{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,3]],"date-time":"2026-10-03T17:07:52Z","timestamp":1791047272407,"version":"4.1.0"},"reference-count":46,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2007,2,26]],"date-time":"2007-02-26T00:00:00Z","timestamp":1172448000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal of Neurochemistry"],"published-print":{"date-parts":[[2007,7]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Defects in axonal transport and synaptic dysfunctions are associated with early stages of several neurodegenerative diseases including Alzheimer\u2019s, Huntington\u2019s, Parkinson\u2019s, and prion diseases. Here, we tested the effect of full\u2010length mammalian prion protein (rPrP) converted into three conformationally different isoforms to induce pathological changes regarded as early subcellular hallmarks of prion disease. We employed human embryonal teratocarcinoma NTERA2 cells (NT2) that were terminally differentiated into neuronal and glial cells and co\u2010cultured together. We found that rPrP fibrils but not \u03b1\u2010rPrP or soluble \u03b2\u2010sheet rich oligomers caused degeneration of neuronal processes. Degeneration of processes was accompanied by a collapse of microtubules and aggregation of cytoskeletal proteins, formation of neuritic beads, and a dramatic change in localization of synaptophysin. Our studies demonstrated the utility of NT2 cells as valuable human model system for elucidating subcellular events of prion pathogenesis, and supported the emerging hypothesis that defects in neuronal transport and synaptic abnormalities are early pathological hallmarks associated with prion diseases.<\/jats:p>","DOI":"10.1111\/j.1471-4159.2007.04537.x","type":"journal-article","created":{"date-parts":[[2007,5,8]],"date-time":"2007-05-08T08:41:15Z","timestamp":1178613675000},"page":"398-407","source":"Crossref","is-referenced-by-count":20,"title":["Amyloid fibrils of mammalian prion protein induce axonal degeneration in NTERA2\u2010derived terminally differentiated neurons"],"prefix":"10.1111","volume":"102","author":[{"given":"Vera","family":"Novitskaya","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Natallia","family":"Makarava","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ian","family":"Sylvester","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Igor B.","family":"Bronstein","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ilia V.","family":"Baskakov","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2007,2,26]]},"reference":[{"key":"e_1_2_7_2_1","doi-asserted-by":"publisher","DOI":"10.1016\/0169-328X(94)90293-3"},{"key":"e_1_2_7_3_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.jmb.2006.02.007"},{"key":"e_1_2_7_4_1","doi-asserted-by":"publisher","DOI":"10.1016\/0012-1606(84)90316-6"},{"key":"e_1_2_7_5_1","first-page":"147","article-title":"Pluripotent embryonal carcinoma clones derived from the human teratocarcinoma cell line Tera\u20102: differentiation in vivo and in vitro","volume":"50","author":"Andrews P. 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