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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/s10822-006-9055-1.

Title:
Pharmacophore model for bile acids recognition by the FPR receptor | Journal of Computer-Aided Molecular Design
Description:
Formyl-peptide receptors (FPRs) belong to the family A of the G-protein coupled receptor superfamily and include three subtypes: FPR, FPR-like-1 and FPR-like-2. They have been involved in the control of␣many inflammatory processes promoting the recruitment and infiltration of leukocytes in regions of inflammation through the molecular recognition of chemotactic factors. A large number of structurally diverse chemotypes modulate the activity of FPRs. Newly identified antagonists include bile acids deoxycholic acid (DCA) and chenodeoxycholic acid (CDCA). The molecular recognition of these compounds at FPR receptor was computationally investigated using both ligand- and structure-based approaches. Our findings suggest that all antagonists bind at the first third of the seven helical bundles. A closer inspection of bile acid interaction reveals a number of unexploited anchor points in the binding site that may be used to aid the design of new potent and selective bile acids derivatives at FPR.
Website Age:
28 years and 1 months (reg. 1997-05-29).

Matching Content Categories {📚}

  • Education
  • Virtual Reality
  • Mobile Technology & AI

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.
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How Does Link.springer.com Make Money? {💸}

We don’t know how the website earns money.

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 cashing in, but we can't detect the method they're using.

Keywords {🔍}

article, google, scholar, cas, bile, receptor, acids, receptors, chem, molecular, wang, recognition, fpr, acid, access, pharmacol, privacy, cookies, content, journal, macchiarulo, costantino, pellicciari, immunol, med, mol, publish, search, design, exp, murphy, oppenheim, data, information, log, research, pharmacophore, ferrari, roberto, formylpeptide, antagonists, selective, open, discover, biol, res, gong, shen, chen, biochem,

Topics {✒️}

bile acids recognition formyl peptide receptor month download article/chapter gabriele costantino & roberto pellicciari molecular recognition molecular operating environment pharmacophore model bile acids nlrp3 inflammasome pathway antagonists bind related subjects fxr selective modulation full article pdf privacy choices/manage cookies check access instant access european economic area inflammatory processes promoting structure-based approaches unexploited anchor points van der velde fatty acids conditions privacy policy design tecnologia del farmaco università di perugia article ferrari accepting optional cookies miettinen hm roberto pellicciari chenodeoxycholic acid article journal journal finder publish main content log pharmacology mills js article log author correspondence fpr receptor article cite mangelsdorf dj privacy policy personal data books a optional cookies manage preferences wang jm journal publish mol cell 5 mol cell 3

