{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T20:22:04Z","timestamp":1791404524251,"version":"4.3.3"},"reference-count":74,"publisher":"Wiley","issue":"10","license":[{"start":{"date-parts":[[2016,4,25]],"date-time":"2016-04-25T00:00:00Z","timestamp":1461542400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/100000957","name":"Alzheimer's Association","doi-asserted-by":"publisher","award":["IIRG\u201009\u2010133206"],"award-info":[{"award-number":["IIRG\u201009\u2010133206"]}],"id":[{"id":"10.13039\/100000957","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["alz-journals.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Alzheimer's &amp;amp; Dementia"],"published-print":{"date-parts":[[2016,10]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:sec>\n                    <jats:title>Introduction<\/jats:title>\n                    <jats:p>Accumulation of hyperphosphorylated tau and the disruption of microtubules are correlated with synaptic loss and pathology of Alzheimer's disease (AD). Impaired cognitive function and pathology of AD is correlated with this lesion. This review looks at the mechanism of neurodegeneration, the prion\u2010like behavior of tau in its interaction with normal MAPs in correlation with tau hyperphosphorylation.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Methods<\/jats:title>\n                    <jats:p>We reviewed our work in the field as well as current literature that pertains to tau phosphorylation and the biological effects.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Results<\/jats:title>\n                    <jats:p>Hyperphosphorylation of tau in AD, in\u00a0vitro, in cells, or in animal models converts this protein into a prion\u2010like protein that is able to propagate the altered conformation.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Discussion<\/jats:title>\n                    <jats:p>These findings suggest that phosphorylation of tau is a critical event in neurodegeneration. The combination of phosphorylation sites can generate a gain of toxic function for tau. The mechanism of tau toxicity might involve not only the microtubule system but also interference with other cellular compartments such as the nucleus and the actin cytoskeleton.<\/jats:p>\n                  <\/jats:sec>","DOI":"10.1016\/j.jalz.2015.12.014","type":"journal-article","created":{"date-parts":[[2016,5,1]],"date-time":"2016-05-01T01:00:08Z","timestamp":1462064408000},"page":"1090-1097","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":51,"title":["Molecular mechanism of prion\u2010like tau\u2010induced neurodegeneration"],"prefix":"10.1002","volume":"12","author":[{"given":"Alejandra D.","family":"Alonso","sequence":"first","affiliation":[{"name":"Department of Biology and Center for Developmental Neuroscience, College of Staten Island, Graduate Center The City University of New York  Staten Island NY 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