Structure and function of the metal-binding protein S100B and its interaction with the receptor for advanced glycation end products

Kurzanzeige
dc.contributor.authorOstendorp, Thorstendeu
dc.date.accessioned2011-03-24T17:40:47Zdeu
dc.date.available2011-03-24T17:40:47Zdeu
dc.date.issued2006deu
dc.description.abstractS100B is one of the most abundant proteins in the brain and exerts intra- as well as extracellular functions. It has been implicated to play a key role in many neurodegenerative diseases. Earlier studies showed that these functions might be controlled in a Ca2+ and / or Zn2+ dependent manner. A crucial step in the pathogenesis of neurodegenerative diseases is the activation of the cell surface receptor RAGE by extracellular S100B. Currently, only two NMR structures of human Ca2+ -S100B has been described: dimeric S100B and a complex with the peptide TRTK12. Furthermore only one crystal structure of bovine S100B has been solved so far, but there is no crystal structure of human S100B. The focus and scope of this doctoral thesis was to collect more structural information on the human S100B protein and to investigate the interaction of S100B with its receptor RAGE.eng
dc.description.versionpublished
dc.format.mimetypeapplication/pdfdeu
dc.identifier.ppn262496267deu
dc.identifier.urihttp://kops.uni-konstanz.de/handle/123456789/8123
dc.language.isoengdeu
dc.legacy.dateIssued2007deu
dc.rightsAttribution-NonCommercial-NoDerivs 2.0 Generic
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/2.0/
dc.subjectProteinstrukturdeu
dc.subjectKalziumdeu
dc.subjectZinkdeu
dc.subjectS100-Proteinedeu
dc.subjectS100Bdeu
dc.subjectS100deu
dc.subjectS100Bdeu
dc.subjectRAGEdeu
dc.subjectProtein-structuredeu
dc.subjectCalciumdeu
dc.subjectZincdeu
dc.subject.ddc570deu
dc.subject.gndPichiadeu
dc.subject.gndAlzheimer-Krankheitdeu
dc.titleStructure and function of the metal-binding protein S100B and its interaction with the receptor for advanced glycation end productseng
dc.title.alternativeStruktur und Funktion des Metall bindenden S100B Protein und seine Interaktion mit dem "Receptor For Advanced Glycation end Products"deu
dc.typeDOCTORAL_THESISdeu
dspace.entity.typePublication
kops.citation.bibtex
@phdthesis{Ostendorp2006Struc-8123,
  year={2006},
  title={Structure and function of the metal-binding protein S100B and its interaction with the receptor for advanced glycation end products},
  author={Ostendorp, Thorsten},
  address={Konstanz},
  school={Universität Konstanz}
}
kops.citation.iso690OSTENDORP, Thorsten, 2006. Structure and function of the metal-binding protein S100B and its interaction with the receptor for advanced glycation end products [Dissertation]. Konstanz: University of Konstanzdeu
kops.citation.iso690OSTENDORP, Thorsten, 2006. Structure and function of the metal-binding protein S100B and its interaction with the receptor for advanced glycation end products [Dissertation]. Konstanz: University of Konstanzeng
kops.citation.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/123456789/8123">
    <dc:format>application/pdf</dc:format>
    <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/>
    <dcterms:alternative>Struktur und Funktion des Metall bindenden S100B Protein und seine Interaktion mit dem "Receptor For Advanced Glycation end Products"</dcterms:alternative>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:40:47Z</dc:date>
    <foaf:homepage rdf:resource="http://localhost:8080/"/>
    <dspace:hasBitstream rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/8123/1/Ostendorp_Diss.pdf"/>
    <dcterms:hasPart rdf:resource="https://kops.uni-konstanz.de/bitstream/123456789/8123/1/Ostendorp_Diss.pdf"/>
    <dcterms:rights rdf:resource="http://creativecommons.org/licenses/by-nc-nd/2.0/"/>
    <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/>
    <dc:contributor>Ostendorp, Thorsten</dc:contributor>
    <dc:rights>Attribution-NonCommercial-NoDerivs 2.0 Generic</dc:rights>
    <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:40:47Z</dcterms:available>
    <dcterms:title>Structure and function of the metal-binding protein S100B and its interaction with the receptor for advanced glycation end products</dcterms:title>
    <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/8123"/>
    <dcterms:issued>2006</dcterms:issued>
    <dc:language>eng</dc:language>
    <dcterms:abstract xml:lang="eng">S100B is one of the most abundant proteins in the brain and exerts intra- as well as extracellular functions. It has been implicated to play a key role in many neurodegenerative diseases. Earlier studies showed that these functions might be controlled in a Ca2+ and / or Zn2+ dependent manner. A crucial step in the pathogenesis of neurodegenerative diseases is the activation of the cell surface receptor RAGE by extracellular S100B. Currently, only two NMR structures of human Ca2+ -S100B has been described: dimeric S100B and a complex with the peptide TRTK12. Furthermore only one crystal structure of bovine S100B has been solved so far, but there is no crystal structure of human S100B. The focus and scope of this doctoral thesis was to collect more structural information on the human S100B protein and to investigate the interaction of S100B with its receptor RAGE.</dcterms:abstract>
    <dc:creator>Ostendorp, Thorsten</dc:creator>
  </rdf:Description>
</rdf:RDF>
kops.date.examination2007-02-13deu
kops.description.abstractS100B ist eins der am häufigsten exprimierten Proteine im Gehirn wo es sowohl intra- als auch extrazellulare Funktion übernimmt. Es wird angenommen dass es eine Schlüsselrolle in der Entstehung verschiedener neurodegenerativer Erkrankungen einnimmt. Frühere Studien zeigten bereits, dass diese Funktionen Ca2+ und / oder Zn2+ abhängig gesteuert werden. Ein entscheidender Schritt in der Pathogenese bei neurodegenerativen Erkrankungen ist die Aktivierung des Zelloberflächenrezeptors RAGE durch extrazelluläres S100B. Bislang sind nur zwei NMR Strukturen des humanen Ca2+ -S100B Protein bekannt. Eine Struktur von S100B allein und eine im Komplex mit dem Peptid TRTK12. Die einzige Kristallstruktur zu S100B ist die des homologen S100B aus Rind. Derzeit ist noch keine Kristallstruktur zum humanen S100B verfügbar.<br />Schwerpunkt und Ziel der hier vorgelegten Doktorarbeit war es detaillierte Strukturinformationen über das menschliche S100B Protein zu bekommen und die Interaktion von S100B mit seinem Rezeptor RAGE zu untersuchen.deu
kops.description.openAccessopenaccessgreen
kops.identifier.nbnurn:nbn:de:bsz:352-opus-23752deu
kops.opus.id2375deu

Dateien

Originalbündel

Gerade angezeigt 1 - 1 von 1
Vorschaubild nicht verfügbar
Name:
Ostendorp_Diss.pdf
Größe:
5.38 MB
Format:
Adobe Portable Document Format
Ostendorp_Diss.pdf
Ostendorp_Diss.pdfGröße: 5.38 MBDownloads: 1145

Sammlungen

Biologie: Publikationen