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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
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We began analyzing https://link.springer.com/article/10.1007/s00109-009-0587-4, but it redirected us to https://link.springer.com/article/10.1007/s00109-009-0587-4. The analysis below is for the second page.

Title[redir]:
Dynamin 2 and human diseases | Journal of Molecular Medicine
Description:
Dynamin 2 (DNM2) mutations cause autosomal dominant centronuclear myopathy, a rare form of congenital myopathy, and intermediate and axonal forms of Charcot–Marie-Tooth disease, a peripheral neuropathy. DNM2 is a large GTPase mainly involved in membrane trafficking through its function in the formation and release of nascent vesicles from biological membranes. DNM2 participates in clathrin-dependent and clathrin-independent endocytosis and intracellular membrane trafficking (from endosomes and Golgi apparatus). Recent studies have also implicated DNM2 in exocytosis. DNM2 belongs to the machinery responsible for the formation of vesicles and regulates the cytoskeleton providing intracellular vesicle transport. In addition, DNM2 tightly interacts with and is involved in the regulation of actin and microtubule networks, independent from membrane trafficking processes. We summarize here the molecular, biochemical, and functional data on DNM2 and discuss the possible pathophysiological mechanisms via which DNM2 mutations can lead to two distinct neuromuscular disorders.

Matching Content Categories {📚}

  • Education
  • Telecommunications
  • Science

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?

🌠 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.
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How Does Doi.org Make Money? {💸}

We don't see any clear sign of profit-making.

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

Keywords {🔍}

google, scholar, pubmed, cas, dynamin, biol, cell, endocytosis, chem, mol, protein, sci, mcniven, regulates, myopathy, cells, article, domain, cao, guicheney, bitoun, membrane, actin, function, mutations, centronuclear, disease, trafficking, dnm, charcotmarietooth, human, prudhon, gtpase, interacts, nat, usa, schmid, vesicle, access, proc, natl, acad, chen, lee, biochem, role, res, durieux, vesicles, exocytosis,

Topics {✒️}

signal-responsive f-actin-binding protein axonal charcot–marie-tooth disease vegfr-2/kdr-mediated endothelial signaling charcot–marie-tooth disease charcot–marie-tooth neuropathy charcot–marie-tooth mutant synaptic vesicle endocytosis endosome-derived clathrin-coated vesicles month download article/chapter endothelial nitric-oxide synthase growth factor-stimulated cells regulates receptor-mediated endocytosis adaptor protein tks5/fish src kinase-sensitive complex fas ligand-mediated apoptosis src-induced dynamin-2 phosphorylation efficient clathrin-mediated endocytosis nitric-oxide synthase function defective excitation-contraction coupling groupe hospitalier pitié-salpêtrière late-onset alzheimer disease shank/prosap scaffolding proteins ap-1-positive endosomal trafficking dynamin-2-mediated slow endocytosis dynamin-1-dependent rapid endocytosis endocytic clathrin-coated pits nk cell-mediated cytotoxicity ubiquitously expressed dynamin-ii excitation-contraction coupling machinery aav-mediated intramuscular delivery occludin-based protein complexes splice-variant specific functions proline/arginine-rich domains focal adhesion kinase dominant centronuclear myopathy proteinuric kidney disease distinct neuromuscular disorders intracellular membrane trafficking autosomal centronuclear myopathy clathrin-mediated endocytosis related subjects anne-cécile durieux grb2 sh3 domain cortactin–dynamin complex sporadic centronuclear myopathy dynamin isoform-specific interaction human myotubular myopathy formin-binding protein 17 membrane trafficking processes isoform ubiquitously expressed

