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LINK . SPRINGER . COM {}

  1. Analyzed Page
  2. Matching Content Categories
  3. CMS
  4. Monthly Traffic Estimate
  5. How Does Link.springer.com Make Money
  6. Keywords
  7. Topics
  8. Schema
  9. External Links
  10. Analytics And Tracking
  11. Libraries
  12. CDN Services

We are analyzing https://link.springer.com/article/10.1186/1471-2199-11-2.

Title:
Non-consensus GLI binding sites in Hedgehog target gene regulation | BMC Molecular Biology
Description:
Background The GLI transcription factors, mediators of the hedgehog signal bind with high affinity to the consensus sequence GACCACCCA. The affinity of variant single substitutions in GLI binding sites has been measured systematically, but the affinities of the variant binding sites appears low compared to the frequency of occurrence of variant sites in known GLI target gene promoters. Results We quantified transcriptional activation by GLI using PTCH1 promoter based luciferase reporters containing all single substitutions of the GLI consensus binding site. As expected variants with very low affinity did not activate the reporter. Many lower affinity binding sequences are, however, functional in the presence of moderate GLI concentration. Using two natural non-consensus GLI site promoters we showed that substitution of the variant sequences by consensus leads to comparable activity. Conclusions Variant GLI binding sites with relatively low affinity can within natural promoters lead to strong transcriptional activation. This may facilitate the identification of additional direct GLI target genes.
Website Age:
28 years and 1 months (reg. 1997-05-29).

Matching Content Categories {📚}

  • Education
  • Books & Literature
  • Science

Content Management System {📝}

What CMS is link.springer.com built with?

Custom-built

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

Traffic Estimate {📈}

What is the average monthly size of link.springer.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.
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How Does Link.springer.com Make Money? {💸}

We're unsure if the website is profiting.

While many websites aim to make money, others are created to share knowledge or showcase creativity. People build websites for various reasons. This could be one of them. Link.springer.com might be making money, but it's not detectable how they're doing it.

Keywords {🔍}

gli, binding, consensus, site, sites, activation, article, pubmed, reporter, sequence, promoter, luciferase, figure, google, scholar, gene, affinity, cas, ptch, variant, expression, target, transcription, construct, transcriptional, functional, activity, single, position, gliact, promoters, results, variants, genes, shown, constructs, human, cells, hedgehog, ptchvar, ptchwt, central, factors, sequences, control, wild, type, data, nonconsensus, substitutions,

Topics {✒️}

thomas eichberger & anna-maria frischauf sandra laner-plamberger open access article protein-dna binding interactions designer zinc-finger proteins finger gli-dna complex article download pdf pen/strep100x stock solution anna-maria frischauf introducing site-specific mutations hedgehog-responsive enhancers linked gli-dna binding domain transcription-factor binding affinity polyclonal goat-anti-gli2 laner-plamberger hedgehog/gli signal transduction full size image hh pathway activation author information authors molecular biology reporter gene transcription gli2-specific transcriptional activation reporter gene assays firefly luciferase gene regulate target genes affinity profile luciferase reporter system luciferase reporter assays transcription factor binding luciferase reporter assay luciferase reporter constructs dna binding domain gli binding site demonstrates specific binding view gli gene encodes hedgehog receptor ptch1 privacy choices/manage cookies ptch1_var luciferase reporter variant binding site binding site variant additional transcription factors wild type promoters gli binding sites dna binding sites authors’ original file gli transcription factors site directed mutagenesis selected binding sequences specific promoters attention

