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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,Mechanisms of Molecular Sorting in Polarized Cells: Relevance to Alzheimer’s Disease, 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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,Alzheimer’s Disease and Hemorrhagic Stroke: Their Relationship to ,A4 Amyloid Deposition,protein (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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Combining In Vitro Cell Biology and In Vivo Mouse Modelling to Study the Mechanisms Underlying Alzhngles and cerebrovascular deposits. Neither the molecular mechanisms of the formation of these structures nor their direct bearing on the neurodegeneration per se are understood. The major component of the senile plaques and vascular deposits is the .-amyloid peptide (.A4), a 39–43 amino acid fragme

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Regulation and Structure of the MAP Kinases ERK1 and ERK2,s, 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

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Calcineurin as a Pivotal Ca2+-Sensitive Switching Element in Biological Responses: Implications formically . to changes in cellular response. A hallmark feature of Alzheimer’s disease is the presence of “hyperphosphorylated” forms of the microtubule-associated protein, tau, in paired helical filaments. Although the relationship of this biochemical abnormality to disease etiology and pathology is

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