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/s00018-006-6167-7.

Title:
Lipid flippases and their biological functions | Cellular and Molecular Life Sciences
Description:
The typically distinct phospholipid composition of the two leaflets of a membrane bilayer is generated and maintained by bi-directional transport (flip-flop) of lipids between the leaflets. Specific membrane proteins, termed lipid flippases, play an essential role in this transport process. Energy-independent flippases allow common phospholipids to equilibrate rapidly between the two monolayers and also play a role in the biosynthesis of a variety of glycoconjugates such as glycosphingolipids, N-glycoproteins, and glycosylphosphatidylinositol (GPI)-anchored proteins. ATP-dependent flippases, including members of a conserved subfamily of P-type ATPases and ATP-binding cassette transporters, mediate the net transfer of specific phospholipids to one leaflet of a membrane and are involved in the creation and maintenance of transbilayer lipid asymmetry of membranes such as the plasma membrane of eukaryotes. Energy-dependent flippases also play a role in the biosynthesis of glycoconjugates such as bacterial lipopolysaccharide. This review summarizes recent progress on the identification and characterization of the various flippases and the demonstration of their biological functions.
Website Age:
28 years and 1 months (reg. 1997-05-29).

Matching Content Categories {📚}

  • Telecommunications
  • Mobile Technology & AI
  • Books & Literature

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're unsure if the website is profiting.

Not every website is profit-driven; some are created to spread information or serve as an online presence. Websites can be made for many 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 {🔍}

article, membrane, lipid, flippases, privacy, cookies, content, information, publish, search, biological, pomorski, access, data, log, journal, research, life, functions, menon, phospholipid, flipflop, proteins, play, role, phospholipids, asymmetry, membranes, discover, author, springer, essential, optional, personal, including, parties, policy, find, track, cellular, molecular, sciences, cmls, review, published, november, cite, explore, leaflets, bilayer,

Topics {✒️}

p-type atpases lipid flip-flop transbilayer lipid asymmetry specific membrane proteins month download article/chapter atp-binding cassette transporters flip-flop termed lipid flippases n-glycoproteins privacy choices/manage cookies membrane bilayer plasma membrane full article pdf biology/biophysics atp-dependent flippases lipid flippases check access instant access membrane european economic area scope submit manuscript related subjects weill medical college energy-independent flippases energy-dependent flippases conditions privacy policy author correspondence bi-directional transport specific phospholipids lipid bilayer anchored proteins biological functions accepting optional cookies common phospholipids main content log lipids humboldt university berlin journal finder publish article cellular 1007/s00018-006-6167-7 keywords membranes life sci privacy policy personal data article log books a optional cookies article cite article pomorski information

