NR ARDF
AU Hänel,K.; Smolinski,J.; Fransson,L.; König,B.W.; Stoldt,M.; Willbold,D.
TI Identification of ligands suitable for stabilization of the prion protein's PrPc conformation
QU TSE-Forum, 4. Kongress - Nationale TSE-Forschungsplattform, Düsseldorf 28.10.-29.10.2004, Vortrag V-22
PT Konferenz-Vortrag
AB The prion-model of transmissible spongioform encephalopathies (TSE) is based on the essential role of the host-encoded prion-protein (PrP). Whatever the details of the special formulation of the prion model may be ("protein-only"-hypothesis, heterodimer-model, seeded polymerization), a conformational change of PrPc into PrPsc is always assumed as the crucial step of the infection mechanism. Development and progression of the disease implies ongoing conversion of PrPc into PrPsc. Any stabilization of the PrPc conformation should slow down or inhibit conversion of PrPc into PrPsc. This would principally lead to retardation or end of the disease progression. Based on these considerations, we started a project to identify substances, that tightly bind PrPc with high specificity. We expect these substances to stabilize the PrPc conformation and possibly inhibit conversion of PrPc into PrPsc.
AD Karen Hänel, Lisa Fransson, Bernd W. König, Matthias Stoldt, Dieter Willbold, Forschungszentrum, Jülich, Germany und Heinrich-Heine-Universität, Düsseledorf, Germany; Jörg Smolinski, Dieter Willbold, Institut für Molekulare Biotechnologie, Jena, Germany
SP englisch
PO Deutschland
OR Tagungsband