Cargando…
Stabilization of Microtubule-Unbound Tau via Tau Phosphorylation at Ser262/356 by Par-1/MARK Contributes to Augmentation of AD-Related Phosphorylation and Aβ42-Induced Tau Toxicity
Abnormal accumulation of the microtubule-interacting protein tau is associated with neurodegenerative diseases including Alzheimer’s disease (AD). β-amyloid (Aβ) lies upstream of abnormal tau behavior, including detachment from microtubules, phosphorylation at several disease-specific sites, and sel...
Autores principales: | Ando, Kanae, Maruko-Otake, Akiko, Ohtake, Yosuke, Hayashishita, Motoki, Sekiya, Michiko, Iijima, Koichi M. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2016
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4811436/ https://www.ncbi.nlm.nih.gov/pubmed/27023670 http://dx.doi.org/10.1371/journal.pgen.1005917 |
Ejemplares similares
-
Loss of Axonal Mitochondria Promotes Tau-Mediated Neurodegeneration and Alzheimer's Disease–Related Tau Phosphorylation Via PAR-1
por: Iijima-Ando, Kanae, et al.
Publicado: (2012) -
The Interplay between GSK3β and Tau Ser262 Phosphorylation during the Progression of Tau Pathology
por: Song, Liqing, et al.
Publicado: (2022) -
The Cellular Distribution and Ser262 Phosphorylation of Tau Protein Are Regulated by BDNF In Vitro
por: Chen, Qian, et al.
Publicado: (2014) -
Overexpression of 14-3-3ζ Promotes Tau Phosphorylation at Ser(262) and Accelerates Proteosomal Degradation of Synaptophysin in Rat Primary Hippocampal Neurons
por: Qureshi, Hamid Y., et al.
Publicado: (2013) -
Phosphorylation
at Ser289 Enhances the Oligomerization
of Tau Repeat R2
por: Man, Viet Hoang, et al.
Publicado: (2023)