Schema {🗺️}

WebPage:
      mainEntity:
         headline:Lipid flippases and their biological functions
         description:The typically distinct phospholipid composition of the two leaflets of a membrane bilayer is generated and maintained by bi-directional transport (flip-flop) of lipids between the leaflets. Specific membrane proteins, termed lipid flippases, play an essential role in this transport process. Energy-independent flippases allow common phospholipids to equilibrate rapidly between the two monolayers and also play a role in the biosynthesis of a variety of glycoconjugates such as glycosphingolipids, N-glycoproteins, and glycosylphosphatidylinositol (GPI)-anchored proteins. ATP-dependent flippases, including members of a conserved subfamily of P-type ATPases and ATP-binding cassette transporters, mediate the net transfer of specific phospholipids to one leaflet of a membrane and are involved in the creation and maintenance of transbilayer lipid asymmetry of membranes such as the plasma membrane of eukaryotes. Energy-dependent flippases also play a role in the biosynthesis of glycoconjugates such as bacterial lipopolysaccharide. This review summarizes recent progress on the identification and characterization of the various flippases and the demonstration of their biological functions.
         datePublished:2006-11-13T00:00:00Z
         dateModified:2006-11-13T00:00:00Z
         pageStart:2908
         pageEnd:2921
         sameAs:https://doi.org/10.1007/s00018-006-6167-7
         keywords:
            Membrane assembly
            membrane asymmetry
            lipid flip-flop
            N-glycosylation
            ABC transporter
            P-type ATPase
            scramblase
            vesicle budding
            Cell Biology
            Biomedicine
            general
            Life Sciences
            Biochemistry
         image:
         isPartOf:
            name:Cellular and Molecular Life Sciences CMLS
            issn:
               1420-9071
               1420-682X
            volumeNumber:63
            type:
               Periodical
               PublicationVolume
         publisher:
            name:Birkhäuser-Verlag
            logo:
               url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
               type:ImageObject
            type:Organization
         author:
               name:T. Pomorski
               affiliation:
                     name:Humboldt University Berlin
                     address:
                        name:Institute of Biology/Biophysics, Humboldt University Berlin, Berlin, Germany
                        type:PostalAddress
                     type:Organization
               email:[email protected]
               type:Person
               name:A. K. Menon
               affiliation:
                     name:Weill Medical College of Cornell University
                     address:
                        name:Department of Biochemistry, Weill Medical College of Cornell University, New York, USA
                        type:PostalAddress
                     type:Organization
               type:Person
         isAccessibleForFree:
         hasPart:
            isAccessibleForFree:
            cssSelector:.main-content
            type:WebPageElement
         type:ScholarlyArticle
      context:https://schema.org
ScholarlyArticle:
      headline:Lipid flippases and their biological functions
      description:The typically distinct phospholipid composition of the two leaflets of a membrane bilayer is generated and maintained by bi-directional transport (flip-flop) of lipids between the leaflets. Specific membrane proteins, termed lipid flippases, play an essential role in this transport process. Energy-independent flippases allow common phospholipids to equilibrate rapidly between the two monolayers and also play a role in the biosynthesis of a variety of glycoconjugates such as glycosphingolipids, N-glycoproteins, and glycosylphosphatidylinositol (GPI)-anchored proteins. ATP-dependent flippases, including members of a conserved subfamily of P-type ATPases and ATP-binding cassette transporters, mediate the net transfer of specific phospholipids to one leaflet of a membrane and are involved in the creation and maintenance of transbilayer lipid asymmetry of membranes such as the plasma membrane of eukaryotes. Energy-dependent flippases also play a role in the biosynthesis of glycoconjugates such as bacterial lipopolysaccharide. This review summarizes recent progress on the identification and characterization of the various flippases and the demonstration of their biological functions.
      datePublished:2006-11-13T00:00:00Z
      dateModified:2006-11-13T00:00:00Z
      pageStart:2908
      pageEnd:2921
      sameAs:https://doi.org/10.1007/s00018-006-6167-7
      keywords:
         Membrane assembly
         membrane asymmetry
         lipid flip-flop
         N-glycosylation
         ABC transporter
         P-type ATPase
         scramblase
         vesicle budding
         Cell Biology
         Biomedicine
         general
         Life Sciences
         Biochemistry
      image:
      isPartOf:
         name:Cellular and Molecular Life Sciences CMLS
         issn:
            1420-9071
            1420-682X
         volumeNumber:63
         type:
            Periodical
            PublicationVolume
      publisher:
         name:Birkhäuser-Verlag
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:T. Pomorski
            affiliation:
                  name:Humboldt University Berlin
                  address:
                     name:Institute of Biology/Biophysics, Humboldt University Berlin, Berlin, Germany
                     type:PostalAddress
                  type:Organization
            email:[email protected]
            type:Person
            name:A. K. Menon
            affiliation:
                  name:Weill Medical College of Cornell University
                  address:
                     name:Department of Biochemistry, Weill Medical College of Cornell University, New York, USA
                     type:PostalAddress
                  type:Organization
            type:Person
      isAccessibleForFree:
      hasPart:
         isAccessibleForFree:
         cssSelector:.main-content
         type:WebPageElement
["Periodical","PublicationVolume"]:
      name:Cellular and Molecular Life Sciences CMLS
      issn:
         1420-9071
         1420-682X
      volumeNumber:63
Organization:
      name:Birkhäuser-Verlag
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:Humboldt University Berlin
      address:
         name:Institute of Biology/Biophysics, Humboldt University Berlin, Berlin, Germany
         type:PostalAddress
      name:Weill Medical College of Cornell University
      address:
         name:Department of Biochemistry, Weill Medical College of Cornell University, New York, USA
         type:PostalAddress
ImageObject:
      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
Person:
      name:T. Pomorski
      affiliation:
            name:Humboldt University Berlin
            address:
               name:Institute of Biology/Biophysics, Humboldt University Berlin, Berlin, Germany
               type:PostalAddress
            type:Organization
      email:[email protected]
      name:A. K. Menon
      affiliation:
            name:Weill Medical College of Cornell University
            address:
               name:Department of Biochemistry, Weill Medical College of Cornell University, New York, USA
               type:PostalAddress
            type:Organization
PostalAddress:
      name:Institute of Biology/Biophysics, Humboldt University Berlin, Berlin, Germany
      name:Department of Biochemistry, Weill Medical College of Cornell University, New York, USA
WebPageElement:
      isAccessibleForFree:
      cssSelector:.main-content

External Links {🔗}(27)

Analytics and Tracking {📊}

  • Google Tag Manager

Libraries {📚}

  • Clipboard.js
  • Prism.js

CDN Services {📦}

  • Crossref

4.23s.