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Andrea Schlicksupp
Researcher at Heidelberg University
Publications - 20
Citations - 1567
Andrea Schlicksupp is an academic researcher from Heidelberg University. The author has contributed to research in topics: Gephyrin & Amyloid precursor protein. The author has an hindex of 15, co-authored 20 publications receiving 1482 citations. Previous affiliations of Andrea Schlicksupp include German Cancer Research Center & Free University of Berlin.
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Journal ArticleDOI
The Amyloid Precursor Protein of Alzheimer's Disease in the Reduction of Copper(II) to Copper(I)
Gerd Multhaup,Andrea Schlicksupp,Lars Hesse,Dirk Beher,Thomas Ruppert,Colin L. Masters,Konrad Beyreuther +6 more
TL;DR: Copper ion-mediated toxicity may contribute to neurodegeneration in Alzheimer's disease.
Journal ArticleDOI
Reactive oxygen species and Alzheimer's disease
Gerd Multhaup,Thomas Ruppert,Andrea Schlicksupp,Lars Hesse,Dirk Beher,Colin L. Masters,Konrad Beyreuther +6 more
TL;DR: Copper-mediated toxicity of APP-Cu(II)/(I) complexes may contribute to neurodegeneration in AD and another neurological disorder, familial amyotrophic lateral sclerosis, supports the view that AD and FALS may be linked through a common mechanism.
Journal ArticleDOI
Copper-binding amyloid precursor protein undergoes a site-specific fragmentation in the reduction of hydrogen peroxide.
Gerd Multhaup,Thomas Ruppert,Andrea Schlicksupp,Lars Hesse,Eckhard Bill,Rüdiger Pipkorn,Colin L Masters,Konrad Beyreuther +7 more
TL;DR: The results suggest that a cytotoxic gain-of-function of APP-Cu(I) complexes might result in a perturbation of free radical homeostasis for the pathogenesis of Alzheimer's disease.
Journal ArticleDOI
Human BACE forms dimers and colocalizes with APP.
Ariane Schmechel,Markus Strauss,Andrea Schlicksupp,Rüdiger Pipkorn,Christian Haass,Thomas A. Bayer,Gerd Multhaup +6 more
TL;DR: It is found that in human brain tissue, BACE occurred as a dimer, and inactivation of the carboxyl-terminal active site motif of BACE without an impairment of overall enzyme activity suggests that the enzyme may act as aDimer.
Journal ArticleDOI
Kinetic Analysis of the Interaction of the Copper Chaperone Atox1 with the Metal Binding Sites of the Menkes Protein
Daniel Strausak,Daniel Strausak,Michelle K. Howie,Stephen D. Firth,Andrea Schlicksupp,Rüdiger Pipkorn,Gerd Multhaup,Julian F.B. Mercer +7 more
TL;DR: Interactions of Atox1 with wild-type and mutated pairs of the MBSs of MNK are investigated using yeast two-hybrid analysis and real-time surface plasmon resonance (SPR) to demonstrate the power and sensitivity of SPR as compared with other, more indirect methods.