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

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

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/10.1007/bf00506266.

Title:
Quercetin inhibits tyrosine phosphorylation by the cyclic nucleotide-independent, transforming protein kinase, pp60src | Naunyn-Schmiedeberg's Archives of Pharmacology
Description:
The bioflavonoid quercetin is a potent inhibitor of a cyclic nucleotide-independent, tumor virus-coded protein kinase which phosphorylates tyrosine residues and acts as a cellular transforming protein. Half-maximal inhibition of the protein kinase occurred at 3–4 μM quercetin whereas rutin was much less effective. The finding, that quercetin inhibits a cyclic nucleotide-independent protein kinase activity, may provide clues to the diverse pharmacological effects of the bioflavonoids.
Website Age:
28 years and 1 months (reg. 1997-05-29).

Matching Content Categories {📚}

  • Health & Fitness
  • Social Networks
  • Telecommunications

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.
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 Link.springer.com Make Money? {💸}

We can't see how the site brings in money.

Some websites aren't about earning revenue; they're built to connect communities or raise awareness. There are numerous motivations behind creating websites. This might be one of them. Link.springer.com could have a money-making trick up its sleeve, but it's undetectable for now.

Keywords {🔍}

kinase, protein, google, scholar, article, quercetin, tyrosine, privacy, cookies, cyclic, transforming, glossmann, presek, eigenbrodt, sarcoma, virus, content, publish, search, phosphorylation, nucleotideindependent, tumor, phosphorylates, access, biol, chem, data, information, log, journal, research, naunynschmiedebergs, inhibits, ppsrc, activity, discover, signalling, usa, nature, product, rous, download, springer, optional, personal, parties, policy, find, track, archives,

Topics {✒️}

monophosphate-independent protein kinase month download article/chapter rous sarcoma virus phosphorylates tyrosine residues protein kinase occurred transforming protein kinase ehrlich ascites tumor privacy choices/manage cookies cyclic nucleotide-independent casein kinase ii article naunyn-schmiedeberg' cellular transforming protein full article pdf protein kinase european economic area scope submit manuscript diverse pharmacological effects mol cell endocrinol conditions privacy policy high aerobic gylcolysis rat hepatoma cells tumor cells accepting optional cookies half-maximal inhibition quercetin inhibits check access instant access main content log transforming gene product journal finder publish naunyn-schmiedeberg' flavonoids pharmacology aims bioflavonoid quercetin 3–4 μm quercetin related subjects quercetin interaction eigenbrodt rights privacy policy personal data books a cyclic adenosine transforming gene tyrosine article log optional cookies manage preferences article glossmann subscription content article cite