Schema {🗺️}

WebPage:
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         headline:Pharmacophore model for bile acids recognition by the FPR receptor
         description:Formyl-peptide receptors (FPRs) belong to the family A of the G-protein coupled receptor superfamily and include three subtypes: FPR, FPR-like-1 and FPR-like-2. They have been involved in the control of␣many inflammatory processes promoting the recruitment and infiltration of leukocytes in regions of inflammation through the molecular recognition of chemotactic factors. A large number of structurally diverse chemotypes modulate the activity of FPRs. Newly identified antagonists include bile acids deoxycholic acid (DCA) and chenodeoxycholic acid (CDCA). The molecular recognition of these compounds at FPR receptor was computationally investigated using both ligand- and structure-based approaches. Our findings suggest that all antagonists bind at the first third of the seven helical bundles. A closer inspection of bile acid interaction reveals a number of unexploited anchor points in the binding site that may be used to aid the design of new potent and selective bile acids derivatives at FPR.
         datePublished:2006-09-14T00:00:00Z
         dateModified:2006-09-14T00:00:00Z
         pageStart:295
         pageEnd:303
         sameAs:https://doi.org/10.1007/s10822-006-9055-1
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            Bile acids
            Formyl-peptide receptors
            G-protein coupled receptors
            Molecular modeling
            Molecular recognition
            Pharmacophore
            Rational drug design
            Physical Chemistry
            Computer Applications in Chemistry
            Animal Anatomy / Morphology / Histology
         image:
         isPartOf:
            name:Journal of Computer-Aided Molecular Design
            issn:
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            volumeNumber:20
            type:
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               PublicationVolume
         publisher:
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            logo:
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               name:Cristina Ferrari
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               name:Gabriele Costantino
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               name:Roberto Pellicciari
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                     name:Università di Perugia
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                        name:Dipartimento di Chimica e Tecnologia del Farmaco, Università di Perugia, Perugia, Italy
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ScholarlyArticle:
      headline:Pharmacophore model for bile acids recognition by the FPR receptor
      description:Formyl-peptide receptors (FPRs) belong to the family A of the G-protein coupled receptor superfamily and include three subtypes: FPR, FPR-like-1 and FPR-like-2. They have been involved in the control of␣many inflammatory processes promoting the recruitment and infiltration of leukocytes in regions of inflammation through the molecular recognition of chemotactic factors. A large number of structurally diverse chemotypes modulate the activity of FPRs. Newly identified antagonists include bile acids deoxycholic acid (DCA) and chenodeoxycholic acid (CDCA). The molecular recognition of these compounds at FPR receptor was computationally investigated using both ligand- and structure-based approaches. Our findings suggest that all antagonists bind at the first third of the seven helical bundles. A closer inspection of bile acid interaction reveals a number of unexploited anchor points in the binding site that may be used to aid the design of new potent and selective bile acids derivatives at FPR.
      datePublished:2006-09-14T00:00:00Z
      dateModified:2006-09-14T00:00:00Z
      pageStart:295
      pageEnd:303
      sameAs:https://doi.org/10.1007/s10822-006-9055-1
      keywords:
         Antagonists
         Bile acids
         Formyl-peptide receptors
         G-protein coupled receptors
         Molecular modeling
         Molecular recognition
         Pharmacophore
         Rational drug design
         Physical Chemistry
         Computer Applications in Chemistry
         Animal Anatomy / Morphology / Histology
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            name:Cristina Ferrari
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                     name:Dipartimento di Chimica e Tecnologia del Farmaco, Università di Perugia, Perugia, Italy
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Antonio Macchiarulo
            affiliation:
                  name:Università di Perugia
                  address:
                     name:Dipartimento di Chimica e Tecnologia del Farmaco, Università di Perugia, Perugia, Italy
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Gabriele Costantino
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                  name:Università di Perugia
                  address:
                     name:Dipartimento di Chimica e Tecnologia del Farmaco, Università di Perugia, Perugia, Italy
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Roberto Pellicciari
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                  name:Università di Perugia
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                     name:Dipartimento di Chimica e Tecnologia del Farmaco, Università di Perugia, Perugia, Italy
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            address:
               name:Dipartimento di Chimica e Tecnologia del Farmaco, Università di Perugia, Perugia, Italy
               type:PostalAddress
            type:Organization
      name:Antonio Macchiarulo
      affiliation:
            name:Università di Perugia
            address:
               name:Dipartimento di Chimica e Tecnologia del Farmaco, Università di Perugia, Perugia, Italy
               type:PostalAddress
            type:Organization
      name:Gabriele Costantino
      affiliation:
            name:Università di Perugia
            address:
               name:Dipartimento di Chimica e Tecnologia del Farmaco, Università di Perugia, Perugia, Italy
               type:PostalAddress
            type:Organization
      name:Roberto Pellicciari
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            name:Università di Perugia
            address:
               name:Dipartimento di Chimica e Tecnologia del Farmaco, Università di Perugia, Perugia, Italy
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      name:Dipartimento di Chimica e Tecnologia del Farmaco, Università di Perugia, Perugia, Italy
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External Links {🔗}(87)

Analytics and Tracking {📊}

  • Google Tag Manager

Libraries {📚}

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CDN Services {📦}

  • Crossref

5s.