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    Home > Biochemistry News > Biotechnology News > Nature Structural & Molecular Biology has made new progress in the field of Alzheimer's disease pathogenesis research

    Nature Structural & Molecular Biology has made new progress in the field of Alzheimer's disease pathogenesis research

    • Last Update: 2022-04-20
    • Source: Internet
    • Author: User
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    On March 25, 2022, Beijing time, the journal Nature Structural & Molecular Biologypublished online the latest achievements of the Shenzhen University of Technology (tentative name, hereinafter referred to as "Shenzhen Science and Technology") Ye Keqiang's team and the Wuhan University People's Hospital Zhang Zhentao's team


     

    Screenshot of the paper online

    AD is the most common neurodegenerative disease in clinic, and abnormal aggregation of tau protein in the brain is an important pathological manifestation of AD


    The research team has conducted a long-term exploration of the molecular mechanism of Tau protein aggregation in the brain


    Next, the team found that ApoE3 binds to Tau and reduces cleavage of Tau by AEP, but the AD-associated allele, ApoE4, loses the ability to bind Tau protein, making Tau more susceptible to cleavage by AEP


    In the newly published study, the team further studied the modification effect of DOPAGEL on Tau and found that DOPAGEL can directly covalently modify the K353 site of Tau.


    The significance of this study is to reveal why the Tau protein in the locus coeruleus first aggregates to form pathological inclusion bodies during the pathogenesis of AD, which is very important for understanding the initiation and dissemination of Tau protein aggregates in the brain of AD patients.


    Professor Ye Keqiang is the dean of the Department of Biology at the School of Life and Health of Shenyang Polytechnic, and was a tenured professor at Emory University in the United States


    Original link: https:// 

     

    Figure 1: DOPAGEL promotes intracellular Tau aggregation while K353R mutation can block DOPEGAL's promotion

     

    Figure 2: Blocking the modification of Tau by DOPEGAL can delay the aggregation of Tau.




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