Molecular cloning and sequence analysis of a human brain cDNA of an Alzheimer amyloid precursor (APP) interacting protein

dc.contributor.authorLiang, Binhuaen_US
dc.date.accessioned2007-05-18T19:58:42Z
dc.date.available2007-05-18T19:58:42Z
dc.date.issued1999-05-01T00:00:00Zen_US
dc.degree.disciplineBiochemistry and Medical Geneticsen_US
dc.degree.levelMaster of Science (M.Sc.)en_US
dc.description.abstractAlzheimer disease (AD) is the most common form of dementia. It is characterized by the accumulation of beta-amyloid peptides (B-AP) derived from Alzheimer amyloid precursor protein (APP) and neurofibrillary tangles in the human brain. Knowledge of the normal functions of APP will provide clues to our understanding of the pathogenesis of Alzheimer disease. The location of APP (membrane-bound) and its structural features are characteristics of plasma membrane receptors such as integrins and epidermal growth factor receptors. Analysis of a protein interaction network from its intracellular carboxyl-terminal domain (APP COOH) indicated that APP might be involved in signal transduction pathways. In order to understand the functions of APP, it is important to identify its effector binding proteins. To address this question, the yeast-two hybrid system was employed. This system is based on a Gal-4 transcriptional assay for detecting specific protein-protein interactions in yeast. This can be used to screen libraries for genes encoding proteins that interact with a known "bait" protein. (Abstract shortened by UMI.)en_US
dc.format.extent5049263 bytes
dc.format.extent184 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.identifier.urihttp://hdl.handle.net/1993/1787
dc.language.isoengen_US
dc.rightsopen accessen_US
dc.titleMolecular cloning and sequence analysis of a human brain cDNA of an Alzheimer amyloid precursor (APP) interacting proteinen_US
dc.typemaster thesisen_US
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