Here's how DOI.ORG makes money* and how much!

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

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. Schema
  9. External Links
  10. Analytics And Tracking
  11. Libraries
  12. Hosting Providers
  13. CDN Services

We began analyzing https://link.springer.com/article/10.1007/BF00232676, but it redirected us to https://link.springer.com/article/10.1007/BF00232676. The analysis below is for the second page.

Title[redir]:
Lipids in biological membrane fusion | The Journal of Membrane Biology
Description:
The results reviewed suggest that membrane fusion in diverse biological fusion reactions involves formation of some specific intermediates: stalks and pores. Energy of these intermediates and, consequently, the rate and extent of fusion depend on the propensity of the corresponding monolayers of membranes to bend in the required directions. Proteins and peptides can control the bending energy of membrane monolayers in a number of ways. Monolayer lipid composition may be altered by different phospholipases [50, 85, 90], flipases and translocases [4, 50]. Proteins and peptides can change monolayer spontaneous curvature or hydrophobic void energy by direct interaction with membrane lipids [20, 32, 111]. Proteins may also provide some barriers for lipid diffusion in the plane of the monolayer [83, 141]. If diffusion of lipids at some specific membrane sites (e.g., in the vicinity of fusion protein) is somehow hindered, the energy of the bent fusion intermediates would reflect the elastic properties of these particular sites rather than the spontaneous curvature of the whole monolayers. Proteins may deform membranes while bringing them locally into close contact. The alteration of the geometric (external) curvature will certainly change the elastic energy of the initial state and, thus affect the energetic barriers of the formation of the intermediates [143]. In addition, the area and the energy of the stalk can be reduced by preliminary bending of the contacting membranes [111]. The possible effects of proteins and polymers on local elastic properties and local shapes of the membranes have been recently analyzed [22, 39, 45, 63]. These studies may provide a good basis for future development of theoretical models of protein-mediated fusion. Various models for biological fusion have been presented as hypothetical sequences of intermediate conformations of proteins, with membrane lipids just covering the empty spaces between the proteins. Although the results discussed above do not allow us to draw an allexplaining cartoon of the fusion mechanism, they do indicate which properties of membrane lipid bilayers (if modified by fusion proteins) would get these bilayers to fuse. In addition, these data suggest a specific geometry to bent fusion intermediates (stalks and pores) and imply a contribution by lipids to the energy of these intermediates. We think that the synthesis of rapidly developing structural information on fusion proteins with the analysis of the physics of membrane rearrangement may soon yield a real understanding of the fascinating and fundamental phenomenon of membrane fusion.

Matching Content Categories {📚}

  • Education
  • Science
  • Fitness & Wellness

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?

🏙️ Massive Traffic: 50M - 100M visitors per month


Based on our best estimate, this website will receive around 80,479,999 visitors per month in the current month.

check SE Ranking
check Ahrefs
check Similarweb
check Ubersuggest
check Semrush

How Does Doi.org Make Money? {💸}

We see no obvious way the site makes money.

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, biophys, membrane, fusion, article, biol, zimmerberg, biochemistry, chernomordik, kozlov, lipids, sci, cell, chem, acad, epand, proteins, nature, phys, biochim, acta, membranes, usa, proc, natl, cas, markin, biological, intermediates, energy, wilschut, pubmed, cohen, yeagle, lipid, leikin, melikyan, helfrich, privacy, cookies, content, information, journal, access, almers, vogel, annu, rev, white,

Topics {✒️}

month download article/chapter biological membrane fusion privacy choices/manage cookies membrane lipid bilayers lipid droplet membranes bent fusion intermediates full article pdf membrane biology aims monolayer lipid composition biological fusion protein-mediated fusion biological membranes specific membrane sites membrane fusion conditions privacy policy alvarez de toledo check access instant access fusion mechanism membrane lipids [20 membrane lipids accepting optional cookies european economic area results reviewed suggest spontaneous curvature preliminary bending previously unpublished results scope submit manuscript freie universitat berlin main content log bending energy hydrophobic void energy colloid interface sci local elastic properties journal finder publish fusion protein membrane rearrangement membrane fluidity membrane biol fusion depend article log membrane monolayers article chernomordik initial state related subjects fusion proteins specific intermediates lipid diffusion privacy policy deform membranes

