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

We are analyzing https://link.springer.com/article/10.1186/1471-2091-8-23.

Title:
The FTO (fat mass and obesity associated) gene codes for a novel member of the non-heme dioxygenase superfamily | BMC Biochemistry
Description:
Background Genetic variants in the FTO (fat mass and obesity associated) gene have been associated with an increased risk of obesity. However, the function of its protein product has not been experimentally studied and previously reported sequence similarity analyses suggested the absence of homologs in existing protein databases. Here, we present the first detailed computational analysis of the sequence and predicted structure of the protein encoded by FTO. Results We performed a sequence similarity search using the human FTO protein as query and then generated a profile using the multiple sequence alignment of the homologous sequences. Profile-to-sequence and profile-to-profile based comparisons identified remote homologs of the non-heme dioxygenase family. Conclusion Our analysis suggests that human FTO is a member of the non-heme dioxygenase (Fe(II)- and 2-oxoglutarate-dependent dioxygenases) superfamily. Amino acid conservation patterns support this hypothesis and indicate that both 2-oxoglutarate and iron should be important for FTO function. This computational prediction of the function of FTO should suggest further steps for its experimental characterization and help to formulate hypothesis about the mechanisms by which it relates to obesity in humans.
Website Age:
28 years and 1 months (reg. 1997-05-29).

Matching Content Categories {📚}

  • Science
  • Education
  • TV

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 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? {💸}

We can't see how the site brings in money.

The purpose of some websites isn't monetary gain; they're meant to inform, educate, or foster collaboration. Everyone has unique reasons for building websites. This could be an example. Link.springer.com has a secret sauce for making money, but we can't detect it yet.

Keywords {🔍}

fto, article, pubmed, protein, sequence, human, google, scholar, family, cas, function, gene, nonheme, analysis, obesity, alignment, structure, dioxygenase, amino, figure, sequences, information, mass, results, alkb, acids, bioinformatics, superfamily, localization, server, search, computational, generated, oxoglutarate, region, nuclear, web, central, authors, research, member, access, andradenavarro, homologs, multiple, homologous, dioxygenases, table, conserved, secondary,

Topics {✒️}

nuclear localization signal reverse dna/rna damage fold assignment results article sanchez-pulido luis sanchez-pulido article download pdf profile-based neural networks sequence similarity search dna-repair protein alkb nuclear-cytoplasmic localization de/hhpred] soding secondary structure predictions hypoxia-inducible factor-1alpha hhpred server fold recognition analyses profile-based sequence searches related web resources /r-rich region conserved n-terminal conserved region inducible nuclear translocation protein localization predictor nail-network analysis interface fto n-terminal region amino acid conservation fold recognition analysis protein cellular localization org/] sanchez-pulido privacy choices/manage cookies joint genome institute canada research chair authors’ original file andrade-navarro faculty hidden markov models dimensional protein structure full size image hypoxia-inducible factor andrade-navarro ma n-terminal region nat rev cancer predictprotein server [25 human abh3 structure signal transduction full access existing protein databases n-terminal extension amino acids involved heme dioxygenase superfamily identified sequences homologous nat chem biol blast server

Questions {❓}

  • Iyer LM, Aravind L, Coon SL, Klein DC, Koonin EV: Evolution of cell-cell signaling in animals: did late horizontal gene transfer from bacteria have a role?
  • Ozer A, Bruick RK: Non-heme dioxygenases: cellular sensors and regulators jelly rolled into one?

