APP Processing and the APP-KPI Domain Involvement in the Amyloid Cascade (original) (raw)
The Alternatively Spliced Kunitz Protease Inhibitor Domain Alters Amyloid β Protein Precursor Processing and Amyloid β Protein Production in Cultured Cells
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Journal of Biological Chemistry, 1996
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Biomedicine & Pharmacotherapy, 1994
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Journal of Biological …, 1999
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Relative Increase in Alzheimer's Disease of Soluble Forms of Cerebral Abeta Amyloid Protein Precursor Containing the Kunitz Protease Inhibitory Domain
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Journal of Biological Chemistry, 1998
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The amyloid beta-protein precursor of Alzheimer's disease is degraded extracellularly by a Kunitz protease inhibitor domain-sensitive trypsin-like serine protease in cultures of chick sympathetic neurons
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European Journal of Biochemistry, 1999
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Evidence Against a Role for the Kunitz Domain in Amyloidogenic and Secretory Processing of the Amyloid Precursor Protein
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APP-BP1, a Novel Protein That Binds to the Carboxyl-terminal Region of the Amyloid Precursor Protein
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Molecular Brain Research, 2004
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Beyond the signaling effect role of amyloid-ß42 on the processing of APP, and its clinical implications
Bryan Maloney
Experimental Neurology, 2010
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Key Enzymes and Proteins in Amyloid-Beta Production and Clearance
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The processing and biological function of the human amyloid precursor protein (APP): lessons from different cellular models
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The Kunitz-protease inhibitor domain in amyloid precursor protein reduces cellular mitochondrial enzymes expression and function
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rivka ravid
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Oxidative stress promotes JNK-dependent amyloidogenic processing of normally expressed human APP by differential modification of α-, β- and γ-secretase expression
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In Vivo Neuronal Synthesis and Axonal Transport of Kunitz Protease Inhibitor (KPI)-Containing Forms of the Amyloid Precursor Protein
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Alzheimer's Disease and the Amyloid β Protein
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