نتایج جستجو برای: kendalls tau

تعداد نتایج: 20931  

Journal: :Neuron 2010
Brian R. Hoover Miranda N. Reed Jianjun Su Rachel D. Penrod Linda A. Kotilinek Marianne K. Grant Rose Pitstick George A. Carlson Lorene M. Lanier Li-Lian Yuan Karen H. Ashe Dezhi Liao

The microtubule-associated protein tau accumulates in Alzheimer's and other fatal dementias, which manifest when forebrain neurons die. Recent advances in understanding these disorders indicate that brain dysfunction precedes neurodegeneration, but the role of tau is unclear. Here, we show that early tau-related deficits develop not from the loss of synapses or neurons, but rather as a result o...

2017
Kaoru Yamada

The pathological aggregation of tau protein is a hallmark of a set of neurodegenerative diseases collectively referred to as tauopathies. Tau aggregates independently in each neuron, but this aggregation can also occur in a non-cell autonomous manner in which aggregated tau is transmitted from one cell to another. Such trans-cellular propagation is initiated by the uptake of extracellular tau, ...

2016
Robert Y. K. Lai Charles R. Harrington Claude M. Wischik

Alzheimer's disease is characterized by redistribution of the tau protein pool from soluble to aggregated states. Aggregation forms proteolytically stable core polymers restricted to the repeat domain, and this binding interaction has prion-like properties. We have compared the binding properties of tau and tubulin in vitro using a system in which we can measure binding affinities for proteins ...

Journal: :Neuron 2015
Yingjun Zhao I-Chu Tseng Charles J. Heyser Edward Rockenstein Michael Mante Anthony Adame Qiuyang Zheng Timothy Huang Xin Wang Pharhad E. Arslan Paramita Chakrabarty Chengbiao Wu Guojun Bu William C. Mobley Yun-wu Zhang Peter St. George-Hyslop Eliezer Masliah Paul Fraser Huaxi Xu

Progressive supranuclear palsy (PSP) is a movement disorder characterized by tau neuropathology where the underlying mechanism is unknown. An SNP (rs1768208 C/T) has been identified as a strong risk factor for PSP. Here, we identified a much higher T-allele occurrence and increased levels of the pro-apoptotic protein appoptosin in PSP patients. Elevations in appoptosin correlate with activated ...

2014
Naruhiko Sahara Miyuki Murayama Makoto Higuchi Tetsuya Suhara Akihiko Takashima

Alzheimer's disease is a progressive dementia that is characterized by a loss of recent memory. Evidence has accumulated to support the hypothesis that synapses are critical storage sites for memory. However, it is still uncertain whether tau protein is involved in associative memory storage and whether tau is distributed in mature brain synapses. To address this question, we examined the synap...

Journal: :The Journal of biological chemistry 2007
Hirofumi Aoyagi Masato Hasegawa Akira Tamaoka

Frontotemporal dementia and parkinsonism linked to chromosome 17 (FTDP-17), an autosomal, dominantly inherited neurodegenerative disorder caused by tau gene mutations, is neuropathologically characterized by intraneuronal filamentous inclusions of hyperphosphorylated tau protein. Biochemical and immunocytochemical analyses have shown that only mutant tau is deposited in patients harboring P301L...

Journal: :Brain : a journal of neurology 2012
David J Irwin Todd J Cohen Murray Grossman Steven E Arnold Sharon X Xie Virginia M-Y Lee John Q Trojanowski

The microtubule-binding protein, tau, is the major component of neurofibrillary inclusions characteristic of Alzheimer's disease and related neurodegenerative tauopathies. When tau fibrillizes, it undergoes abnormal post-translational modifications resulting in decreased solubility and altered microtubule-stabilizing properties. Recently, we reported that the abnormal acetylation of tau at lysi...

2017
Wen Hu Feng Wu Yanchong Zhang Cheng-Xin Gong Khalid Iqbal Fei Liu

Microtubule-associated protein tau is hyperphosphorylated and aggregated in affected neurons in Alzheimer disease (AD) brains. The tau pathology starts from the entorhinal cortex (EC), spreads to the hippocampus and frontal and temporal cortices, and finally to all isocortex areas, but the cerebellum is spared from tau lesions. The molecular basis of differential vulnerability of different brai...

Journal: :The Journal of biological chemistry 2005
Kiran Bhaskar Shu-Hui Yen Gloria Lee

Microtubule-associated protein tau is the major component of the neurofibrillary tangles of Alzheimer disease (AD) and is genetically linked to frontotemporal dementias (FTDP-17). We have recently shown that tau interacts with the SH3 domain of Fyn, an Src family non-receptor tyrosine kinase, and is tyrosine-phosphorylated by Fyn on Tyr-18. Also, tyrosine-phosphorylated tau is present in the ne...

Journal: :Brain pathology 1999
L Buée A Delacourte

Neurodegenerative disorders referred to as tauopathies have cellular hyperphosphorylated tau protein aggregates in the absence of amyloid deposits. Comparative biochemistry of tau aggregates shows that they differ in both phosphorylation and content of tau isoforms. The six tau isoforms found in human brain contain either three (3R) or four microtubule-binding domains (4R). In Alzheimer's disea...

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