Schema {🗺️}

WebPage:
      mainEntity:
         headline:The FTO (fat mass and obesity associated) gene codes for a novel member of the non-heme dioxygenase superfamily
         description:Genetic variants in the FTO (fat mass and obesity associated) gene have been associated with an increased risk of obesity. However, the function of its protein product has not been experimentally studied and previously reported sequence similarity analyses suggested the absence of homologs in existing protein databases. Here, we present the first detailed computational analysis of the sequence and predicted structure of the protein encoded by FTO. We performed a sequence similarity search using the human FTO protein as query and then generated a profile using the multiple sequence alignment of the homologous sequences. Profile-to-sequence and profile-to-profile based comparisons identified remote homologs of the non-heme dioxygenase family. Our analysis suggests that human FTO is a member of the non-heme dioxygenase (Fe(II)- and 2-oxoglutarate-dependent dioxygenases) superfamily. Amino acid conservation patterns support this hypothesis and indicate that both 2-oxoglutarate and iron should be important for FTO function. This computational prediction of the function of FTO should suggest further steps for its experimental characterization and help to formulate hypothesis about the mechanisms by which it relates to obesity in humans.
         datePublished:2007-11-08T00:00:00Z
         dateModified:2007-11-08T00:00:00Z
         pageStart:1
         pageEnd:6
         license:http://creativecommons.org/licenses/by/2.0
         sameAs:https://doi.org/10.1186/1471-2091-8-23
         keywords:
            Nuclear Localization Signal
            Secondary Structure Prediction
            Bipartite Nuclear Localization Signal
            Fold Assignment
            HHpred Server
            Biochemistry
            general
            Life Sciences
         image:
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1186%2F1471-2091-8-23/MediaObjects/12858_2007_Article_166_Fig1_HTML.jpg
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1186%2F1471-2091-8-23/MediaObjects/12858_2007_Article_166_Fig2_HTML.jpg
         isPartOf:
            name:BMC Biochemistry
            issn:
               1471-2091
            volumeNumber:8
            type:
               Periodical
               PublicationVolume
         publisher:
            name:BioMed Central
            logo:
               url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
               type:ImageObject
            type:Organization
         author:
               name:Luis Sanchez-Pulido
               affiliation:
                     name:CSIC
                     address:
                        name:Centro Nacional de Biotecnologia, CSIC, Madrid, Spain
                        type:PostalAddress
                     type:Organization
               email:[email protected]
               type:Person
               name:Miguel A Andrade-Navarro
               affiliation:
                     name:Ottawa Health Research Institute
                     address:
                        name:Molecular Medicine, Ottawa Health Research Institute, Ottawa, Canada
                        type:PostalAddress
                     type:Organization
                     name:University of Ottawa
                     address:
                        name:Faculty of Medicine, University of Ottawa, Ottawa, Canada
                        type:PostalAddress
                     type:Organization
                     name:Max Delbrück Center for Molecular Medicine
                     address:
                        name:Max Delbrück Center for Molecular Medicine, Berlin, Germany
                        type:PostalAddress
                     type:Organization
               type:Person
         isAccessibleForFree:1
         type:ScholarlyArticle
      context:https://schema.org
ScholarlyArticle:
      headline:The FTO (fat mass and obesity associated) gene codes for a novel member of the non-heme dioxygenase superfamily
      description:Genetic variants in the FTO (fat mass and obesity associated) gene have been associated with an increased risk of obesity. However, the function of its protein product has not been experimentally studied and previously reported sequence similarity analyses suggested the absence of homologs in existing protein databases. Here, we present the first detailed computational analysis of the sequence and predicted structure of the protein encoded by FTO. We performed a sequence similarity search using the human FTO protein as query and then generated a profile using the multiple sequence alignment of the homologous sequences. Profile-to-sequence and profile-to-profile based comparisons identified remote homologs of the non-heme dioxygenase family. Our analysis suggests that human FTO is a member of the non-heme dioxygenase (Fe(II)- and 2-oxoglutarate-dependent dioxygenases) superfamily. Amino acid conservation patterns support this hypothesis and indicate that both 2-oxoglutarate and iron should be important for FTO function. This computational prediction of the function of FTO should suggest further steps for its experimental characterization and help to formulate hypothesis about the mechanisms by which it relates to obesity in humans.
