한빛사 논문
Geewoo Nam1,6, Yuxi Lin2,6, Mi Hee Lim3, Young-Ho Lee2,4,5,*
1Department of Chemistry, Ulsan National Institute of Science and Technology (UNIST), Ulsan 44919, Republic of Korea
2Research Center of Bioconvergence Analysis, Korea Basic Science Institute (KBSI), Ochang, Chungbuk 28119, Republic of Korea
3Department of Chemistry, Korea Advanced Institute of Science and Technology (KAIST), Daejeon 34141, Republic of Korea
4Neurovascular Research Group, Korea Brain Research Institute (KBRI), Daegu 41068, Republic of Korea
5Bio-Analytical Science, University of Science and Technology (UST), Daejeon 34113, Republic of Korea
6These authors contributed equally
*Corresponding author
Abstract
Recent findings have garnered a substantial amount of attention toward tau based on its pathological contribution to neurodegenerative diseases, such as Alzheimer’s disease (AD). Studies investigating the structure and aggregation of tau under various in vitro and in vivo conditions have revealed its intrinsically disordered structures and amyloidogenesis process. The aggregation behavior of tau is strongly dependent on the experimental conditions due to the high sensitivity of both the soluble tau conformations and the amyloid nucleation process toward its surrounding environments. Herein, we review and discuss (1) the effects of different physicochemical and biological factors as well as intermolecular interactions with various molecular chaperones on tau aggregation, (2) context-dependent liquid-liquid phase separation of tau and its amyloidogenic transformation, and (3) the utility of the phase diagram in comprehending the phase transition and separation of proteins.
논문정보
관련 링크
연구자 키워드
관련분야 연구자보기
소속기관 논문보기
관련분야 논문보기
해당논문 저자보기