Cargando…
An acetylation–phosphorylation switch that regulates tau aggregation propensity and function
The aberrant accumulation of tau protein is a pathological hallmark of a class of neurodegenerative diseases known as tauopathies, including Alzheimer's disease and related dementias. On the basis of previous observations that tau is a direct substrate of histone deacetylase 6 (HDAC6), we sough...
Autores principales: | Carlomagno, Yari, Chung, Dah-eun Chloe, Yue, Mei, Castanedes-Casey, Monica, Madden, Benjamin J., Dunmore, Judy, Tong, Jimei, DeTure, Michael, Dickson, Dennis W., Petrucelli, Leonard, Cook, Casey |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Society for Biochemistry and Molecular Biology
2017
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5602388/ https://www.ncbi.nlm.nih.gov/pubmed/28760828 http://dx.doi.org/10.1074/jbc.M117.794602 |
Ejemplares similares
-
Acetylation of the KXGS motifs in tau is a critical determinant in modulation of tau aggregation and clearance
por: Cook, Casey, et al.
Publicado: (2014) -
Loss of HDAC6, a novel CHIP substrate, alleviates abnormal tau accumulation
por: Cook, Casey, et al.
Publicado: (2012) -
Tau exhibits unique seeding properties in globular glial tauopathy
por: Chung, Dah-eun Chloe, et al.
Publicado: (2019) -
Enhanced phosphorylation of T153 in soluble tau is a defining biochemical feature of the A152T tau risk variant
por: Carlomagno, Yari, et al.
Publicado: (2019) -
Acetylation: a new key to unlock tau’s role in neurodegeneration
por: Cook, Casey, et al.
Publicado: (2014)