Titlebook: Alzheimer’s Disease: Lessons from Cell Biology; K. S. Kosik (Associate Professor of Neurology and Conference proceedings 1995 Springer-Ve

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https://doi.org/10.1007/978-3-662-34627-3 that the targeting of newly synthesized membrane proteins is governed largely by a ubiquitously distributed set of cytoplasmic domain sorting signals. These determinants may be superficially related to well-characterized signals for localization at plasma membrane-coated pits. Their inactivation re

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https://doi.org/10.1007/978-3-662-34626-6protein (APP) located at chromosome 21q21.2. Mutations in APP have also been found in families segregating hemorrhagic stroke due to congophilic .A4 amyloid angiopathy (CAA) both in the presence and absence of AD. These mutations are located close to known proteolytic cleavage sites in APP, either a

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https://doi.org/10.1007/978-3-531-90487-0larger transmembrane glycoprotein which can be subject to several cleavage events and secreted. The predominant processing pathway cleaves APP within the .A4 peptide sequence, while other events can result in minor quantities of .A4. Thus it is believed that the accumulation of .A4 results from one

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https://doi.org/10.1007/978-3-531-90487-0s, growth factor-stimulated protein kinases that phosphorylate and thereby modulate the properties of many proteins that have key regulatory functions. These include other protein kinases, transcription factors, membrane enzymes, and cytoskeletal proteins (e.g., tau, MAP2). This wide array of phosph