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/bf00812070.

Title:
The muscle ryanodine receptor and its intrinsic Ca2+ channel activity | Journal of Bioenergetics and Biomembranes
Description:
In skeletal and cardiac muscle, contraction is initiated by the rapid release of Ca2+ ions from the intracellular membrane system, sarcoplasmic reticulum. Rapid-mixing vesicle ion flux and planar lipid bilayer-single-channel measurements have shown that Ca2+ release is mediated by a high-conductance, ligand-gated Ca2+ channel. Using the Ca2+ release-specific probe ryanodine, a 30 S protein complex composed of four polypeptides ofM r ∼ 400,000 has been isolated. Reconstitution of the purified skeletal and cardiac muscle 30 S complexes into planar lipid bilayers induced single Ca2+ channel currents with conductance and gating kinetics similar to those of native Ca2+ release channels. Electron microscopy revealed structural similarity with the protein bridges (“feet”) that span the transverse-tubule-sarcoplasmic reticulum junction. These results suggest that striated muscle contains an intracellular Ca2+ release channel that is identical with the ryanodine receptor and the transverse-tubule-sarcoplasmic reticulum spanning feet structures.
Website Age:
28 years and 1 months (reg. 1997-05-29).

Matching Content Categories {📚}

  • Education
  • Health & Fitness
  • 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 figure out the monetization strategy.

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 might be plotting its profit, but the way they're doing it isn't detectable yet.

Keywords {🔍}

google, scholar, biol, meissner, biophys, chem, cell, fleischer, lai, article, rousseau, physiol, muscle, smith, channel, biochim, acta, biochem, inui, rev, ryanodine, liu, campbell, sutko, saito, privacy, cookies, content, journal, receptor, release, res, commun, coronado, jones, casida, nature, publish, search, skeletal, reticulum, ion, channels, access, physiology, brunschwig, caswell, franziniarmstrong, annu, fairhurst,

Topics {✒️}

transverse-tubule-sarcoplasmic reticulum junction ligand-gated ca2+ channel muscle ryanodine receptor month download article/chapter sarcoplasmic reticulum frog skeletal muscle cardiac muscle cardiac muscle 30 cell calcium 9 ryanodine receptor ca2+ release preserved ca2+ handling high intracellular [ca2+] excitation–contraction coupling privacy choices/manage cookies full article pdf related subjects rapid release check access instant access intracellular membrane system european economic area scope submit manuscript �feet” american physiological society conditions privacy policy protein complex composed gating kinetics similar ca2+ ions purified skeletal striated muscle muscle fibres accepting optional cookies journal finder publish main content log article journal article lai skeletal biomembranes article article log privacy policy personal data books a article cite optional cookies similar content manage preferences franzini-armstrong journal publish data protection

