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. Schema
  9. Social Networks
  10. External Links
  11. Analytics And Tracking
  12. Libraries
  13. Hosting Providers
  14. CDN Services

We began analyzing https://www.nature.com/articles/nsb1194-789, but it redirected us to https://www.nature.com/articles/nsb1194-789. The analysis below is for the second page.

Title[redir]:
Human mannose-binding protein carbohydrate recognition domain trimerizes through a triple α-helical coiled-coil | Nature Structural & Molecular Biology
Description:
Human mannose-binding protein is a hexamer of trimers with each subunit consisting of an amino-terminal region rich in cysteine, 19 collagen repeats, a ‘neck’, and a carbohydrate recognition domain that requires calcium to bind ligand. A 148-residue peptide, consisting of the ‘neck’ and carbohydrate recognition domains forms trimers in solution and in crystals. The structure of this trimeric peptide has been determined in two different crystal forms. The ‘neck’ forms a triple α-helical coiled-coil. Each α-helix interacts with a neighbouring carbohydrate recognition domain. The spatial arrangement of the carbohydrate recognition domains suggest how MBP trimers form the basic recognition unit for branched oligosaccharides on microorganisms.

Matching Content Categories {📚}

  • Education
  • Mobile Technology & AI
  • Virtual Reality

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 9,135,289 visitors per month in the current month.

check SE Ranking
check Ahrefs
check Similarweb
check Ubersuggest
check Semrush

How Does Doi.org Make Money? {💸}

We see no obvious way the site makes money.

While profit motivates many websites, others exist to inspire, entertain, or provide valuable resources. Websites have a variety of goals. And this might be one of them. Doi.org might be plotting its profit, but the way they're doing it isn't detectable yet.

Keywords {🔍}

article, google, scholar, cas, pubmed, nature, protein, mannosebinding, access, human, recognition, structure, biol, ezekowitz, content, cookies, carbohydrate, domain, αhelical, forms, privacy, data, open, lectins, rab, complement, drickamer, molecular, biology, coiledcoil, sheriff, chang, domains, reid, kbm, pathway, chem, structures, crystallogr, research, advertising, analysis, information, subscribe, structural, triple, trimers, neck, crystal, institution,

Topics {✒️}

nature portfolio permissions reprints privacy policy triple α-helical coiled-coil α-helical coiled-coil stalks advertising human mannose-binding protein social media nature genet mannose-binding protein multimerize nature 343 nature 360 nature 367 nature 371 nature 289 nature carbohydrate-recognition domains linked protein data bank stranded α-helical bundle related c-type lectins mannose-binding proteins isolated computer-based archival file hematology/oncology harvard department extracorporeal blood-cleansing device amino-terminal region rich mannose-rich salmonella montevideo collagenous c-type lectins calcium-dependent lectin domain collagen triple-helix formation carbohydrate recognition domain carbohydrate-recognition domain preliminary x-ray analysis mannose-binding protein e-selectin/ligand interaction springerlink instant access generalized molecular replacement mannan-binding protein permissions personal data mannose-rich isolate data protection human immunodeficiency virus α-helix interacts x-ray crystallography stranded coiled coils privacy proenzyme c1r2c1s2 complex yale university press basic recognition unit protein structure stabilization