Schema {🗺️}

WebPage:
      mainEntity:
         headline:Lipids in biological membrane fusion
         description:The results reviewed suggest that membrane fusion in diverse biological fusion reactions involves formation of some specific intermediates: stalks and pores. Energy of these intermediates and, consequently, the rate and extent of fusion depend on the propensity of the corresponding monolayers of membranes to bend in the required directions. Proteins and peptides can control the bending energy of membrane monolayers in a number of ways. Monolayer lipid composition may be altered by different phospholipases [50, 85, 90], flipases and translocases [4, 50]. Proteins and peptides can change monolayer spontaneous curvature or hydrophobic void energy by direct interaction with membrane lipids [20, 32, 111]. Proteins may also provide some barriers for lipid diffusion in the plane of the monolayer [83, 141]. If diffusion of lipids at some specific membrane sites (e.g., in the vicinity of fusion protein) is somehow hindered, the energy of the bent fusion intermediates would reflect the elastic properties of these particular sites rather than the spontaneous curvature of the whole monolayers. Proteins may deform membranes while bringing them locally into close contact. The alteration of the geometric (external) curvature will certainly change the elastic energy of the initial state and, thus affect the energetic barriers of the formation of the intermediates [143]. In addition, the area and the energy of the stalk can be reduced by preliminary bending of the contacting membranes [111]. The possible effects of proteins and polymers on local elastic properties and local shapes of the membranes have been recently analyzed [22, 39, 45, 63]. These studies may provide a good basis for future development of theoretical models of protein-mediated fusion. Various models for biological fusion have been presented as hypothetical sequences of intermediate conformations of proteins, with membrane lipids just covering the empty spaces between the proteins. Although the results discussed above do not allow us to draw an allexplaining cartoon of the fusion mechanism, they do indicate which properties of membrane lipid bilayers (if modified by fusion proteins) would get these bilayers to fuse. In addition, these data suggest a specific geometry to bent fusion intermediates (stalks and pores) and imply a contribution by lipids to the energy of these intermediates. We think that the synthesis of rapidly developing structural information on fusion proteins with the analysis of the physics of membrane rearrangement may soon yield a real understanding of the fascinating and fundamental phenomenon of membrane fusion.
         datePublished:
         dateModified:
         pageStart:1
         pageEnd:14
         sameAs:https://doi.org/10.1007/BF00232676
         keywords:
            Membrane fusion
            Lipid bilayer
            Bending elasticity
            Fusion intermediates
            Lysolipid
            Exocytosis
            Biochemistry
            general
            Human Physiology
         image:
         isPartOf:
            name:The Journal of Membrane Biology
            issn:
               1432-1424
               0022-2631
            volumeNumber:146
            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:L. Chernomordik
               affiliation:
                     name:Laboratory of Theoretical and Physical Biology, National Institute of Child Health and Human Development, National Institutes of Health
                     address:
                        name:Laboratory of Theoretical and Physical Biology, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda
                        type:PostalAddress
                     type:Organization
               type:Person
               name:M. M. Kozlov
               affiliation:
                     name:FB Physik, Freie Universitat Berlin
                     address:
                        name:FB Physik, Freie Universitat Berlin, Berlin, Germany
                        type:PostalAddress
                     type:Organization
               type:Person
               name:J. Zimmerberg
               affiliation:
                     name:Laboratory of Theoretical and Physical Biology, National Institute of Child Health and Human Development, National Institutes of Health
                     address:
                        name:Laboratory of Theoretical and Physical Biology, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda
                        type:PostalAddress
                     type:Organization
               type:Person
         isAccessibleForFree:
         hasPart:
            isAccessibleForFree:
            cssSelector:.main-content
            type:WebPageElement
         type:ScholarlyArticle
      context:https://schema.org
ScholarlyArticle:
      headline:Lipids in biological membrane fusion
      description:The results reviewed suggest that membrane fusion in diverse biological fusion reactions involves formation of some specific intermediates: stalks and pores. Energy of these intermediates and, consequently, the rate and extent of fusion depend on the propensity of the corresponding monolayers of membranes to bend in the required directions. Proteins and peptides can control the bending energy of membrane monolayers in a number of ways. Monolayer lipid composition may be altered by different phospholipases [50, 85, 90], flipases and translocases [4, 50]. Proteins and peptides can change monolayer spontaneous curvature or hydrophobic void energy by direct interaction with membrane lipids [20, 32, 111]. Proteins may also provide some barriers for lipid diffusion in the plane of the monolayer [83, 141]. If diffusion of lipids at some specific membrane sites (e.g., in the vicinity of fusion protein) is somehow hindered, the energy of the bent fusion intermediates would reflect the elastic properties of these particular sites rather than the spontaneous curvature of the whole monolayers. Proteins may deform membranes while bringing them locally into close contact. The alteration of the geometric (external) curvature will certainly change the elastic energy of the initial state and, thus affect the energetic barriers of the formation of the intermediates [143]. In addition, the area and the energy of the stalk can be reduced by preliminary bending of the contacting membranes [111]. The possible effects of proteins and polymers on local elastic properties and local shapes of the membranes have been recently analyzed [22, 39, 45, 63]. These studies may provide a good basis for future development of theoretical models of protein-mediated fusion. Various models for biological fusion have been presented as hypothetical sequences of intermediate conformations of proteins, with membrane lipids just covering the empty spaces between the proteins. Although the results discussed above do not allow us to draw an allexplaining cartoon of the fusion mechanism, they do indicate which properties of membrane lipid bilayers (if modified by fusion proteins) would get these bilayers to fuse. In addition, these data suggest a specific geometry to bent fusion intermediates (stalks and pores) and imply a contribution by lipids to the energy of these intermediates. We think that the synthesis of rapidly developing structural information on fusion proteins with the analysis of the physics of membrane rearrangement may soon yield a real understanding of the fascinating and fundamental phenomenon of membrane fusion.
      datePublished:
      dateModified:
      pageStart:1
      pageEnd:14
      sameAs:https://doi.org/10.1007/BF00232676
      keywords:
         Membrane fusion
         Lipid bilayer
         Bending elasticity
         Fusion intermediates
         Lysolipid
         Exocytosis
         Biochemistry
         general
         Human Physiology
      image:
      isPartOf:
         name:The Journal of Membrane Biology
         issn:
            1432-1424
            0022-2631
         volumeNumber:146
         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:L. Chernomordik
            affiliation:
                  name:Laboratory of Theoretical and Physical Biology, National Institute of Child Health and Human Development, National Institutes of Health
                  address:
                     name:Laboratory of Theoretical and Physical Biology, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda
                     type:PostalAddress
                  type:Organization
            type:Person
            name:M. M. Kozlov
            affiliation:
                  name:FB Physik, Freie Universitat Berlin
                  address:
                     name:FB Physik, Freie Universitat Berlin, Berlin, Germany
                     type:PostalAddress
                  type:Organization
            type:Person
            name:J. Zimmerberg
            affiliation:
                  name:Laboratory of Theoretical and Physical Biology, National Institute of Child Health and Human Development, National Institutes of Health
                  address:
                     name:Laboratory of Theoretical and Physical Biology, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda
                     type:PostalAddress
                  type:Organization
            type:Person
      isAccessibleForFree:
      hasPart:
         isAccessibleForFree:
         cssSelector:.main-content
         type:WebPageElement
["Periodical","PublicationVolume"]:
      name:The Journal of Membrane Biology
      issn:
         1432-1424
         0022-2631
      volumeNumber:146
Organization:
      name:Springer-Verlag
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:Laboratory of Theoretical and Physical Biology, National Institute of Child Health and Human Development, National Institutes of Health
      address:
         name:Laboratory of Theoretical and Physical Biology, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda
         type:PostalAddress
      name:FB Physik, Freie Universitat Berlin
      address:
         name:FB Physik, Freie Universitat Berlin, Berlin, Germany
         type:PostalAddress
      name:Laboratory of Theoretical and Physical Biology, National Institute of Child Health and Human Development, National Institutes of Health
      address:
         name:Laboratory of Theoretical and Physical Biology, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda
         type:PostalAddress
ImageObject:
      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
Person:
      name:L. Chernomordik
      affiliation:
            name:Laboratory of Theoretical and Physical Biology, National Institute of Child Health and Human Development, National Institutes of Health
            address:
               name:Laboratory of Theoretical and Physical Biology, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda
               type:PostalAddress
            type:Organization
      name:M. M. Kozlov
      affiliation:
            name:FB Physik, Freie Universitat Berlin
            address:
               name:FB Physik, Freie Universitat Berlin, Berlin, Germany
               type:PostalAddress
            type:Organization
      name:J. Zimmerberg
      affiliation:
            name:Laboratory of Theoretical and Physical Biology, National Institute of Child Health and Human Development, National Institutes of Health
            address:
               name:Laboratory of Theoretical and Physical Biology, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda
               type:PostalAddress
            type:Organization
PostalAddress:
      name:Laboratory of Theoretical and Physical Biology, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda
      name:FB Physik, Freie Universitat Berlin, Berlin, Germany
      name:Laboratory of Theoretical and Physical Biology, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda
WebPageElement:
      isAccessibleForFree:
      cssSelector:.main-content

External Links {🔗}(233)

Analytics and Tracking {📊}

  • Google Tag Manager

Libraries {📚}

  • Clipboard.js
  • Prism.js

Emails and Hosting {✉️}

Mail Servers:

  • mx.zoho.eu
  • mx2.zoho.eu
  • mx3.zoho.eu

Name Servers:

  • josh.ns.cloudflare.com
  • zita.ns.cloudflare.com

CDN Services {📦}

  • Crossref

4.62s.