title: Interactions of ginkgolides A and B with a recombinant human prion protein.
abstract: In the presence of ginkgolides A and B a recombinant human prion protein (90-231) is more susceptible to proteolysis, which is characteristic for the non-infective form of prion proteins and more thermostable than in the absence of ginkgolides. Probably, ginkgolides exert a neuroprotective effect through a rearrangement of the prion structure.
authors: Institute of Biochemistry and Molecular Biology, University of Hamburg, Martin-Luther-King Platz 6, 20146 Hamburg, Germany.
authors: Dessislava
authors: D
authors: Georgieva
authors: Lars
authors: L
authors: Redecke
authors: Martin
authors: M
authors: von Bergen
authors: Nicolay
authors: N
authors: Genov
authors: Chrsitian
authors: C
authors: Betzel
mesh_terms: D046934:Ginkgolides / Q000737:chemistry* / Q000378:metabolism / Q000494:pharmacology; D006358:Hot Temperature; D006801:Humans; D008027:Light; D018696:Neuroprotective Agents / Q000378:metabolism; D011328:Prions / Q000737:chemistry* / Q000378:metabolism; D011489:Protein Denaturation / Q000187:drug effects; D017510:Protein Folding; D055550:Protein Stability; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology; D012542:Scattering, Radiation
chemical_list: D046934:Ginkgolides; D018696:Neuroprotective Agents; D011328:Prions; D011994:Recombinant Proteins