An acetylation–phosphorylation switch that regulates tau aggregation propensity and function
出版年份 2017 全文链接
标题
An acetylation–phosphorylation switch that regulates tau aggregation propensity and function
作者
关键词
-
出版物
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 292, Issue 37, Pages 15277-15286
出版商
American Society for Biochemistry & Molecular Biology (ASBMB)
发表日期
2017-08-01
DOI
10.1074/jbc.m117.794602
参考文献
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注意:仅列出部分参考文献,下载原文获取全部文献信息。- Cryo-EM structures of tau filaments from Alzheimer’s disease
- (2017) Anthony W. P. Fitzpatrick et al. NATURE
- Tau deposition drives neuropathological, inflammatory and behavioral abnormalities independently of neuronal loss in a novel mouse model
- (2015) Casey Cook et al. HUMAN MOLECULAR GENETICS
- Critical role of acetylation in tau-mediated neurodegeneration and cognitive deficits
- (2015) Sang-Won Min et al. NATURE MEDICINE
- Tau post-translational modifications in wild-type and human amyloid precursor protein transgenic mice
- (2015) Meaghan Morris et al. NATURE NEUROSCIENCE
- Lysine methylation is an endogenous post-translational modification of tau protein in human brain and a modulator of aggregation propensity
- (2014) Kristen E. Funk et al. BIOCHEMICAL JOURNAL
- Nuclear Magnetic Resonance Analysis of the Acetylation Pattern of the Neuronal Tau Protein
- (2014) Amina Kamah et al. BIOCHEMISTRY
- Histone deacetylase 6 inhibition improves memory and reduces total tau levels in a mouse model of tau deposition
- (2014) Maj-Linda Selenica et al. Alzheimers Research & Therapy
- Acetylation: a new key to unlock tau’s role in neurodegeneration
- (2014) Casey Cook et al. Alzheimers Research & Therapy
- Acetylation of the KXGS motifs in tau is a critical determinant in modulation of tau aggregation and clearance
- (2013) Casey Cook et al. HUMAN MOLECULAR GENETICS
- The microtubule-associated tau protein has intrinsic acetyltransferase activity
- (2013) Todd J Cohen et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- The CAMKK2-AMPK Kinase Pathway Mediates the Synaptotoxic Effects of Aβ Oligomers through Tau Phosphorylation
- (2013) Georges Mairet-Coello et al. NEURON
- Biochemistry and Cell Biology of Tau Protein in Neurofibrillary Degeneration
- (2013) E.-M. Mandelkow et al. Cold Spring Harbor Perspectives in Medicine
- Acetylated tau, a novel pathological signature in Alzheimer's disease and other tauopathies
- (2012) David J. Irwin et al. BRAIN
- Loss of HDAC6, a novel CHIP substrate, alleviates abnormal tau accumulation
- (2012) Casey Cook et al. HUMAN MOLECULAR GENETICS
- HDAC6 Inhibitor Blocks Amyloid Beta-Induced Impairment of Mitochondrial Transport in Hippocampal Neurons
- (2012) Chaeyoung Kim et al. PLoS One
- Novel diffusion barrier for axonal retention of Tau in neurons and its failure in neurodegeneration
- (2011) Xiaoyu Li et al. EMBO JOURNAL
- A critical role for the PAR-1/MARK-tau axis in mediating the toxic effects of Aβ on synapses and dendritic spines
- (2011) Wendou Yu et al. HUMAN MOLECULAR GENETICS
- Alzheimer's Disease: The Challenge of the Second Century
- (2011) D. M. Holtzman et al. Science Translational Medicine
- The acetylation of tau inhibits its function and promotes pathological tau aggregation
- (2011) Todd J. Cohen et al. Nature Communications
- Acetylation of Tau Inhibits Its Degradation and Contributes to Tauopathy
- (2010) Sang-Won Min et al. NEURON
- Aging Analysis Reveals Slowed Tau Turnover and Enhanced Stress Response in a Mouse Model of Tauopathy
- (2008) Chad Dickey et al. AMERICAN JOURNAL OF PATHOLOGY
- Histone deacetylase 6 interacts with the microtubule-associated protein tau
- (2008) Huiping Ding et al. JOURNAL OF NEUROCHEMISTRY
- Akt and CHIP coregulate tau degradation through coordinated interactions
- (2008) C. A. Dickey et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
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