Schema {🗺️}

WebPage:
      mainEntity:
         headline:Non-consensus GLI binding sites in Hedgehog target gene regulation
         description:The GLI transcription factors, mediators of the hedgehog signal bind with high affinity to the consensus sequence GACCACCCA. The affinity of variant single substitutions in GLI binding sites has been measured systematically, but the affinities of the variant binding sites appears low compared to the frequency of occurrence of variant sites in known GLI target gene promoters. We quantified transcriptional activation by GLI using PTCH1 promoter based luciferase reporters containing all single substitutions of the GLI consensus binding site. As expected variants with very low affinity did not activate the reporter. Many lower affinity binding sequences are, however, functional in the presence of moderate GLI concentration. Using two natural non-consensus GLI site promoters we showed that substitution of the variant sequences by consensus leads to comparable activity. Variant GLI binding sites with relatively low affinity can within natural promoters lead to strong transcriptional activation. This may facilitate the identification of additional direct GLI target genes.
         datePublished:2010-01-13T00:00:00Z
         dateModified:2010-01-13T00:00:00Z
         pageStart:1
         pageEnd:9
         license:https://creativecommons.org/licenses/by/2.0
         sameAs:https://doi.org/10.1186/1471-2199-11-2
         keywords:
            Luciferase Reporter
            HaCaT Cell
            Consensus Site
            Luciferase Reporter Construct
            Consensus Binding Site
            Biochemistry
            general
            Nucleic Acid Chemistry
            Cell Biology
         image:
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         isPartOf:
            name:BMC Molecular Biology
            issn:
               1471-2199
            volumeNumber:11
            type:
               Periodical
               PublicationVolume
         publisher:
            name:BioMed Central
            logo:
               url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
               type:ImageObject
            type:Organization
         author:
               name:Martina Winklmayr
               affiliation:
                     name:University of Salzburg
                     address:
                        name:Department of Molecular Biology, University of Salzburg, Salzburg, Austria
                        type:PostalAddress
                     type:Organization
               type:Person
               name:Carmen Schmid
               affiliation:
                     name:University of Salzburg
                     address:
                        name:Department of Molecular Biology, University of Salzburg, Salzburg, Austria
                        type:PostalAddress
                     type:Organization
               type:Person
               name:Sandra Laner-Plamberger
               affiliation:
                     name:University of Salzburg
                     address:
                        name:Department of Molecular Biology, University of Salzburg, Salzburg, Austria
                        type:PostalAddress
                     type:Organization
               type:Person
               name:Alexandra Kaser
               affiliation:
                     name:University of Salzburg
                     address:
                        name:Department of Molecular Biology, University of Salzburg, Salzburg, Austria
                        type:PostalAddress
                     type:Organization
               type:Person
               name:Fritz Aberger
               affiliation:
                     name:University of Salzburg
                     address:
                        name:Department of Molecular Biology, University of Salzburg, Salzburg, Austria
                        type:PostalAddress
                     type:Organization
               type:Person
               name:Thomas Eichberger
               affiliation:
                     name:University of Salzburg
                     address:
                        name:Department of Molecular Biology, University of Salzburg, Salzburg, Austria
                        type:PostalAddress
                     type:Organization
               type:Person
               name:Anna-Maria Frischauf
               affiliation:
                     name:University of Salzburg
                     address:
                        name:Department of Molecular Biology, University of Salzburg, Salzburg, Austria
                        type:PostalAddress
                     type:Organization
               email:[email protected]
               type:Person
         isAccessibleForFree:1
         type:ScholarlyArticle
      context:https://schema.org
ScholarlyArticle:
      headline:Non-consensus GLI binding sites in Hedgehog target gene regulation
      description:The GLI transcription factors, mediators of the hedgehog signal bind with high affinity to the consensus sequence GACCACCCA. The affinity of variant single substitutions in GLI binding sites has been measured systematically, but the affinities of the variant binding sites appears low compared to the frequency of occurrence of variant sites in known GLI target gene promoters. We quantified transcriptional activation by GLI using PTCH1 promoter based luciferase reporters containing all single substitutions of the GLI consensus binding site. As expected variants with very low affinity did not activate the reporter. Many lower affinity binding sequences are, however, functional in the presence of moderate GLI concentration. Using two natural non-consensus GLI site promoters we showed that substitution of the variant sequences by consensus leads to comparable activity. Variant GLI binding sites with relatively low affinity can within natural promoters lead to strong transcriptional activation. This may facilitate the identification of additional direct GLI target genes.
      datePublished:2010-01-13T00:00:00Z
      dateModified:2010-01-13T00:00:00Z
      pageStart:1
      pageEnd:9
      license:https://creativecommons.org/licenses/by/2.0
      sameAs:https://doi.org/10.1186/1471-2199-11-2
      keywords:
         Luciferase Reporter
         HaCaT Cell
         Consensus Site
         Luciferase Reporter Construct
         Consensus Binding Site
         Biochemistry
         general
         Nucleic Acid Chemistry
         Cell Biology
      image:
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1186%2F1471-2199-11-2/MediaObjects/12867_2009_Article_483_Fig1_HTML.jpg
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1186%2F1471-2199-11-2/MediaObjects/12867_2009_Article_483_Fig2_HTML.jpg
