:
            cssSelector:.main-content
            type:WebPageElement
         type:ScholarlyArticle
      context:https://schema.org
ScholarlyArticle:
      headline:Cathelicidin LL-37: A Multitask Antimicrobial Peptide
      description:The antimicrobial peptide LL-37 is the only known member of the cathelicidin family of peptides expressed in humans. LL-37 is a multifunctional host defense molecule essential for normal immune responses to infection and tissue injury. LL-37 peptide is a potent killer of different microorganisms with the ability to prevent immunostimulatory effects of bacterial wall molecules such as lipopolysaccharide and can therefore protect against lethal endotoxemia. Additional reported activities of LL-37 include chemoattractant function, inhibition of neutrophil apoptosis, and stimulation of angiogenesis, tissue regeneration, and cytokine release (e.g. IL-8). Cellular production of LL-37 is affected by multiple factors, including bacterial products, host cytokines, availability of oxygen, and sun exposure through the activation of CAP-18 gene expression by vitamin D3. At infection sites, the function of LL-37 can be inhibited by charge-driven interactions with DNA and F-actin released from dead neutrophils and other cells lysed as the result of inflammation. A better understanding of LL-37’s biological properties is necessary for its possible therapeutic application for immunomodulatory purposes as well as in treating bacterial infection.
      datePublished:2010-01-05T00:00:00Z
      dateModified:2010-01-05T00:00:00Z
      pageStart:15
      pageEnd:25
      sameAs:https://doi.org/10.1007/s00005-009-0057-2
      keywords:
         Antibacterial agents
         Bacteria
         Infection
         hCAP-18
         Immunology
         Pharmacology/Toxicology
      image:
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00005-009-0057-2/MediaObjects/5_2009_57_Fig1_HTML.jpg
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs00005-009-0057-2/MediaObjects/5_2009_57_Fig2_HTML.jpg
      isPartOf:
         name:Archivum Immunologiae et Therapiae Experimentalis
         issn:
            1661-4917
            0004-069X
         volumeNumber:58
         type:
            Periodical
            PublicationVolume
      publisher:
         name:SP Birkhäuser Verlag Basel
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:Robert Bucki
            affiliation:
                  name:University of Pennsylvania
                  address:
                     name:Institute for Medicine and Engineering, University of Pennsylvania, Philadelphia, USA
                     type:PostalAddress
                  type:Organization
            email:[email protected]
            type:Person
            name:Katarzyna Leszczyńska
            affiliation:
                  name:Medical University of Bialystok
                  address:
                     name:Department of Diagnostic Microbiology, Medical University of Bialystok, Bialystok, Poland
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Andrzej Namiot
            affiliation:
                  name:Medical University of Bialystok
                  address:
                     name:Department of Anatomy, Medical University of Bialystok, Bialystok, Poland
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Wojciech Sokołowski
            affiliation:
                  name:University of Pennsylvania
                  address:
                     name:Institute for Medicine and Engineering, University of Pennsylvania, Philadelphia, USA
                     type:PostalAddress
                  type:Organization
            type:Person
      isAccessibleForFree:
      hasPart:
         isAccessibleForFree:
         cssSelector:.main-content
         type:WebPageElement
["Periodical","PublicationVolume"]:
      name:Archivum Immunologiae et Therapiae Experimentalis
      issn:
         1661-4917
         0004-069X
      volumeNumber:58
Organization:
      name:SP Birkhäuser Verlag Basel
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:University of Pennsylvania
      address:
         name:Institute for Medicine and Engineering, University of Pennsylvania, Philadelphia, USA
         type:PostalAddress
      name:Medical University of Bialystok
      address:
         name:Department of Diagnostic Microbiology, Medical University of Bialystok, Bialystok, Poland
         type:PostalAddress
      name:Medical University of Bialystok
      address:
         name:Department of Anatomy, Medical University of Bialystok, Bialystok, Poland
         type:PostalAddress
      name:University of Pennsylvania
      address:
         name:Institute for Medicine and Engineering, University of Pennsylvania, Philadelphia, USA
         type:PostalAddress
ImageObject:
      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
Person:
      name:Robert Bucki
      affiliation:
            name:University of Pennsylvania
            address:
               name:Institute for Medicine and Engineering, University of Pennsylvania, Philadelphia, USA
               type:PostalAddress
            type:Organization
      email:[email protected]
      name:Katarzyna Leszczyńska
      affiliation:
            name:Medical University of Bialystok
            address:
               name:Department of Diagnostic Microbiology, Medical University of Bialystok, Bialystok, Poland
               type:PostalAddress
            type:Organization
      name:Andrzej Namiot
      affiliation:
            name:Medical University of Bialystok
            address:
               name:Department of Anatomy, Medical University of Bialystok, Bialystok, Poland
               type:PostalAddress
            type:Organization
      name:Wojciech Sokołowski
      affiliation:
            name:University of Pennsylvania
            address:
               name:Institute for Medicine and Engineering, University of Pennsylvania, Philadelphia, USA
               type:PostalAddress
            type:Organization
PostalAddress:
      name:Institute for Medicine and Engineering, University of Pennsylvania, Philadelphia, USA
      name:Department of Diagnostic Microbiology, Medical University of Bialystok, Bialystok, Poland
      name:Department of Anatomy, Medical University of Bialystok, Bialystok, Poland
      name:Institute for Medicine and Engineering, University of Pennsylvania, Philadelphia, USA
WebPageElement:
      isAccessibleForFree:
      cssSelector:.main-content

External Links {🔗}(347)

Analytics and Tracking {📊}

  • Google Tag Manager

Libraries {📚}

  • Clipboard.js
  • Prism.js

Emails and Hosting {✉️}

Mail Servers:

  • mx.zoho.eu
  • mx2.zoho.eu
  • mx3.zoho.eu

Name Servers:

  • josh.ns.cloudflare.com
  • zita.ns.cloudflare.com

CDN Services {📦}

  • Crossref

4.34s.