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

We began analyzing https://www.nature.com/articles/nrm2838, but it redirected us to https://www.nature.com/articles/nrm2838. The analysis below is for the second page.

Title[redir]:
The mechanism of eukaryotic translation initiation and principles of its regulation | Nature Reviews Molecular Cell Biology
Description:
Protein synthesis is regulated at the initiation stage. Determining the structures and activities of initiation factors, and mapping their interactions in ribosomal initiation complexes, has advanced our understanding of translation initiation and provided a foundation for studying its regulation. Protein synthesis is principally regulated at the initiation stage (rather than during elongation or termination), allowing rapid, reversible and spatial control of gene expression. Progress over recent years in determining the structures and activities of initiation factors, and in mapping their interactions in ribosomal initiation complexes, have advanced our understanding of the complex translation initiation process. These developments have provided a solid foundation for studying the regulation of translation initiation by mechanisms that include the modulation of initiation factor activity (which affects almost all scanning-dependent initiation) and through sequence-specific RNA-binding proteins and microRNAs (which affect individual mRNAs).

Matching Content Categories {📚}

  • Education
  • Science
  • Telecommunications

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? {💸}

We can't tell how the site generates income.

Not all websites focus on profit; some are designed to educate, connect people, or share useful tools. People create websites for numerous reasons. And this could be one such example. Doi.org might be plotting its profit, but the way they're doing it isn't detectable yet.

Keywords {🔍}

pubmed, google, scholar, article, cas, initiation, translation, central, cell, mrna, protein, biol, eukaryotic, ribosomal, nature, eif, mol, factor, rna, subunit, ribosome, pestova, complex, translational, mrnas, repression, regulation, hellen, genes, dev, codon, factors, human, sci, usa, proteins, mammalian, domain, proc, natl, acad, eife, structure, interaction, complexes, eifa, open, binding, access, site,

Topics {✒️}

nature portfolio permissions reprints privacy policy eif2–gtp–met-trnameti ternary complexes author information authors cap-distal iron-responsive elements advertising research social media sequence-specific rna-binding proteins nature cell biol micro-rna-mediated translation repression nature rev nature struct asp-glu-ala-asp asp-glu-x-asp composite nucleotide-binding sites classical gtpase-activator protein nature 455 nature 394 nature 403 nature 438 nature 447 nature cap-binding complex elf4f post-transcriptional gene expression affect pabp-dependent deadenylation codon–anticodon base pairing codon-anticodon base-pairing cap-independent translation switch hypoxia-controlled cap-dependent protein–protein interaction surfaces normal deadenylation-dependent route canonical scanning-dependent mode met-trnameti cold spring harbor dead-box protein ded1p recapitulate mirna-mediated repression mtor-independent translational upregulation blocks eif4f access post-termination ribosomal complexes springerlink instant access eif4g-pabp interaction increases dead-box rna helicase 'open' conformation open conformation internal ribosomal entry yeast eif4a–eif4g complex cap-binding complex eif4f stem-loop binding protein

Questions {❓}

  • How do microRNAs regulate gene expression?
  • Supplementary information S5 (box) | Does the "closed loop" configuration resulting from PABP-eIF4G interaction promote ribosome recycling?
  • What determines whether mammalian ribosomes resume scanning after translation of a short upstream open reading frame?