Schema {🗺️}

WebPage:
      mainEntity:
         headline:Quercetin inhibits tyrosine phosphorylation by the cyclic nucleotide-independent, transforming protein kinase, pp60src
         description:The bioflavonoid quercetin is a potent inhibitor of a cyclic nucleotide-independent, tumor virus-coded protein kinase which phosphorylates tyrosine residues and acts as a cellular transforming protein. Half-maximal inhibition of the protein kinase occurred at 3–4 μM quercetin whereas rutin was much less effective. The finding, that quercetin inhibits a cyclic nucleotide-independent protein kinase activity, may provide clues to the diverse pharmacological effects of the bioflavonoids.
         datePublished:
         dateModified:
         pageStart:100
         pageEnd:102
         sameAs:https://doi.org/10.1007/BF00506266
         keywords:
            Quercetin
            Tyrosine Phosphorylation
            Protein kinase activity
            Tumor virus
            Flavonoids
            Pharmacology/Toxicology
            Neurosciences
         image:
         isPartOf:
            name:Naunyn-Schmiedeberg's Archives of Pharmacology
            issn:
               1432-1912
               0028-1298
            volumeNumber:317
            type:
               Periodical
               PublicationVolume
         publisher:
            name:Springer-Verlag
            logo:
               url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
               type:ImageObject
            type:Organization
         author:
               name:H. Glossmann
               affiliation:
                     name:Rudolf-Buchheim-Institut für Pharmakologie
                     address:
                        name:Rudolf-Buchheim-Institut für Pharmakologie, Giessen, Federal Republic of Germany
                        type:PostalAddress
                     type:Organization
               type:Person
               name:P. Presek
               affiliation:
                     name:Rudolf-Buchheim-Institut für Pharmakologie
                     address:
                        name:Rudolf-Buchheim-Institut für Pharmakologie, Giessen, Federal Republic of Germany
                        type:PostalAddress
                     type:Organization
               type:Person
               name:E. Eigenbrodt
               affiliation:
                     name:Institut für Biochemie und Endokrinologie
                     address:
                        name:Institut für Biochemie und Endokrinologie, Giessen, Federal Republic of Germany
                        type:PostalAddress
                     type:Organization
               type:Person
         isAccessibleForFree:
         hasPart:
            isAccessibleForFree:
            cssSelector:.main-content
            type:WebPageElement
         type:ScholarlyArticle
      context:https://schema.org
ScholarlyArticle:
      headline:Quercetin inhibits tyrosine phosphorylation by the cyclic nucleotide-independent, transforming protein kinase, pp60src
      description:The bioflavonoid quercetin is a potent inhibitor of a cyclic nucleotide-independent, tumor virus-coded protein kinase which phosphorylates tyrosine residues and acts as a cellular transforming protein. Half-maximal inhibition of the protein kinase occurred at 3–4 μM quercetin whereas rutin was much less effective. The finding, that quercetin inhibits a cyclic nucleotide-independent protein kinase activity, may provide clues to the diverse pharmacological effects of the bioflavonoids.
      datePublished:
      dateModified:
      pageStart:100
      pageEnd:102
      sameAs:https://doi.org/10.1007/BF00506266
      keywords:
         Quercetin
         Tyrosine Phosphorylation
         Protein kinase activity
         Tumor virus
         Flavonoids
         Pharmacology/Toxicology
         Neurosciences
      image:
      isPartOf:
         name:Naunyn-Schmiedeberg's Archives of Pharmacology
         issn:
            1432-1912
            0028-1298
         volumeNumber:317
         type:
            Periodical
            PublicationVolume
      publisher:
         name:Springer-Verlag
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:H. Glossmann
            affiliation:
                  name:Rudolf-Buchheim-Institut für Pharmakologie
                  address:
                     name:Rudolf-Buchheim-Institut für Pharmakologie, Giessen, Federal Republic of Germany
                     type:PostalAddress
                  type:Organization
            type:Person
            name:P. Presek
            affiliation:
                  name:Rudolf-Buchheim-Institut für Pharmakologie
                  address:
                     name:Rudolf-Buchheim-Institut für Pharmakologie, Giessen, Federal Republic of Germany
                     type:PostalAddress
                  type:Organization
            type:Person
            name:E. Eigenbrodt
            affiliation:
                  name:Institut für Biochemie und Endokrinologie
                  address:
                     name:Institut für Biochemie und Endokrinologie, Giessen, Federal Republic of Germany
                     type:PostalAddress
                  type:Organization
            type:Person
      isAccessibleForFree:
      hasPart:
         isAccessibleForFree:
         cssSelector:.main-content
         type:WebPageElement
["Periodical","PublicationVolume"]:
      name:Naunyn-Schmiedeberg's Archives of Pharmacology
      issn:
         1432-1912
         0028-1298
      volumeNumber:317
Organization:
      name:Springer-Verlag
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:Rudolf-Buchheim-Institut für Pharmakologie
      address:
         name:Rudolf-Buchheim-Institut für Pharmakologie, Giessen, Federal Republic of Germany
         type:PostalAddress
      name:Rudolf-Buchheim-Institut für Pharmakologie
      address:
         name:Rudolf-Buchheim-Institut für Pharmakologie, Giessen, Federal Republic of Germany
         type:PostalAddress
      name:Institut für Biochemie und Endokrinologie
      address:
         name:Institut für Biochemie und Endokrinologie, Giessen, Federal Republic of Germany
         type:PostalAddress
ImageObject:
      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
Person:
      name:H. Glossmann
      affiliation:
            name:Rudolf-Buchheim-Institut für Pharmakologie
            address:
               name:Rudolf-Buchheim-Institut für Pharmakologie, Giessen, Federal Republic of Germany
               type:PostalAddress
            type:Organization
      name:P. Presek
      affiliation:
            name:Rudolf-Buchheim-Institut für Pharmakologie
            address:
               name:Rudolf-Buchheim-Institut für Pharmakologie, Giessen, Federal Republic of Germany
               type:PostalAddress
            type:Organization
      name:E. Eigenbrodt
      affiliation:
            name:Institut für Biochemie und Endokrinologie
            address:
               name:Institut für Biochemie und Endokrinologie, Giessen, Federal Republic of Germany
               type:PostalAddress
            type:Organization
PostalAddress:
      name:Rudolf-Buchheim-Institut für Pharmakologie, Giessen, Federal Republic of Germany
      name:Rudolf-Buchheim-Institut für Pharmakologie, Giessen, Federal Republic of Germany
      name:Institut für Biochemie und Endokrinologie, Giessen, Federal Republic of Germany
WebPageElement:
      isAccessibleForFree:
      cssSelector:.main-content

External Links {🔗}(39)

Analytics and Tracking {📊}

  • Google Tag Manager

Libraries {📚}

  • Clipboard.js
  • Prism.js

CDN Services {📦}

  • Crossref

4.59s.