Dual modification of Alzheimer's disease PHF-tau protein by lysine methylation and ubiquitylation: a mass spectrometry approach.
about
Disrupting self-assembly and toxicity of amyloidogenic protein oligomers by "molecular tweezers" - from the test tube to animal modelsNeurochemical profile of dementia pugilisticaGlial contributions to neurodegeneration in tauopathies.Structure and mechanism of action of tau aggregation inhibitors.Lysine methylation is an endogenous post-translational modification of tau protein in human brain and a modulator of aggregation propensity.Recent advances in applying mass spectrometry and systems biology to determine brain dynamics.Transcriptional signaling pathways inversely regulated in Alzheimer's disease and glioblastoma multiform.Tau prions from Alzheimer's disease and chronic traumatic encephalopathy patients propagate in cultured cells.Mass Spectrometry Analysis of Lysine Posttranslational Modifications of Tau Protein from Alzheimer's Disease Brain.Degradation of tau protein by autophagy and proteasomal pathways.Lysosomal fusion dysfunction as a unifying hypothesis for Alzheimer's disease pathology.Tau-induced neurodegeneration: mechanisms and targets.The physiology and pathology of microtubule-associated protein tau.The Emerging Role of Proteomics in Precision Medicine: Applications in Neurodegenerative Diseases and Neurotrauma.Acetylated tau in Alzheimer's disease: An instigator of synaptic dysfunction underlying memory loss: Increased levels of acetylated tau blocks the postsynaptic signaling required for plasticity and promotes memory deficits associated with tauopathy.Therapeutic Strategies for Restoring Tau Homeostasis.Microtubule affinity-regulating kinases are potential druggable targets for Alzheimer's disease.Lysine-Directed Post-translational Modifications of Tau Protein in Alzheimer's Disease and Related Tauopathies.FLEXITau: Quantifying Post-translational Modifications of Tau Protein in Vitro and in Human Disease.Amyloid-β and tau complexity - towards improved biomarkers and targeted therapies.Tau post-translational modifications in wild-type and human amyloid precursor protein transgenic mice.What is the evidence that tau pathology spreads through prion-like propagation?Tau-based therapies in neurodegeneration: opportunities and challenges.Amyloidogenesis of Tau protein.A liquid chromatography tandem mass spectroscopy approach for quantification of protein methylation stoichiometry.Minimotifs dysfunction is pervasive in neurodegenerative disorders
P2860
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P2860
Dual modification of Alzheimer's disease PHF-tau protein by lysine methylation and ubiquitylation: a mass spectrometry approach.
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
2011年论文
@zh
2011年论文
@zh-cn
name
Dual modification of Alzheimer ...... a mass spectrometry approach.
@ast
Dual modification of Alzheimer ...... a mass spectrometry approach.
@en
type
label
Dual modification of Alzheimer ...... a mass spectrometry approach.
@ast
Dual modification of Alzheimer ...... a mass spectrometry approach.
@en
prefLabel
Dual modification of Alzheimer ...... a mass spectrometry approach.
@ast
Dual modification of Alzheimer ...... a mass spectrometry approach.
@en
P2093
P2860
P1476
Dual modification of Alzheimer ...... a mass spectrometry approach.
@en
P2093
Austin J Yang
Jeff Kuret
Kristen E Funk
Peter Davies
Stefani N Thomas
Zhongping Liao
P2860
P2888
P304
P356
10.1007/S00401-011-0893-0
P577
2011-10-28T00:00:00Z