Schema {🗺️}

WebPage:
      mainEntity:
         headline:The mechanism of eukaryotic translation initiation and principles of its regulation
         description: Protein synthesis is regulated at the initiation stage. Determining the structures and activities of initiation factors, and mapping their interactions in ribosomal initiation complexes, has advanced our understanding of translation initiation and provided a foundation for studying its regulation. Protein synthesis is principally regulated at the initiation stage (rather than during elongation or termination), allowing rapid, reversible and spatial control of gene expression. Progress over recent years in determining the structures and activities of initiation factors, and in mapping their interactions in ribosomal initiation complexes, have advanced our understanding of the complex translation initiation process. These developments have provided a solid foundation for studying the regulation of translation initiation by mechanisms that include the modulation of initiation factor activity (which affects almost all scanning-dependent initiation) and through sequence-specific RNA-binding proteins and microRNAs (which affect individual mRNAs).
         datePublished:
         dateModified:
         pageStart:113
         pageEnd:127
         sameAs:https://doi.org/10.1038/nrm2838
         keywords:
            miRNAs
            Translation
            Life Sciences
            general
            Cell Biology
            Cancer Research
            Developmental Biology
            Stem Cells
            Biochemistry
         image:
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1038%2Fnrm2838/MediaObjects/41580_2010_Article_BFnrm2838_Fig1_HTML.jpg
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1038%2Fnrm2838/MediaObjects/41580_2010_Article_BFnrm2838_Fig2_HTML.jpg
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1038%2Fnrm2838/MediaObjects/41580_2010_Article_BFnrm2838_Fig3_HTML.jpg
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1038%2Fnrm2838/MediaObjects/41580_2010_Article_BFnrm2838_Fig4_HTML.jpg
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1038%2Fnrm2838/MediaObjects/41580_2010_Article_BFnrm2838_Fig5_HTML.jpg
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1038%2Fnrm2838/MediaObjects/41580_2010_Article_BFnrm2838_Figa_HTML.jpg
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1038%2Fnrm2838/MediaObjects/41580_2010_Article_BFnrm2838_Figb_HTML.jpg
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1038%2Fnrm2838/MediaObjects/41580_2010_Article_BFnrm2838_Figc_HTML.jpg
         isPartOf:
            name:Nature Reviews Molecular Cell Biology
            issn:
               1471-0080
               1471-0072
            volumeNumber:11
            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:Richard J. Jackson
               affiliation:
                     name:University of Cambridge
                     address:
                        name:Department of Biochemistry, University of Cambridge, Cambridge, UK
                        type:PostalAddress
                     type:Organization
               type:Person
               name:Christopher U. T. Hellen
               affiliation:
                     name:State University of New York Downstate Medical Center
                     address:
                        name:Department of Cell Biology, State University of New York Downstate Medical Center, Brooklyn, USA
                        type:PostalAddress
                     type:Organization
                     name:
                     address:
                        name:
                        type:PostalAddress
                     type:Organization
               type:Person
               name:Tatyana V. Pestova
               affiliation:
                     name:State University of New York Downstate Medical Center
                     address:
                        name:Department of Cell Biology, State University of New York Downstate Medical Center, Brooklyn, USA
                        type:PostalAddress
                     type:Organization
                     name:
                     address:
                        name:
                        type:PostalAddress
                     type:Organization
               type:Person
         isAccessibleForFree:
         hasPart:
            isAccessibleForFree:
            cssSelector:.main-content
            type:WebPageElement
         type:ScholarlyArticle
      context:https://schema.org
ScholarlyArticle:
      headline:The mechanism of eukaryotic translation initiation and principles of its regulation
      description: Protein synthesis is regulated at the initiation stage. Determining the structures and activities of initiation factors, and mapping their interactions in ribosomal initiation complexes, has advanced our understanding of translation initiation and provided a foundation for studying its regulation. Protein synthesis is principally regulated at the initiation stage (rather than during elongation or termination), allowing rapid, reversible and spatial control of gene expression. Progress over recent years in determining the structures and activities of initiation factors, and in mapping their interactions in ribosomal initiation complexes, have advanced our understanding of the complex translation initiation process. These developments have provided a solid foundation for studying the regulation of translation initiation by mechanisms that include the modulation of initiation factor activity (which affects almost all scanning-dependent initiation) and through sequence-specific RNA-binding proteins and microRNAs (which affect individual mRNAs).
      datePublished:
      dateModified:
      pageStart:113
      pageEnd:127
      sameAs:https://doi.org/10.1038/nrm2838
      keywords:
         miRNAs
         Translation
         Life Sciences
         general
         Cell Biology
         Cancer Research
         Developmental Biology
         Stem Cells
         Biochemistry
      image:
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1038%2Fnrm2838/MediaObjects/41580_2010_Article_BFnrm2838_Fig1_HTML.jpg
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1038%2Fnrm2838/MediaObjects/41580_2010_Article_BFnrm2838_Fig2_HTML.jpg
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1038%2Fnrm2838/MediaObjects/41580_2010_Article_BFnrm2838_Fig3_HTML.jpg
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1038%2Fnrm2838/MediaObjects/41580_2010_Article_BFnrm2838_Fig4_HTML.jpg
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1038%2Fnrm2838/MediaObjects/41580_2010_Article_BFnrm2838_Fig5_HTML.jpg
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1038%2Fnrm2838/MediaObjects/41580_2010_Article_BFnrm2838_Figa_HTML.jpg
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1038%2Fnrm2838/MediaObjects/41580_2010_Article_BFnrm2838_Figb_HTML.jpg
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1038%2Fnrm2838/MediaObjects/41580_2010_Article_BFnrm2838_Figc_HTML.jpg
      isPartOf:
         name:Nature Reviews Molecular Cell Biology
         issn:
            1471-0080
            1471-0072
         volumeNumber:11
         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:Richard J. Jackson
            affiliation:
                  name:University of Cambridge
                  address:
                     name:Department of Biochemistry, University of Cambridge, Cambridge, UK
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Christopher U. T. Hellen
            affiliation:
                  name:State University of New York Downstate Medical Center
                  address:
                     name:Department of Cell Biology, State University of New York Downstate Medical Center, Brooklyn, USA
                     type:PostalAddress
                  type:Organization
                  name:
                  address:
                     name:
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Tatyana V. Pestova
            affiliation:
                  name:State University of New York Downstate Medical Center
                  address:
                     name:Department of Cell Biology, State University of New York Downstate Medical Center, Brooklyn, USA
                     type:PostalAddress
                  type:Organization
                  name:
                  address:
                     name:
                     type:PostalAddress
                  type:Organization
            type:Person
      isAccessibleForFree:
      hasPart:
         isAccessibleForFree:
         cssSelector:.main-content
         type:WebPageElement
["Periodical","PublicationVolume"]:
      name:Nature Reviews Molecular Cell Biology
      issn:
         1471-0080
         1471-0072
      volumeNumber:11
Organization:
      name:Nature Publishing Group UK
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:University of Cambridge
      address:
         name:Department of Biochemistry, University of Cambridge, Cambridge, UK
         type:PostalAddress
      name:State University of New York Downstate Medical Center
      address:
         name:Department of Cell Biology, State University of New York Downstate Medical Center, Brooklyn, USA
         type:PostalAddress
      name:
      address:
         name:
         type:PostalAddress
      name:State University of New York Downstate Medical Center
      address:
         name:Department of Cell Biology, State University of New York Downstate Medical Center, Brooklyn, USA
         type:PostalAddress
      name:
      address:
         name:
         type:PostalAddress
ImageObject:
      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
Person:
      name:Richard J. Jackson
      affiliation:
            name:University of Cambridge
            address:
               name:Department of Biochemistry, University of Cambridge, Cambridge, UK
               type:PostalAddress
            type:Organization
      name:Christopher U. T. Hellen
      affiliation:
            name:State University of New York Downstate Medical Center
            address:
               name:Department of Cell Biology, State University of New York Downstate Medical Center, Brooklyn, USA
               type:PostalAddress
            type:Organization
            name:
            address:
               name:
               type:PostalAddress
            type:Organization
      name:Tatyana V. Pestova
      affiliation:
            name:State University of New York Downstate Medical Center
            address:
               name:Department of Cell Biology, State University of New York Downstate Medical Center, Brooklyn, USA
               type:PostalAddress
            type:Organization
            name:
            address:
               name:
               type:PostalAddress
            type:Organization
PostalAddress:
      name:Department of Biochemistry, University of Cambridge, Cambridge, UK
      name:Department of Cell Biology, State University of New York Downstate Medical Center, Brooklyn, USA
      name:
      name:Department of Cell Biology, State University of New York Downstate Medical Center, Brooklyn, USA
      name:
WebPageElement:
      isAccessibleForFree:
      cssSelector:.main-content

Social Networks {👍}(2)

External Links {🔗}(501)

Analytics and Tracking {📊}

  • Google Tag Manager

Libraries {📚}

  • Particles.js
  • 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

4.53s.