Schema {🗺️}

WebPage:
      mainEntity:
         headline:The muscle ryanodine receptor and its intrinsic Ca2+ channel activity
         description:In skeletal and cardiac muscle, contraction is initiated by the rapid release of Ca2+ ions from the intracellular membrane system, sarcoplasmic reticulum. Rapid-mixing vesicle ion flux and planar lipid bilayer-single-channel measurements have shown that Ca2+ release is mediated by a high-conductance, ligand-gated Ca2+ channel. Using the Ca2+ release-specific probe ryanodine, a 30 S protein complex composed of four polypeptides ofM r ∼ 400,000 has been isolated. Reconstitution of the purified skeletal and cardiac muscle 30 S complexes into planar lipid bilayers induced single Ca2+ channel currents with conductance and gating kinetics similar to those of native Ca2+ release channels. Electron microscopy revealed structural similarity with the protein bridges (“feet”) that span the transverse-tubule-sarcoplasmic reticulum junction. These results suggest that striated muscle contains an intracellular Ca2+ release channel that is identical with the ryanodine receptor and the transverse-tubule-sarcoplasmic reticulum spanning feet structures.
         datePublished:
         dateModified:
         pageStart:227
         pageEnd:246
         sameAs:https://doi.org/10.1007/BF00812070
         keywords:
            Skeletal muscle
            cardiac muscle
            ryanodine receptor
            Ca2+ release channel
            transverse tubule
            sarcoplasmic reticulum
            junctional feet
            Bioorganic Chemistry
            Biochemistry
            general
            Animal Anatomy / Morphology / Histology
            Animal Biochemistry
            Organic Chemistry
         image:
         isPartOf:
            name:Journal of Bioenergetics and Biomembranes
            issn:
               1573-6881
               0145-479X
            volumeNumber:21
            type:
               Periodical
               PublicationVolume
         publisher:
            name:Kluwer Academic Publishers-Plenum Publishers
            logo:
               url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
               type:ImageObject
            type:Organization
         author:
               name:F. Anthony Lai
               affiliation:
                     name:University of North Carolina
                     address:
                        name:Departments of Biochemistry and Physiology, School of Medicine, University of North Carolina, Chapel Hill
                        type:PostalAddress
                     type:Organization
               type:Person
               name:Gerhard Meissner
               affiliation:
                     name:University of North Carolina
                     address:
                        name:Departments of Biochemistry and Physiology, School of Medicine, University of North Carolina, Chapel Hill
                        type:PostalAddress
                     type:Organization
               type:Person
         isAccessibleForFree:
         hasPart:
            isAccessibleForFree:
            cssSelector:.main-content
            type:WebPageElement
         type:ScholarlyArticle
      context:https://schema.org
ScholarlyArticle:
      headline:The muscle ryanodine receptor and its intrinsic Ca2+ channel activity
      description:In skeletal and cardiac muscle, contraction is initiated by the rapid release of Ca2+ ions from the intracellular membrane system, sarcoplasmic reticulum. Rapid-mixing vesicle ion flux and planar lipid bilayer-single-channel measurements have shown that Ca2+ release is mediated by a high-conductance, ligand-gated Ca2+ channel. Using the Ca2+ release-specific probe ryanodine, a 30 S protein complex composed of four polypeptides ofM r ∼ 400,000 has been isolated. Reconstitution of the purified skeletal and cardiac muscle 30 S complexes into planar lipid bilayers induced single Ca2+ channel currents with conductance and gating kinetics similar to those of native Ca2+ release channels. Electron microscopy revealed structural similarity with the protein bridges (“feet”) that span the transverse-tubule-sarcoplasmic reticulum junction. These results suggest that striated muscle contains an intracellular Ca2+ release channel that is identical with the ryanodine receptor and the transverse-tubule-sarcoplasmic reticulum spanning feet structures.
      datePublished:
      dateModified:
      pageStart:227
      pageEnd:246
      sameAs:https://doi.org/10.1007/BF00812070
      keywords:
         Skeletal muscle
         cardiac muscle
         ryanodine receptor
         Ca2+ release channel
         transverse tubule
         sarcoplasmic reticulum
         junctional feet
         Bioorganic Chemistry
         Biochemistry
         general
         Animal Anatomy / Morphology / Histology
         Animal Biochemistry
         Organic Chemistry
      image:
      isPartOf:
         name:Journal of Bioenergetics and Biomembranes
         issn:
            1573-6881
            0145-479X
         volumeNumber:21
         type:
            Periodical
            PublicationVolume
      publisher:
         name:Kluwer Academic Publishers-Plenum Publishers
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:F. Anthony Lai
            affiliation:
                  name:University of North Carolina
                  address:
                     name:Departments of Biochemistry and Physiology, School of Medicine, University of North Carolina, Chapel Hill
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Gerhard Meissner
            affiliation:
                  name:University of North Carolina
                  address:
                     name:Departments of Biochemistry and Physiology, School of Medicine, University of North Carolina, Chapel Hill
                     type:PostalAddress
                  type:Organization
            type:Person
      isAccessibleForFree:
      hasPart:
         isAccessibleForFree:
         cssSelector:.main-content
         type:WebPageElement
["Periodical","PublicationVolume"]:
      name:Journal of Bioenergetics and Biomembranes
      issn:
         1573-6881
         0145-479X
      volumeNumber:21
Organization:
      name:Kluwer Academic Publishers-Plenum Publishers
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:University of North Carolina
      address:
         name:Departments of Biochemistry and Physiology, School of Medicine, University of North Carolina, Chapel Hill
         type:PostalAddress
      name:University of North Carolina
      address:
         name:Departments of Biochemistry and Physiology, School of Medicine, University of North Carolina, Chapel Hill
         type:PostalAddress
ImageObject:
      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
Person:
      name:F. Anthony Lai
      affiliation:
            name:University of North Carolina
            address:
               name:Departments of Biochemistry and Physiology, School of Medicine, University of North Carolina, Chapel Hill
               type:PostalAddress
            type:Organization
      name:Gerhard Meissner
      affiliation:
            name:University of North Carolina
            address:
               name:Departments of Biochemistry and Physiology, School of Medicine, University of North Carolina, Chapel Hill
               type:PostalAddress
            type:Organization
PostalAddress:
      name:Departments of Biochemistry and Physiology, School of Medicine, University of North Carolina, Chapel Hill
      name:Departments of Biochemistry and Physiology, School of Medicine, University of North Carolina, Chapel Hill
WebPageElement:
      isAccessibleForFree:
      cssSelector:.main-content

External Links {🔗}(114)

Analytics and Tracking {📊}

  • Google Tag Manager

Libraries {📚}

  • Clipboard.js
  • Prism.js

CDN Services {📦}

  • Crossref

4.48s.