We are analyzing https://link.springer.com/chapter/10.1007/978-94-017-9050-5_5.

Title:
RXRs: Collegial Partners | SpringerLink
Description:
Retinoid X Receptors (RXR) were initially identified as nuclear receptors binding with stereo-selectivity the vitamin A derivative 9-cis retinoic acid, although the relevance of this molecule as endogenous activator of RXRs is still elusive. Importantly, within the...
Website Age:
28 years and 1 months (reg. 1997-05-29).

Matching Content Categories {📚}

Education
Science
Environment

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.
However, some sources were not loaded, we suggest to reload the page to get complete results.

check SE Ranking
check Ahrefs
check Similarweb
check Ubersuggest
check Semrush

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

We see no obvious way the site makes money.

Websites don't always need to be profitable; some serve as platforms for education or personal expression. Websites can serve multiple purposes. And this might be one of them. Link.springer.com could be getting rich in stealth mode, or the way it's monetizing isn't detectable.

Keywords {🔍}

pubmed, google, scholar, cas, receptor, nuclear, retinoid, central, receptors, acid, rxr, cell, biol, mol, retinoic, hormone, chem, nature, binding, thyroid, chambon, genes, cancer, evans, alpha, activation, desvergne, peroxisome, structure, heterodimers, ligand, transcriptional, human, liu, heyman, res, endocrinol, function, chapter, proliferatoractivated, mangelsdorf, chen, protein, gene, gronemeyer, heterodimer, response, cells, dev, dna,

Topics {✒️}

peroxisome proliferator-activated receptor/retinoid peroxisome proliferator-activated receptor-retinoid intact vdr-rxr complex peroxisome proliferator-activated receptor peroxisome proliferator-activated receptors rxr[beta] ligand-binding domains unraveling protein-protein interactions month download article/chapter pml-rara/rxr alters ppar-rxr heterodimer activates human car/rxralpha heterodimer ra-induced rar[gamma] degradation specific sequence requirements retinoic acid-induced degradation farnesoid x-activated receptor rxr ligand-binding domains gampe rt jr receptor gamma-deficient mice dna binding specificity nuclear receptors sxr/pxr ligand-independent nuclear receptors small-cell lung cancer receptor α mediated prolactin gene transcription ligand-bound crystal structure retinoic acid receptor/retinoid fluorescence imaging reveals gene-specific permissivity ppar target genes ubiquitin-proteasome pathway multiple parameters control dr3 target dna vdr/rxr cistrome receptor heterodimer binding privacy choices/manage cookies specific dna requires multiple physiological processes ligand binding domain device instant download key cellular functions dna-induced dissociation human thyroid carcinomas forkhead protein foxa1 editor information editors analog bind rxralpha cognate response elements bifunctional enzyme gene human hepatocellular carcinoma receptor-gamma gene decreased dna binding

Schema {🗺️}

ScholarlyArticle:
      headline:RXRs: Collegial Partners
      pageEnd:102
      pageStart:75
      image:https://media.springernature.com/w153/springer-static/cover/book/978-94-017-9050-5.jpg
      genre:
         Biomedical and Life Sciences
         Biomedical and Life Sciences (R0)
      isPartOf:
         name:The Biochemistry of Retinoic Acid Receptors I: Structure, Activation, and Function at the Molecular Level
         isbn:
            978-94-017-9050-5
            978-94-017-9049-9
         type:Book
      publisher:
         name:Springer Netherlands
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:Federica Gilardi
            affiliation:
                  name:University of Lausanne
                  address:
                     name:Center for Integrative Genomics, University of Lausanne, Lausanne, Switzerland
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Béatrice Desvergne
            affiliation:
                  name:University of Lausanne
                  address:
                     name:Center for Integrative Genomics, University of Lausanne, Lausanne, Switzerland
                     type:PostalAddress
                  type:Organization
            email:[email protected]
            type:Person
      keywords:Nuclear Receptor, Constitutive Androstane Receptor, Heterodimerization Partner, Nuclear Receptor Binding, Chicken Ovalbumin Upstream Promoter Transcription
      description:Retinoid X Receptors (RXR) were initially identified as nuclear receptors binding with stereo-selectivity the vitamin A derivative 9-cis retinoic acid, although the relevance of this molecule as endogenous activator of RXRs is still elusive. Importantly, within the nuclear receptor superfamily, RXRs occupy a peculiar place, as they are obligatory partners for a number of other nuclear receptors, thus integrating the corresponding signaling pathways. In this chapter, we describe the structural features allowing RXR to form homo- and heterodimers, and the functional consequences of this unique ability. Furthermore, we discuss the importance of studying RXR activity at a genome-wide level in order to comprehensively address the biological implications of their action that is fundamental to understand to what extent RXRs could be exploited as new therapeutic targets.
      datePublished:2014
      isAccessibleForFree:
      hasPart:
         isAccessibleForFree:
         cssSelector:.main-content
         type:WebPageElement
      context:https://schema.org
Book:
      name:The Biochemistry of Retinoic Acid Receptors I: Structure, Activation, and Function at the Molecular Level
      isbn:
         978-94-017-9050-5
         978-94-017-9049-9
Organization:
      name:Springer Netherlands
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:University of Lausanne
      address:
         name:Center for Integrative Genomics, University of Lausanne, Lausanne, Switzerland
         type:PostalAddress
      name:University of Lausanne
      address:
         name:Center for Integrative Genomics, University of Lausanne, Lausanne, Switzerland
         type:PostalAddress
ImageObject:
      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
Person:
      name:Federica Gilardi
      affiliation:
            name:University of Lausanne
            address:
               name:Center for Integrative Genomics, University of Lausanne, Lausanne, Switzerland
               type:PostalAddress
            type:Organization
      name:Béatrice Desvergne
      affiliation:
            name:University of Lausanne
            address:
               name:Center for Integrative Genomics, University of Lausanne, Lausanne, Switzerland
               type:PostalAddress
            type:Organization
      email:[email protected]
PostalAddress:
      name:Center for Integrative Genomics, University of Lausanne, Lausanne, Switzerland
      name:Center for Integrative Genomics, University of Lausanne, Lausanne, Switzerland
WebPageElement:
      isAccessibleForFree:
      cssSelector:.main-content

External Links {🔗}(364)

Analytics and Tracking {📊}

Google Tag Manager

Libraries {📚}

Clipboard.js

CDN Services {📦}

Pbgrd

4.77s.

LINK . SPRINGER . COM {}