Schema {🗺️}

WebPage:
      mainEntity:
         headline:Human mannose-binding protein carbohydrate recognition domain trimerizes through a triple α-helical coiled-coil
         description:Human mannose-binding protein is a hexamer of trimers with each subunit consisting of an amino-terminal region rich in cysteine, 19 collagen repeats, a ‘neck’, and a carbohydrate recognition domain that requires calcium to bind ligand. A 148-residue peptide, consisting of the ‘neck’ and carbohydrate recognition domains forms trimers in solution and in crystals. The structure of this trimeric peptide has been determined in two different crystal forms. The ‘neck’ forms a triple α-helical coiled-coil. Each α-helix interacts with a neighbouring carbohydrate recognition domain. The spatial arrangement of the carbohydrate recognition domains suggest how MBP trimers form the basic recognition unit for branched oligosaccharides on microorganisms.
         datePublished:
         dateModified:
         pageStart:789
         pageEnd:794
         sameAs:https://doi.org/10.1038/nsb1194-789
         keywords:
            Life Sciences
            general
            Biochemistry
            Protein Structure
            Membrane Biology
            Biological Microscopy
         image:
         isPartOf:
            name:Nature Structural Biology
            issn:
               1545-9985
               1072-8368
            volumeNumber:1
            type:
               Periodical
               PublicationVolume
         publisher:
            name:Nature Publishing Group US
            logo:
               url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
               type:ImageObject
            type:Organization
         author:
               name:Steven Sheriff
               affiliation:
                     name:Bristol-Myers Squibb Pharmaceutical Research Institute
                     address:
                        name:Bristol-Myers Squibb Pharmaceutical Research Institute, Princeton, USA
                        type:PostalAddress
                     type:Organization
               type:Person
               name:ChiehYing Y. Chang
               affiliation:
                     name:Bristol-Myers Squibb Pharmaceutical Research Institute
                     address:
                        name:Bristol-Myers Squibb Pharmaceutical Research Institute, Princeton, USA
                        type:PostalAddress
                     type:Organization
               type:Person
               name:R. Alan B. Ezekowitz
               affiliation:
                     name:Divison of Hematology/Oncology Harvard Department of Pediatrics Children's Hospital and Dana Farber Cancer Institute
                     address:
                        name:Divison of Hematology/Oncology Harvard Department of Pediatrics Children's Hospital and Dana Farber Cancer Institute, Boston, USA
                        type:PostalAddress
                     type:Organization
               type:Person
         isAccessibleForFree:
         hasPart:
            isAccessibleForFree:
            cssSelector:.main-content
            type:WebPageElement
         type:ScholarlyArticle
      context:https://schema.org
ScholarlyArticle:
      headline:Human mannose-binding protein carbohydrate recognition domain trimerizes through a triple α-helical coiled-coil
      description:Human mannose-binding protein is a hexamer of trimers with each subunit consisting of an amino-terminal region rich in cysteine, 19 collagen repeats, a ‘neck’, and a carbohydrate recognition domain that requires calcium to bind ligand. A 148-residue peptide, consisting of the ‘neck’ and carbohydrate recognition domains forms trimers in solution and in crystals. The structure of this trimeric peptide has been determined in two different crystal forms. The ‘neck’ forms a triple α-helical coiled-coil. Each α-helix interacts with a neighbouring carbohydrate recognition domain. The spatial arrangement of the carbohydrate recognition domains suggest how MBP trimers form the basic recognition unit for branched oligosaccharides on microorganisms.
      datePublished:
      dateModified:
      pageStart:789
      pageEnd:794
      sameAs:https://doi.org/10.1038/nsb1194-789
      keywords:
         Life Sciences
         general
         Biochemistry
         Protein Structure
         Membrane Biology
         Biological Microscopy
      image:
      isPartOf:
         name:Nature Structural Biology
         issn:
            1545-9985
            1072-8368
         volumeNumber:1
         type:
            Periodical
            PublicationVolume
      publisher:
         name:Nature Publishing Group US
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:Steven Sheriff
            affiliation:
                  name:Bristol-Myers Squibb Pharmaceutical Research Institute
                  address:
                     name:Bristol-Myers Squibb Pharmaceutical Research Institute, Princeton, USA
                     type:PostalAddress
                  type:Organization
            type:Person
            name:ChiehYing Y. Chang
            affiliation:
                  name:Bristol-Myers Squibb Pharmaceutical Research Institute
                  address:
                     name:Bristol-Myers Squibb Pharmaceutical Research Institute, Princeton, USA
                     type:PostalAddress
                  type:Organization
            type:Person
            name:R. Alan B. Ezekowitz
            affiliation:
                  name:Divison of Hematology/Oncology Harvard Department of Pediatrics Children's Hospital and Dana Farber Cancer Institute
                  address:
                     name:Divison of Hematology/Oncology Harvard Department of Pediatrics Children's Hospital and Dana Farber Cancer Institute, Boston, USA
                     type:PostalAddress
                  type:Organization
            type:Person
      isAccessibleForFree:
      hasPart:
         isAccessibleForFree:
         cssSelector:.main-content
         type:WebPageElement
["Periodical","PublicationVolume"]:
      name:Nature Structural Biology
      issn:
         1545-9985
         1072-8368
      volumeNumber:1
Organization:
      name:Nature Publishing Group US
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:Bristol-Myers Squibb Pharmaceutical Research Institute
      address:
         name:Bristol-Myers Squibb Pharmaceutical Research Institute, Princeton, USA
         type:PostalAddress
      name:Bristol-Myers Squibb Pharmaceutical Research Institute
      address:
         name:Bristol-Myers Squibb Pharmaceutical Research Institute, Princeton, USA
         type:PostalAddress
      name:Divison of Hematology/Oncology Harvard Department of Pediatrics Children's Hospital and Dana Farber Cancer Institute
      address:
         name:Divison of Hematology/Oncology Harvard Department of Pediatrics Children's Hospital and Dana Farber Cancer Institute, Boston, USA
         type:PostalAddress
ImageObject:
      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
Person:
      name:Steven Sheriff
      affiliation:
            name:Bristol-Myers Squibb Pharmaceutical Research Institute
            address:
               name:Bristol-Myers Squibb Pharmaceutical Research Institute, Princeton, USA
               type:PostalAddress
            type:Organization
      name:ChiehYing Y. Chang
      affiliation:
            name:Bristol-Myers Squibb Pharmaceutical Research Institute
            address:
               name:Bristol-Myers Squibb Pharmaceutical Research Institute, Princeton, USA
               type:PostalAddress
            type:Organization
      name:R. Alan B. Ezekowitz
      affiliation:
            name:Divison of Hematology/Oncology Harvard Department of Pediatrics Children's Hospital and Dana Farber Cancer Institute
            address:
               name:Divison of Hematology/Oncology Harvard Department of Pediatrics Children's Hospital and Dana Farber Cancer Institute, Boston, USA
               type:PostalAddress
            type:Organization
PostalAddress:
      name:Bristol-Myers Squibb Pharmaceutical Research Institute, Princeton, USA
      name:Bristol-Myers Squibb Pharmaceutical Research Institute, Princeton, USA
      name:Divison of Hematology/Oncology Harvard Department of Pediatrics Children's Hospital and Dana Farber Cancer Institute, Boston, USA
WebPageElement:
      isAccessibleForFree:
      cssSelector:.main-content

Social Networks {👍}(1)

External Links {🔗}(200)

Analytics and Tracking {📊}

  • Google Tag Manager

Libraries {📚}

  • Prism.js
  • Zoom.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

5.96s.