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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

We began analyzing https://link.springer.com/chapter/10.1007/978-3-642-80481-6_8, but it redirected us to https://link.springer.com/chapter/10.1007/978-3-642-80481-6_8. The analysis below is for the second page.

Title[redir]:
The IRS-Signaling System: A Network of Docking Proteins That Mediate Insulin and Cytokine Action | SpringerLink
Description:
The integration of multiple transmembrane signals is especially important during development and maintenance of the nervous system, communication between cells of the immune system, evolution of transformed cells, and metabolic control (Hunter 1997). Tyrosine...

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.

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How Does Doi.org Make Money? {💸}

We're unsure how the site profits.

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 cashing in, but we can't detect the method they're using.

Keywords {🔍}

google, scholar, cas, pubmed, insulin, receptor, biol, chem, white, cell, kinase, substrate, signaling, protein, irs, tyrosine, growth, phosphorylation, factor, myers, nature, sun, domain, kahn, phosphatidylinositol, mol, signal, proteins, cells, domains, insulinlike, transduction, chapter, yenush, activation, wang, van, role, pawson, schlessinger, pierce, interaction, phosphotyrosine, activity, receptors, phosphatase, kasuga, backer, science, sci,

Topics {✒️}

irsi-independent p21ras-gtp formation insulin-stimulated glucose transport insulin-induced glucose transport pdgf-stimulated membrane ruffling month download article/chapter gi-coupled receptor signaling insulin-receptor autophos- phorylation growth hormone interferon-gamma tyrosine phosphorylation-dependent manner freeman rm jr chemotactic peptide-induced stimulation protein-tyrosine-phosphatase shptp2 il-4-mediated irs-1 phosphorylation pdgf-activated phosphatidylinositol 3-kinase akt proto-oncogene serine/threonine phosphorylation obesity-induced insulin resistance phosphotyrosine phosphatase sh-ptp2 constitutively tyrosine-phosphorylated amino acid uptake insulin-stimulated ras activation insulin-stimulated glucose 3t3/l1 cells ras signaling pathways tumor necrosis factor privacy choices/manage cookies myers mg jr insulin receptor/irs-1 interaction protein-tyrosine-phosphatase protein-tyrosine phosphatase modulates insulin action multiple transmembrane signals multiple serine residues tumour necrosis factor controlling igf-receptor function consititutively active form tyrosine kinase activity tyrosine-phosphorylated peptides device instant download stat6 signaling molecules tyrosine phosphorylation plays mitogenic signaling induced protein-tyrosine kinase mitogenic tyrosine kinases insulin receptor substrate-1 insulin receptor substrate insulin receptor substrate-2 il-4 receptor region tyrosine phosphorylation sites growth factor-1 receptor

Questions {❓}

  • Morrison D (1994) 14–3–3: modulators of signaling proteins?

Schema {🗺️}

ScholarlyArticle:
      headline:The IRS-Signaling System: A Network of Docking Proteins That Mediate Insulin and Cytokine Action
      pageEnd:208
      pageStart:179
      image:https://media.springernature.com/w153/springer-static/cover/book/978-3-642-80481-6.jpg
      genre:
         Biomedical and Life Sciences
         Biomedical and Life Sciences (R0)
      isPartOf:
         name:Protein Modules in Signal Transduction
         isbn:
            978-3-642-80481-6
            978-3-642-80483-0
         type:Book
      publisher:
         name:Springer Berlin Heidelberg
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:M. F. White
            affiliation:
                  name:Joslin Diabetes Center
                  address:
                     name:Research Division, Joslin Diabetes Center, Boston, USA
                     type:PostalAddress
                  type:Organization
                  name:Harvard Medical School
                  address:
                     name:The Graduate Program in Biomedical and Biological Sciences, Harvard Medical School, Boston, USA
                     type:PostalAddress
                  type:Organization
            type:Person
            name:L. Yenush
            affiliation:
                  name:Joslin Diabetes Center
                  address:
                     name:Research Division, Joslin Diabetes Center, Boston, USA
                     type:PostalAddress
                  type:Organization
                  name:Harvard Medical School
                  address:
                     name:The Graduate Program in Biomedical and Biological Sciences, Harvard Medical School, Boston, USA
                     type:PostalAddress
                  type:Organization
            type:Person
      keywords:Insulin Receptor, Tyrosine Phosphorylation, Insulin Receptor Substrate, Insulin Stimulation, Docking Protein
      description:The integration of multiple transmembrane signals is especially important during development and maintenance of the nervous system, communication between cells of the immune system, evolution of transformed cells, and metabolic control (Hunter 1997). Tyrosine phosphorylation plays a key role in many of these processes by directly controlling the activity of receptors or enzymes at early steps in signaling cascades, or by the assembly of multicomponent signaling complexes around activated receptors or their cellular substrates (Pawson 1995). In most if not all cases, initialization of the signaling cascade controlled by growth factor and cytokine receptors originates with multisite tyrosine phosphorylation catalyzed directly by kinases activated during ligand-induced dimerization of specific membrane receptors (Schlessinger 1988; Helding 1995). In many cases, tyrosine autophosphorylation sites in activated receptors directly bind signaling proteins containing Src homology-2 domains (SH2 proteins). In other cases, tyrosine autophosphorylation increases the activity of the receptor kinase, which mediates tyrosine phosphorylation of cytosolic substrates or docking proteins that recruit SH2 proteins into multipotential signaling complexes (Myers and White 1995). The network is further elaborated through other modules which mediate protein-protein or protein-lipid interactions, including PTB, PDZ, SH3, WW, and PH domains.
      datePublished:1998
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Book:
      name:Protein Modules in Signal Transduction
      isbn:
         978-3-642-80481-6
         978-3-642-80483-0
Organization:
      name:Springer Berlin Heidelberg
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:Joslin Diabetes Center
      address:
         name:Research Division, Joslin Diabetes Center, Boston, USA
         type:PostalAddress
      name:Harvard Medical School
      address:
         name:The Graduate Program in Biomedical and Biological Sciences, Harvard Medical School, Boston, USA
         type:PostalAddress
      name:Joslin Diabetes Center
      address:
         name:Research Division, Joslin Diabetes Center, Boston, USA
         type:PostalAddress
      name:Harvard Medical School
      address:
         name:The Graduate Program in Biomedical and Biological Sciences, Harvard Medical School, Boston, USA
         type:PostalAddress
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      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
Person:
      name:M. F. White
      affiliation:
            name:Joslin Diabetes Center
            address:
               name:Research Division, Joslin Diabetes Center, Boston, USA
               type:PostalAddress
            type:Organization
            name:Harvard Medical School
            address:
               name:The Graduate Program in Biomedical and Biological Sciences, Harvard Medical School, Boston, USA
               type:PostalAddress
            type:Organization
      name:L. Yenush
      affiliation:
            name:Joslin Diabetes Center
            address:
               name:Research Division, Joslin Diabetes Center, Boston, USA
               type:PostalAddress
            type:Organization
            name:Harvard Medical School
            address:
               name:The Graduate Program in Biomedical and Biological Sciences, Harvard Medical School, Boston, USA
               type:PostalAddress
            type:Organization
PostalAddress:
      name:Research Division, Joslin Diabetes Center, Boston, USA
      name:The Graduate Program in Biomedical and Biological Sciences, Harvard Medical School, Boston, USA
      name:Research Division, Joslin Diabetes Center, Boston, USA
      name:The Graduate Program in Biomedical and Biological Sciences, Harvard Medical School, Boston, USA
WebPageElement:
      isAccessibleForFree:
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External Links {🔗}(522)

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