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In NDAN, unlike AD, toxic amyloid-\u03b2 oligomers do not localize to the postsynaptic densities (PSDs). Synaptic resistance to amyloid-\u03b2 in NDAN may thus enable these individuals to remain cognitively intact despite the AD-like pathology. The mechanism(s) responsible for this resistance remains unresolved and understanding such protective biological processes could reveal novel targets for the development of effective treatments for AD. The present study uses a proteomic approach to compare the hippocampal postsynaptic densities of NDAN, AD, and healthy age-matched persons to identify protein signatures characteristic for these groups. Subcellular fractionation followed by 2D gel electrophoresis and mass spectrometry were used to analyze the PSDs. We describe fifteen proteins which comprise the unique proteomic signature of NDAN PSDs, thus setting them apart from control subjects and AD patients.<\/jats:p>","DOI":"10.3233\/jad-180179","type":"journal-article","created":{"date-parts":[[2018,7,31]],"date-time":"2018-07-31T18:17:00Z","timestamp":1533061020000},"page":"659-682","update-policy":"https:\/\/doi.org\/10.1177\/sage-journals-update-policy","source":"Crossref","is-referenced-by-count":39,"title":["Postsynaptic Proteome of Non-Demented Individuals with Alzheimer\u2019s Disease Neuropathology"],"prefix":"10.1177","volume":"65","author":[{"given":"Olga","family":"Zolochevska","sequence":"first","affiliation":[{"name":"Department of Neurology, University of Texas Medical Branch, Galveston, TX, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Nicole","family":"Bjorklund","sequence":"additional","affiliation":[{"name":"Department of Neurology, University of Texas Medical Branch, Galveston, TX, 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