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/bf00769525.

Title:
Toward the molecular structure of the mitochondrial channel, VDAC | Journal of Bioenergetics and Biomembranes
Description:
A summary is presented of the most recent information about the structure and mechanism of closure of the mitochondrial channel, VDAC. Considerable information has come from studies involving electron microscopy of two-dimensional crystals and from electrophysiological studies of wild-type channels and site-directed mutants. Available evidence points to a Ξ²-barrel as the basic structural model for VDAC. Two models for voltage- or effector- induced closure have been proposed, the first involving removal of strands from the wall of the pore, the second invoking movement of protein domains into the lumen. Experimental strategies to resolve the actual mechanism are presented.
Website Age:
28 years and 1 months (reg. 1997-05-29).

Matching Content Categories {πŸ“š}

  • Education
  • Science
  • News & Politics

Content Management System {πŸ“}

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 {πŸ“ˆ}

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 7,642,828 visitors per month in the current month.

check SE Ranking
check Ahrefs
check Similarweb
check Ubersuggest
check Semrush

How Does Link.springer.com Make Money? {πŸ’Έ}

We find it hard to spot revenue streams.

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 could have a money-making trick up its sleeve, but it's undetectable for now.

Keywords {πŸ”}

google, scholar, colombini, mannella, biol, article, forte, biophys, mitochondrial, vdac, bioenerg, biomembr, membr, channel, channels, benz, biochim, acta, privacy, cookies, content, information, journal, research, electron, access, lett, blachlydyson, press, state, york, nature, publish, search, structure, microscopy, febs, peng, acad, sci, eds, guo, san, francisco, membrane, university, albany, london, chem, data,

Topics {βœ’οΈ}

2d membrane crystals site-directed mutants wild-type channels month download article/chapter electron microscopy society mitochondrial channel electron microscopy electron microscopic studies privacy choices/manage cookies voltage check access instant access full article pdf vdac minireview published dimensional crystals gating advanced biomedical research protein domains empire state plaza european economic area basic structural model related subjects american chemical society xiith international congress 42nd annual meeting conditions privacy policy accepting optional cookies effector- induced closure journal finder publish site san francisco press york state department article journal article mannella article log biomembranes article vdac structures privacy policy personal data blachly-dyson biomedical sciences article cite books a state university optional cookies manage preferences electrophysiological studies involving removal san francisco journal publish

