Jeong, Hyeanjeong Shin, Seulgi Lee, Jun-Seok Lee, Soo Hyun Baik, Ja-Hyun Lim, Sungsu Kim, Yun Kyung 2024-01-19T19:31:00Z 2024-01-19T19:31:00Z 2021-09-04 2019-09 1661-6596 https://pubs.kist.re.kr/handle/201004/119648 Epigenetic remodeling via histone acetylation has become a popular therapeutic strategy to treat Alzheimer’s disease (AD). In particular, histone deacetylase (HDAC) inhibitors including M344 and SAHA have been elucidated to be new drug candidates for AD, improving cognitive abilities impaired in AD mouse models. Although emerged as a promising target for AD, most of the HDAC inhibitors are poorly selective and could cause unwanted side effects. Here we show that tau is one of the cytosolic substrates of HDAC and the treatment of HDAC inhibitors such as Scriptaid, M344, BML281, and SAHA could increase the level of acetylated tau, resulting in the activation of tau pathology. English MDPI Pan-HDAC Inhibitors Promote Tau Aggregation by Increasing the Level of Acetylated Tau Article 10.3390/ijms20174283 1 INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, v.20, no.17 INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES 20 17 Y scie scopus 000486888400215 2-s2.0-85071765020 Biochemistry & Molecular Biology Chemistry, Multidisciplinary Biochemistry & Molecular Biology Chemistry Article HISTONE DEACETYLASE INHIBITORS ALZHEIMERS-DISEASE MEDIATED NEURODEGENERATION MOUSE MODEL PATHOLOGY PROTEIN PHOSPHORYLATION DEGRADATION THERAPY histone deacetylase inhibitor tau acetylation tau aggregation Alzheimer&apos s disease