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1186%2F1471-2199-11-2/MediaObjects/12867_2009_Article_483_Fig3_HTML.jpg
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1186%2F1471-2199-11-2/MediaObjects/12867_2009_Article_483_Fig4_HTML.jpg
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1186%2F1471-2199-11-2/MediaObjects/12867_2009_Article_483_Fig5_HTML.jpg
      isPartOf:
         name:BMC Molecular Biology
         issn:
            1471-2199
         volumeNumber:11
         type:
            Periodical
            PublicationVolume
      publisher:
         name:BioMed Central
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:Martina Winklmayr
            affiliation:
                  name:University of Salzburg
                  address:
                     name:Department of Molecular Biology, University of Salzburg, Salzburg, Austria
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Carmen Schmid
            affiliation:
                  name:University of Salzburg
                  address:
                     name:Department of Molecular Biology, University of Salzburg, Salzburg, Austria
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Sandra Laner-Plamberger
            affiliation:
                  name:University of Salzburg
                  address:
                     name:Department of Molecular Biology, University of Salzburg, Salzburg, Austria
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Alexandra Kaser
            affiliation:
                  name:University of Salzburg
                  address:
                     name:Department of Molecular Biology, University of Salzburg, Salzburg, Austria
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Fritz Aberger
            affiliation:
                  name:University of Salzburg
                  address:
                     name:Department of Molecular Biology, University of Salzburg, Salzburg, Austria
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Thomas Eichberger
            affiliation:
                  name:University of Salzburg
                  address:
                     name:Department of Molecular Biology, University of Salzburg, Salzburg, Austria
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Anna-Maria Frischauf
            affiliation:
                  name:University of Salzburg
                  address:
                     name:Department of Molecular Biology, University of Salzburg, Salzburg, Austria
                     type:PostalAddress
                  type:Organization
            email:[email protected]
            type:Person
      isAccessibleForFree:1
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      name:BMC Molecular Biology
      issn:
         1471-2199
      volumeNumber:11
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      name:BioMed Central
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         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:University of Salzburg
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         name:Department of Molecular Biology, University of Salzburg, Salzburg, Austria
         type:PostalAddress
      name:University of Salzburg
      address:
         name:Department of Molecular Biology, University of Salzburg, Salzburg, Austria
         type:PostalAddress
      name:University of Salzburg
      address:
         name:Department of Molecular Biology, University of Salzburg, Salzburg, Austria
         type:PostalAddress
      name:University of Salzburg
      address:
         name:Department of Molecular Biology, University of Salzburg, Salzburg, Austria
         type:PostalAddress
      name:University of Salzburg
      address:
         name:Department of Molecular Biology, University of Salzburg, Salzburg, Austria
         type:PostalAddress
      name:University of Salzburg
      address:
         name:Department of Molecular Biology, University of Salzburg, Salzburg, Austria
         type:PostalAddress
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      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
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      name:Martina Winklmayr
      affiliation:
            name:University of Salzburg
            address:
               name:Department of Molecular Biology, University of Salzburg, Salzburg, Austria
               type:PostalAddress
            type:Organization
      name:Carmen Schmid
      affiliation:
            name:University of Salzburg
            address:
               name:Department of Molecular Biology, University of Salzburg, Salzburg, Austria
               type:PostalAddress
            type:Organization
      name:Sandra Laner-Plamberger
      affiliation:
            name:University of Salzburg
            address:
               name:Department of Molecular Biology, University of Salzburg, Salzburg, Austria
               type:PostalAddress
            type:Organization
      name:Alexandra Kaser
      affiliation:
            name:University of Salzburg
            address:
               name:Department of Molecular Biology, University of Salzburg, Salzburg, Austria
               type:PostalAddress
            type:Organization
      name:Fritz Aberger
      affiliation:
            name:University of Salzburg
            address:
               name:Department of Molecular Biology, University of Salzburg, Salzburg, Austria
               type:PostalAddress
            type:Organization
      name:Thomas Eichberger
      affiliation:
            name:University of Salzburg
            address:
               name:Department of Molecular Biology, University of Salzburg, Salzburg, Austria
               type:PostalAddress
            type:Organization
      name:Anna-Maria Frischauf
      affiliation:
            name:University of Salzburg
            address:
               name:Department of Molecular Biology, University of Salzburg, Salzburg, Austria
               type:PostalAddress
            type:Organization
      email:[email protected]
PostalAddress:
      name:Department of Molecular Biology, University of Salzburg, Salzburg, Austria
      name:Department of Molecular Biology, University of Salzburg, Salzburg, Austria
      name:Department of Molecular Biology, University of Salzburg, Salzburg, Austria
      name:Department of Molecular Biology, University of Salzburg, Salzburg, Austria
      name:Department of Molecular Biology, University of Salzburg, Salzburg, Austria
      name:Department of Molecular Biology, University of Salzburg, Salzburg, Austria
      name:Department of Molecular Biology, University of Salzburg, Salzburg, Austria

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