| Literature DB >> 30507581 |
Hasan A M M Almansoub1,2,3, Hui Tang1,2, Ying Wu1,2, Ding-Qi Wang1,2, Yacoubou Abdoul Razak Mahaman1,2, Na Wei4,5, Yusra A M Almansob6, Wei He7, Dan Liu2,8.
Abstract
Alzheimer's disease (AD) is one of the most prevalent neurodegenerative diseases that is characterized by progressive memory loss and two main pathological hallmarks, including the extracellular amyloid plaques and intracellular neurofibrillary tangles. The microtubule-related protein tau is involved in the pathogenesis of many neurological diseases commonly known as tauopathies and is found to be abnormally hyperphosphorylated in AD and accumulated in neurons. Besides hyperphosphorylation, tau also undergoes abnormal glycosylation, ubiquitination, glycation, and other posttranslational modifications. These abnormalities lead to the aberrant aggregation of tau in the synaptic loci in AD. In this review, we highlighted the most recent studies about how tau is abnormally regulated and how those abnormalities play important roles in the pathogenesis of AD.Entities:
Keywords: Aggregation; Alzheimer’s disease; hyperphosphorylation; post-translational modifications; tau
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Year: 2019 PMID: 30507581 DOI: 10.3233/JAD-180868
Source DB: PubMed Journal: J Alzheimers Dis ISSN: 1387-2877 Impact factor: 4.472