Schema {πŸ—ΊοΈ}

WebPage:
      mainEntity:
         headline:Toward the molecular structure of the mitochondrial channel, VDAC
         description:A summary is presented of the most recent information about the structure and mechanism of closure of the mitochondrial channel, VDAC. Considerable information has come from studies involving electron microscopy of two-dimensional crystals and from electrophysiological studies of wild-type channels and site-directed mutants. Available evidence points to a Ξ²-barrel as the basic structural model for VDAC. Two models for voltage- or effector- induced closure have been proposed, the first involving removal of strands from the wall of the pore, the second invoking movement of protein domains into the lumen. Experimental strategies to resolve the actual mechanism are presented.
         datePublished:
         dateModified:
         pageStart:7
         pageEnd:19
         sameAs:https://doi.org/10.1007/BF00769525
         keywords:
            Mitochondrial outer membrane
            VDAC
            membrane channel
            voltage gating
            electron microscopy
            membrane crystals
            site-directed mutagenesis
            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:24
            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:Carmen A. Mannella
               affiliation:
                     name:New York State Department of Health
                     address:
                        name:Wadsworth Center for Laboratories and Research, New York State Department of Health, Albany
                        type:PostalAddress
                     type:Organization
                     name:State University of New York at Albany
                     address:
                        name:Department of Biomedical Sciences, School of Public Health, State University of New York at Albany, Albany
                        type:PostalAddress
                     type:Organization
               type:Person
               name:Michael Forte
               affiliation:
                     name:Oregon Health Sciences University
                     address:
                        name:Vollum Institute for Advanced Biomedical Research, Oregon Health Sciences University, Portland
                        type:PostalAddress
                     type:Organization
               type:Person
               name:Marco Colombini
               affiliation:
                     name:University of Maryland
                     address:
                        name:Laboratories of Cell Biology, Department of Zoology, University of Maryland, College Park
                        type:PostalAddress
                     type:Organization
               type:Person
         isAccessibleForFree:
         hasPart:
            isAccessibleForFree:
            cssSelector:.main-content
            type:WebPageElement
         type:ScholarlyArticle
      context:https://schema.org
ScholarlyArticle:
      headline:Toward the molecular structure of the mitochondrial channel, VDAC
      description:A summary is presented of the most recent information about the structure and mechanism of closure of the mitochondrial channel, VDAC. Considerable information has come from studies involving electron microscopy of two-dimensional crystals and from electrophysiological studies of wild-type channels and site-directed mutants. Available evidence points to a Ξ²-barrel as the basic structural model for VDAC. Two models for voltage- or effector- induced closure have been proposed, the first involving removal of strands from the wall of the pore, the second invoking movement of protein domains into the lumen. Experimental strategies to resolve the actual mechanism are presented.
      datePublished:
      dateModified:
      pageStart:7
      pageEnd:19
      sameAs:https://doi.org/10.1007/BF00769525
      keywords:
         Mitochondrial outer membrane
         VDAC
         membrane channel
         voltage gating
         electron microscopy
         membrane crystals
         site-directed mutagenesis
         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:24
         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:Carmen A. Mannella
            affiliation:
                  name:New York State Department of Health
                  address:
                     name:Wadsworth Center for Laboratories and Research, New York State Department of Health, Albany
                     type:PostalAddress
                  type:Organization
                  name:State University of New York at Albany
                  address:
                     name:Department of Biomedical Sciences, School of Public Health, State University of New York at Albany, Albany
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Michael Forte
            affiliation:
                  name:Oregon Health Sciences University
                  address:
                     name:Vollum Institute for Advanced Biomedical Research, Oregon Health Sciences University, Portland
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Marco Colombini
            affiliation:
                  name:University of Maryland
                  address:
                     name:Laboratories of Cell Biology, Department of Zoology, University of Maryland, College Park
                     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:24
Organization:
      name:Kluwer Academic Publishers-Plenum Publishers
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:New York State Department of Health
      address:
         name:Wadsworth Center for Laboratories and Research, New York State Department of Health, Albany
         type:PostalAddress
      name:State University of New York at Albany
      address:
         name:Department of Biomedical Sciences, School of Public Health, State University of New York at Albany, Albany
         type:PostalAddress
      name:Oregon Health Sciences University
      address:
         name:Vollum Institute for Advanced Biomedical Research, Oregon Health Sciences University, Portland
         type:PostalAddress
      name:University of Maryland
      address:
         name:Laboratories of Cell Biology, Department of Zoology, University of Maryland, College Park
         type:PostalAddress
ImageObject:
      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
Person:
      name:Carmen A. Mannella
      affiliation:
            name:New York State Department of Health
            address:
               name:Wadsworth Center for Laboratories and Research, New York State Department of Health, Albany
               type:PostalAddress
            type:Organization
            name:State University of New York at Albany
            address:
               name:Department of Biomedical Sciences, School of Public Health, State University of New York at Albany, Albany
               type:PostalAddress
            type:Organization
      name:Michael Forte
      affiliation:
            name:Oregon Health Sciences University
            address:
               name:Vollum Institute for Advanced Biomedical Research, Oregon Health Sciences University, Portland
               type:PostalAddress
            type:Organization
      name:Marco Colombini
      affiliation:
            name:University of Maryland
            address:
               name:Laboratories of Cell Biology, Department of Zoology, University of Maryland, College Park
               type:PostalAddress
            type:Organization
PostalAddress:
      name:Wadsworth Center for Laboratories and Research, New York State Department of Health, Albany
      name:Department of Biomedical Sciences, School of Public Health, State University of New York at Albany, Albany
      name:Vollum Institute for Advanced Biomedical Research, Oregon Health Sciences University, Portland
      name:Laboratories of Cell Biology, Department of Zoology, University of Maryland, College Park
WebPageElement:
      isAccessibleForFree:
      cssSelector:.main-content

External Links {πŸ”—}(89)

Analytics and Tracking {πŸ“Š}

  • Google Tag Manager

Libraries {πŸ“š}

  • Clipboard.js
  • Prism.js

CDN Services {πŸ“¦}

  • Crossref

4.14s.