Interactions of Ginkgolides A and B with a recombinant human prion protein

Dessislava Georgieva; Lars Redecke; Martin von Bergen; Nicolay Genov; Christian Betzel

doi:10.2174/092986610790780314

Interactions of Ginkgolides A and B with a recombinant human prion protein

Dessislava Georgieva, Lars Redecke, Martin von Bergen, Nicolay Genov, Christian Betzel

Institut für Biochemie

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.

Originalsprache	Englisch
Zeitschrift	Protein and Peptide Letters
Jahrgang	17
Ausgabenummer	3
Seiten (von - bis)	399-404
Seitenumfang	6
ISSN	0929-8665
DOIs	https://doi.org/10.2174/092986610790780314
Publikationsstatus	Veröffentlicht - 2010

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Forschungsschwerpunkt: Infektion und Entzündung - Zentrum für Infektions- und Entzündungsforschung Lübeck (ZIEL)

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10.2174/092986610790780314

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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.",

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AU - Georgieva, Dessislava

AU - Redecke, Lars

AU - von Bergen, Martin

AU - Genov, Nicolay

AU - Betzel, Christian

PY - 2010

Y1 - 2010

N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/77949989663

U2 - 10.2174/092986610790780314

DO - 10.2174/092986610790780314

M3 - Journal articles

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AN - SCOPUS:77949989663

SN - 0929-8665

VL - 17

SP - 399

EP - 404

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ER -

Interactions of Ginkgolides A and B with a recombinant human prion protein

Abstract

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