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Publications by G. Multhaup
Proteolytic Processing of the Alzheimer Disease-Associated Presenilin-1 Generates an in Vivo Substrate for Protein Kinase C
Proceedings of the National Academy of Sciences of the United States of America
Multidisciplinary
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Homozygosity of the Autosomal Dominant Alzheimer Disease Presenilin 1 E280A Mutation
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Variant Alzheimer Disease With Spastic Paraparesis: A Rare Presenilin-1 Mutation
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Cell Surface Expression of the Alzheimer Disease-Related Presenilin Proteins
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Taking Advantage of Physiological Proteolytic Processing of the Prion Protein for a Therapeutic Perspective in Prion and Alzheimer Diseases
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Phenotypic Variability in Autosomal Dominant Familial Alzheimer Disease Due to the S170F Mutation of Presenilin-1
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Regulation of Protein Phosphatase 1Iby Cdc25C-Associated Kinase 1 (C-Tak1) and PFTAIRE Protein Kinase
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Presenilin-1 280Glu→Ala Mutation Alters C-Terminal APP Processing Yielding Longer Aβ Peptides: Implications for Alzheimer’s Disease
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The Proteolytic Fragments of the Alzheimer’s Disease-Associated Presenilin-1 Form Heterodimers and Occur as a 100–150-kDa Molecular Mass Complex
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