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We began analyzing https://link.springer.com/protocol/10.1007/978-1-60761-376-3_4, but it redirected us to https://link.springer.com/protocol/10.1007/978-1-60761-376-3_4. The analysis below is for the second page.

Title[redir]:
Jasplakinolide: An Actin-Specific Reagent that Promotes Actin Polymerization | SpringerLink
Description:
Jasplakinolide, a cyclo-depsipeptide is a commonly used actin filament polymerizing and stabilizing drug. The substance has originally been isolated from a marine sponge, and can now be synthesized and has become commercially available. This, together with the...

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  • Education
  • Telecommunications
  • Science

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Custom-built

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πŸ™οΈ Massive Traffic: 50M - 100M visitors per month


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

Keywords {πŸ”}

google, scholar, article, cas, actin, pubmed, cell, jasplakinolide, cytoskeleton, biol, cells, polymerization, chem, methods, marine, sponge, holzinger, filaments, crews, filament, apoptosis, phalloidin, motil, mol, jaspamide, privacy, cookies, content, information, publish, protocols, protocol, stabilizing, stabilization, effects, sci, inhibits, lett, factin, jaspis, search, promotes, biology, membrane, chapter, access, micrasterias, duncan, induces, formation,

Topics {βœ’οΈ}

actin-targeting natural products springer science+business media na-k-2cl cotransport myosin-ii-dependent localization oriented actin-filament bundles potent actin-targeting jaspamide actin stabilizing agent privacy choices/manage cookies focal adhesion kinase actin-specific reagent actin stabilizing drugs cell polarity revealed membrane raft proteins actin cytoskeletal derangement induces actin polymerization potent anticancer drug journal finder publish competitive binding capacities humana press actin filament polymerizing actin filament fragments cytotoxic natural product protease-dependent pathway promotes actin polymerization actin polymerization promotes actin-perturbing substances f-actin aggregates actin inhibitor misakinolide european economic area epithelial cl- secretion fluid-phase markers suspension-cultured tobacco crane-fly spermatocytes cortical granule exocytosis renal ischemia/reperfusion pure metabolites obtained trigger fibroblast polarization micrasterias denticulata brΓ©b micrasterias denticulata visualized actin filament stabilization golgi cisternae morphology intra-golgi ph trans-golgi network lewis lung carcinoma conditions privacy policy green alga micrasterias f-actin stabilization lacrimal acinar cells jaspamide inhibits ruffling human prostate carcinoma

Schema {πŸ—ΊοΈ}

ScholarlyArticle:
      headline:Jasplakinolide: An Actin-Specific Reagent that Promotes Actin Polymerization
      pageEnd:87
      pageStart:71
      image:https://media.springernature.com/w153/springer-static/cover/book/978-1-60761-376-3.jpg
      genre:
         Springer Protocols
      isPartOf:
         name:Cytoskeleton Methods and Protocols
         isbn:
            978-1-60761-376-3
            978-1-60761-375-6
         type:Book
      publisher:
         name:Humana Press
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:Andreas Holzinger
            affiliation:
                  name:University of Innsbruck
                  address:
                     name:Institute of Botany, Department of Physiology and Cell Physiology, University of Innsbruck, Innsbruck, Austria
                     type:PostalAddress
                  type:Organization
            type:Person
      keywords:Actin filaments, Chondramides, Cytochalasins, Depsipeptide, Jasplakinolide, Latrunculin, Phalloidin
      description:Jasplakinolide, a cyclo-depsipeptide is a commonly used actin filament polymerizing and stabilizing drug. The substance has originally been isolated from a marine sponge, and can now be synthesized and has become commercially available. This, together with the benefit that jasplakinolide is membrane permeable has made it a commonly used tool in cell biology, when actin filament stabilization or polymerization has to be achieved. This may either be the case in studies on morphogenesis, motility, organelle movement, or when apoptosis has to be induced. Its use as a potent anticancer drug is discussed. The direct action on actin filaments may have further consequences in golgi body and membrane raft protein organization. In this chapter, the visualization of jasplaklinolide effects by different fluorescent and transmission electron microscopic methods is described. As competitive binding capacities of jasplakinolide and phalloidin make the detection of actin filaments by fluorescently labeled phalloidin problematic, alternatives are given here.
      datePublished:2009
      isAccessibleForFree:
      hasPart:
         isAccessibleForFree:
         cssSelector:.main-content
         type:WebPageElement
      context:https://schema.org
Book:
      name:Cytoskeleton Methods and Protocols
      isbn:
         978-1-60761-376-3
         978-1-60761-375-6
Organization:
      name:Humana Press
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:University of Innsbruck
      address:
         name:Institute of Botany, Department of Physiology and Cell Physiology, University of Innsbruck, Innsbruck, Austria
         type:PostalAddress
ImageObject:
      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
Person:
      name:Andreas Holzinger
      affiliation:
            name:University of Innsbruck
            address:
               name:Institute of Botany, Department of Physiology and Cell Physiology, University of Innsbruck, Innsbruck, Austria
               type:PostalAddress
            type:Organization
PostalAddress:
      name:Institute of Botany, Department of Physiology and Cell Physiology, University of Innsbruck, Innsbruck, Austria
WebPageElement:
      isAccessibleForFree:
      cssSelector:.main-content

External Links {πŸ”—}(205)

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