Pan-HDAC Inhibitors Promote Tau Aggregation by Increasing the Level of Acetylated Tau
DC Field | Value | Language |
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dc.contributor.author | Jeong, Hyeanjeong | - |
dc.contributor.author | Shin, Seulgi | - |
dc.contributor.author | Lee, Jun-Seok | - |
dc.contributor.author | Lee, Soo Hyun | - |
dc.contributor.author | Baik, Ja-Hyun | - |
dc.contributor.author | Lim, Sungsu | - |
dc.contributor.author | Kim, Yun Kyung | - |
dc.date.accessioned | 2021-09-01T07:17:04Z | - |
dc.date.available | 2021-09-01T07:17:04Z | - |
dc.date.created | 2021-06-18 | - |
dc.date.issued | 2019-09-01 | - |
dc.identifier.issn | 1661-6596 | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/62952 | - |
dc.description.abstract | 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. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | MDPI | - |
dc.subject | HISTONE DEACETYLASE INHIBITORS | - |
dc.subject | ALZHEIMERS-DISEASE | - |
dc.subject | MEDIATED NEURODEGENERATION | - |
dc.subject | MOUSE MODEL | - |
dc.subject | PATHOLOGY | - |
dc.subject | PROTEIN | - |
dc.subject | PHOSPHORYLATION | - |
dc.subject | DEGRADATION | - |
dc.subject | THERAPY | - |
dc.title | Pan-HDAC Inhibitors Promote Tau Aggregation by Increasing the Level of Acetylated Tau | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Lee, Jun-Seok | - |
dc.contributor.affiliatedAuthor | Baik, Ja-Hyun | - |
dc.identifier.doi | 10.3390/ijms20174283 | - |
dc.identifier.scopusid | 2-s2.0-85071765020 | - |
dc.identifier.wosid | 000486888400215 | - |
dc.identifier.bibliographicCitation | INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, v.20, no.17 | - |
dc.relation.isPartOf | INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES | - |
dc.citation.title | INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES | - |
dc.citation.volume | 20 | - |
dc.citation.number | 17 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Chemistry | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Chemistry, Multidisciplinary | - |
dc.subject.keywordPlus | HISTONE DEACETYLASE INHIBITORS | - |
dc.subject.keywordPlus | ALZHEIMERS-DISEASE | - |
dc.subject.keywordPlus | MEDIATED NEURODEGENERATION | - |
dc.subject.keywordPlus | MOUSE MODEL | - |
dc.subject.keywordPlus | PATHOLOGY | - |
dc.subject.keywordPlus | PROTEIN | - |
dc.subject.keywordPlus | PHOSPHORYLATION | - |
dc.subject.keywordPlus | DEGRADATION | - |
dc.subject.keywordPlus | THERAPY | - |
dc.subject.keywordAuthor | histone deacetylase inhibitor | - |
dc.subject.keywordAuthor | tau acetylation | - |
dc.subject.keywordAuthor | tau aggregation | - |
dc.subject.keywordAuthor | Alzheimer&apos | - |
dc.subject.keywordAuthor | s disease | - |
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