Chang, Ya-LanYa-LanChangYang, Chan-ChihChan-ChihYangHuang, Yun-YuYun-YuHuangChen, Yi-AnYi-AnChenYang, Chia-WeiChia-WeiYangLiao, Chia-YuChia-YuLiaoLi, HsunHsunLiCHING-SHYI WUCHIN-HSIEN LINSHU-CHUN TENG2024-01-292024-01-292023-12-181741-7007https://scholars.lib.ntu.edu.tw/handle/123456789/638972Alzheimer's disease (AD) is the most common neurodegenerative disorder with clinical presentations of progressive cognitive and memory deterioration. The pathologic hallmarks of AD include tau neurofibrillary tangles and amyloid plaque depositions in the hippocampus and associated neocortex. The neuronal aggregated tau observed in AD cells suggests that the protein folding problem is a major cause of AD. J-domain-containing proteins (JDPs) are the largest family of cochaperones, which play a vital role in specifying and directing HSP70 chaperone functions. JDPs bind substrates and deliver them to HSP70. The association of JDP and HSP70 opens the substrate-binding domain of HSP70 to help the loading of the clients. However, in the initial HSP70 cycle, which JDP delivers tau to the HSP70 system in neuronal cells remains unclear.enAlzheimer’s disease; Cochaperone; DNAJB6b; J-domain proteins; Tau[SDGs]SDG3journal article10.1186/s12915-023-01798-6381109162-s2.0-85180251324https://api.elsevier.com/content/abstract/scopus_id/85180251324