Schema {🗺️}

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         headline:Dynamin 2 and human diseases
         description:Dynamin 2 (DNM2) mutations cause autosomal dominant centronuclear myopathy, a rare form of congenital myopathy, and intermediate and axonal forms of Charcot–Marie-Tooth disease, a peripheral neuropathy. DNM2 is a large GTPase mainly involved in membrane trafficking through its function in the formation and release of nascent vesicles from biological membranes. DNM2 participates in clathrin-dependent and clathrin-independent endocytosis and intracellular membrane trafficking (from endosomes and Golgi apparatus). Recent studies have also implicated DNM2 in exocytosis. DNM2 belongs to the machinery responsible for the formation of vesicles and regulates the cytoskeleton providing intracellular vesicle transport. In addition, DNM2 tightly interacts with and is involved in the regulation of actin and microtubule networks, independent from membrane trafficking processes. We summarize here the molecular, biochemical, and functional data on DNM2 and discuss the possible pathophysiological mechanisms via which DNM2 mutations can lead to two distinct neuromuscular disorders.
         datePublished:2010-02-03T00:00:00Z
         dateModified:2010-02-03T00:00:00Z
         pageStart:339
         pageEnd:350
         sameAs:https://doi.org/10.1007/s00109-009-0587-4
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            Centronuclear myopathy
            Charcot–Marie-Tooth neuropathy
            Endocytosis
            Cytoskeleton
            Monogenic disease
            Biology
            Molecular Medicine
            Human Genetics
            Internal Medicine
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      headline:Dynamin 2 and human diseases
      description:Dynamin 2 (DNM2) mutations cause autosomal dominant centronuclear myopathy, a rare form of congenital myopathy, and intermediate and axonal forms of Charcot–Marie-Tooth disease, a peripheral neuropathy. DNM2 is a large GTPase mainly involved in membrane trafficking through its function in the formation and release of nascent vesicles from biological membranes. DNM2 participates in clathrin-dependent and clathrin-independent endocytosis and intracellular membrane trafficking (from endosomes and Golgi apparatus). Recent studies have also implicated DNM2 in exocytosis. DNM2 belongs to the machinery responsible for the formation of vesicles and regulates the cytoskeleton providing intracellular vesicle transport. In addition, DNM2 tightly interacts with and is involved in the regulation of actin and microtubule networks, independent from membrane trafficking processes. We summarize here the molecular, biochemical, and functional data on DNM2 and discuss the possible pathophysiological mechanisms via which DNM2 mutations can lead to two distinct neuromuscular disorders.
      datePublished:2010-02-03T00:00:00Z
      dateModified:2010-02-03T00:00:00Z
      pageStart:339
      pageEnd:350
      sameAs:https://doi.org/10.1007/s00109-009-0587-4
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         Centronuclear myopathy
         Charcot–Marie-Tooth neuropathy
         Endocytosis
         Cytoskeleton
         Monogenic disease
         Biology
         Molecular Medicine
         Human Genetics
         Internal Medicine
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                     name:Inserm, UMR S974, Institut de Myologie, Groupe Hospitalier Pitié-Salpêtrière, Paris, France
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         name:UPMC Univ Paris 06, Paris, France
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            address:
               name:UPMC Univ Paris 06, Paris, France
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            address:
               name:Inserm, UMR S956, Groupe Hospitalier Pitié-Salpêtrière, Paris, France
               type:PostalAddress
            type:Organization
      name:Marc Bitoun
      affiliation:
            name:Groupe Hospitalier Pitié-Salpêtrière
            address:
               name:Inserm, UMR S974, Institut de Myologie, Groupe Hospitalier Pitié-Salpêtrière, Paris, France
               type:PostalAddress
            type:Organization
            name:UPMC Univ Paris 06
            address:
               name:UPMC Univ Paris 06, Paris, France
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            name:Groupe Hospitalier Pitié-Salpêtrière
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               name:UMR_S974, Institut de Myologie, Groupe Hospitalier Pitié-Salpêtrière, Paris, France
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      name:UPMC Univ Paris 06, Paris, France
      name:UPMC Univ Paris 06, Paris, France
      name:Inserm, UMR S956, Groupe Hospitalier Pitié-Salpêtrière, Paris, France
      name:Inserm, UMR S974, Institut de Myologie, Groupe Hospitalier Pitié-Salpêtrière, Paris, France
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External Links {🔗}(454)

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Libraries {📚}

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Emails and Hosting {✉️}

Mail Servers:

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Name Servers:

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CDN Services {📦}

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