      datePublished:2007-11-08T00:00:00Z
      dateModified:2007-11-08T00:00:00Z
      pageStart:1
      pageEnd:6
      license:http://creativecommons.org/licenses/by/2.0
      sameAs:https://doi.org/10.1186/1471-2091-8-23
      keywords:
         Nuclear Localization Signal
         Secondary Structure Prediction
         Bipartite Nuclear Localization Signal
         Fold Assignment
         HHpred Server
         Biochemistry
         general
         Life Sciences
      image:
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1186%2F1471-2091-8-23/MediaObjects/12858_2007_Article_166_Fig1_HTML.jpg
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1186%2F1471-2091-8-23/MediaObjects/12858_2007_Article_166_Fig2_HTML.jpg
      isPartOf:
         name:BMC Biochemistry
         issn:
            1471-2091
         volumeNumber:8
         type:
            Periodical
            PublicationVolume
      publisher:
         name:BioMed Central
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:Luis Sanchez-Pulido
            affiliation:
                  name:CSIC
                  address:
                     name:Centro Nacional de Biotecnologia, CSIC, Madrid, Spain
                     type:PostalAddress
                  type:Organization
            email:[email protected]
            type:Person
            name:Miguel A Andrade-Navarro
            affiliation:
                  name:Ottawa Health Research Institute
                  address:
                     name:Molecular Medicine, Ottawa Health Research Institute, Ottawa, Canada
                     type:PostalAddress
                  type:Organization
                  name:University of Ottawa
                  address:
                     name:Faculty of Medicine, University of Ottawa, Ottawa, Canada
                     type:PostalAddress
                  type:Organization
                  name:Max Delbrück Center for Molecular Medicine
                  address:
                     name:Max Delbrück Center for Molecular Medicine, Berlin, Germany
                     type:PostalAddress
                  type:Organization
            type:Person
      isAccessibleForFree:1
["Periodical","PublicationVolume"]:
      name:BMC Biochemistry
      issn:
         1471-2091
      volumeNumber:8
Organization:
      name:BioMed Central
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:CSIC
      address:
         name:Centro Nacional de Biotecnologia, CSIC, Madrid, Spain
         type:PostalAddress
      name:Ottawa Health Research Institute
      address:
         name:Molecular Medicine, Ottawa Health Research Institute, Ottawa, Canada
         type:PostalAddress
      name:University of Ottawa
      address:
         name:Faculty of Medicine, University of Ottawa, Ottawa, Canada
         type:PostalAddress
      name:Max Delbrück Center for Molecular Medicine
      address:
         name:Max Delbrück Center for Molecular Medicine, Berlin, Germany
         type:PostalAddress
ImageObject:
      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
Person:
      name:Luis Sanchez-Pulido
      affiliation:
            name:CSIC
            address:
               name:Centro Nacional de Biotecnologia, CSIC, Madrid, Spain
               type:PostalAddress
            type:Organization
      email:[email protected]
      name:Miguel A Andrade-Navarro
      affiliation:
            name:Ottawa Health Research Institute
            address:
               name:Molecular Medicine, Ottawa Health Research Institute, Ottawa, Canada
               type:PostalAddress
            type:Organization
            name:University of Ottawa
            address:
               name:Faculty of Medicine, University of Ottawa, Ottawa, Canada
               type:PostalAddress
            type:Organization
            name:Max Delbrück Center for Molecular Medicine
            address:
               name:Max Delbrück Center for Molecular Medicine, Berlin, Germany
               type:PostalAddress
            type:Organization
PostalAddress:
      name:Centro Nacional de Biotecnologia, CSIC, Madrid, Spain
      name:Molecular Medicine, Ottawa Health Research Institute, Ottawa, Canada
      name:Faculty of Medicine, University of Ottawa, Ottawa, Canada
      name:Max Delbrück Center for Molecular Medicine, Berlin, Germany

External Links {🔗}(103)

Analytics and Tracking {📊}

  • Google Tag Manager

Libraries {📚}

  • Clipboard.js
  • Prism.js

CDN Services {📦}

  • Crossref

4.92s.