Binding of S100 proteins to RAGE : An update

Leclerc, Estelle; Fritz, Günter; Vetter, Stefan W.; Heizmann, Claus W.

Binding of S100 proteins to RAGE : An update

Dateien

Zu diesem Dokument gibt es keine Dateien.

Datum

2009

Autor:innen

Leclerc, Estelle

Fritz, Günter

Vetter, Stefan W.

Heizmann, Claus W.

DOI (zitierfähiger Link)

https://doi.org/10.1016/j.bbamcr.2008.11.016

Sammlungen

Biologie

Publikationstyp

Zeitschriftenartikel

Publikationsstatus

Published

Erschienen in

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. Elsevier. 2009, 1793(6), pp. 993-1007. ISSN 0167-4889. eISSN 1879-2596. Available under: doi: 10.1016/j.bbamcr.2008.11.016

Zusammenfassung

The Receptor for Advanced Glycation Endproducts (RAGE) is a multi-ligand receptor of the immunoglobulin family. RAGE interacts with structurally different ligands probably through the oligomerization of the receptor on the cell surface. However, the exact mechanism is unknown. Among RAGE ligands are members of the S100 protein family. S100 proteins are small calcium binding proteins with high structural homology. Several members of the family have been shown to interact with RAGE in vitro or in cell-based assays. Interestingly, many RAGE ligands appear to interact with distinct domains of the extracellular portion of RAGE and to trigger various cellular effects. In this review, we summarize the modes of S100 protein–RAGE interaction with regard to their cellular functions.

Fachgebiet (DDC)

570 Biowissenschaften, Biologie

Zitieren

ISO 690

LECLERC, Estelle, Günter FRITZ, Stefan W. VETTER, Claus W. HEIZMANN, 2009. Binding of S100 proteins to RAGE : An update. In: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. Elsevier. 2009, 1793(6), pp. 993-1007. ISSN 0167-4889. eISSN 1879-2596. Available under: doi: 10.1016/j.bbamcr.2008.11.016

BibTex

@article{Leclerc2009-06Bindi-58213,
  year={2009},
  doi={10.1016/j.bbamcr.2008.11.016},
  title={Binding of S100 proteins to RAGE : An update},
  number={6},
  volume={1793},
  issn={0167-4889},
  journal={Biochimica et Biophysica Acta (BBA) - Molecular Cell Research},
  pages={993--1007},
  author={Leclerc, Estelle and Fritz, Günter and Vetter, Stefan W. and Heizmann, Claus W.}
}

RDF

<rdf:RDF
    xmlns:dcterms="http://purl.org/dc/terms/"
    xmlns:dc="http://purl.org/dc/elements/1.1/"
    xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#"
    xmlns:bibo="http://purl.org/ontology/bibo/"
    xmlns:dspace="http://digital-repositories.org/ontologies/dspace/0.1.0#"
    xmlns:foaf="http://xmlns.com/foaf/0.1/"
    xmlns:void="http://rdfs.org/ns/void#"
    xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > 
  <rdf:Description rdf:about="https://kops.uni-konstanz.de/server/rdf/resource/123456789/58213">
    <dc:contributor>Vetter, Stefan W.</dc:contributor>
    <dcterms:issued>2009-06</dcterms:issued>
    <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
    <dc:contributor>Fritz, Günter</dc:contributor>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2022-07-29T10:50:31Z</dc:date>
    <dc:creator>Leclerc, Estelle</dc:creator>
    <dc:contributor>Leclerc, Estelle</dc:contributor>
    <dc:creator>Heizmann, Claus W.</dc:creator>
    <dc:contributor>Heizmann, Claus W.</dc:contributor>
    <dc:creator>Vetter, Stefan W.</dc:creator>
    <dcterms:title>Binding of S100 proteins to RAGE : An update</dcterms:title>
    <dc:creator>Fritz, Günter</dc:creator>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dc:language>eng</dc:language>
    <bibo:uri rdf:resource="https://kops.uni-konstanz.de/handle/123456789/58213"/>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2022-07-29T10:50:31Z</dcterms:available>
    <foaf:homepage rdf:resource="http://localhost:8080/"/>
    <dcterms:abstract xml:lang="eng">The Receptor for Advanced Glycation Endproducts (RAGE) is a multi-ligand receptor of the immunoglobulin family. RAGE interacts with structurally different ligands probably through the oligomerization of the receptor on the cell surface. However, the exact mechanism is unknown. Among RAGE ligands are members of the S100 protein family. S100 proteins are small calcium binding proteins with high structural homology. Several members of the family have been shown to interact with RAGE in vitro or in cell-based assays. Interestingly, many RAGE ligands appear to interact with distinct domains of the extracellular portion of RAGE and to trigger various cellular effects. In this review, we summarize the modes of S100 protein–RAGE interaction with regard to their cellular functions.</dcterms:abstract>
  </rdf:Description>
</rdf:RDF>

Universitätsbibliographie

Ja

Begutachtet

Ja