نتایج جستجو برای: tau protein

تعداد نتایج: 1249886  

Journal: :Human molecular genetics 2011
Lili C Kudo Liubov Parfenova Guijie Ren Nancy Vi Maria Hui Zhongcai Ma Kimbley Lau Michelle Gray Fawzia Bardag-Gorce Martina Wiedau-Pazos Koon-Sea Hui Stanislav L Karsten

Accumulation of neurotoxic hyperphosphorylated TAU protein is a major pathological hallmark of Alzheimer disease and other neurodegenerative dementias collectively called tauopathies. Puromycin-sensitive aminopeptidase (PSA/NPEPPS) is a novel modifier of TAU-induced neurodegeneration with neuroprotective effects via direct proteolysis of TAU protein. Here, to examine the effects of PSA/NPEPPS o...

2016
Val J. Lowe Geoffry Curran Ping Fang Amanda M. Liesinger Keith A. Josephs Joseph E. Parisi Kejal Kantarci Bradley F. Boeve Mukesh K. Pandey Tyler Bruinsma David S. Knopman David T. Jones Leonard Petrucelli Casey N. Cook Neill R. Graff-Radford Dennis W. Dickson Ronald C. Petersen Clifford R. Jack Melissa E. Murray

BACKGROUND It is essential to determine the specificity of AV-1451 PET for tau in brain imaging by using pathological comparisons. We performed autoradiography in autopsy-confirmed Alzheimer disease and other neurodegenerative disorders to evaluate the specificity of AV-1451 binding for tau aggregates. METHODS Tissue samples were selected that had a variety of dementia-related neuropathologie...

2014
Virginia Meyer Paul D. Dinkel Emily Rickman Hager Martin Margittai

The propagation of Tau pathology in Alzheimer's disease (AD) is thought to proceed through templated conversion of Tau protein into fibrils and cell-to-cell transfer of elongation-competent seeds. To investigate the efficiency of Tau conversion, we adapted the protein misfolding cyclic amplification assay used for the conversion of prions. Utilizing heparin as a cofactor and employing repetitiv...

2017
Lindsey B. Shelton John Koren Laura J. Blair

The ATP-dependent 90 kDa heat shock protein, Hsp90, is a major regulator of protein triage, from assisting in nascent protein folding to refolding or degrading aberrant proteins. Tau, a microtubule associated protein, aberrantly accumulates in Alzheimer's disease (AD) and other neurodegenerative diseases, deemed tauopathies. Hsp90 binds to and regulates tau fate in coordination with a diverse g...

Journal: :Ageing and neurodegenerative diseases 2022

Alzheimer’s disease (AD) is a progressive neurodegenerative disorder characterized by two pathological hallmark lesions: extracellular plaques composed of ?-amyloid (A?) peptide and intracellular neurofibrillary tangles made up highly phosphorylated tau protein. Over the past decades, most disease-modifying therapies against AD have been developed mainly on basis amyloid cascade hypothesis with...

Journal: :Brain : a journal of neurology 2009
Fei Liu Jianhua Shi Hitoshi Tanimukai Jinhua Gu Jianlan Gu Inge Grundke-Iqbal Khalid Iqbal Cheng-Xin Gong

It has been established for a long time that brain glucose metabolism is impaired in Alzheimer's disease. Recent studies have demonstrated that impaired brain glucose metabolism precedes the appearance of clinical symptoms, implying its active role in the development of Alzheimer's disease. However, the molecular mechanism by which this impairment contributes to the disease is not known. In thi...

Journal: :Biochemical Society transactions 2012
Yipeng Wang Eckhard Mandelkow

Tau aggregates are present in several neurodegenerative diseases and correlate with the severity of memory deficit in AD (Alzheimer's disease). However, the triggers of tau aggregation and tau-induced neurodegeneration are still elusive. The impairment of protein-degradation systems might play a role in such processes, as these pathways normally keep tau levels at a low level which may prevent ...

2016
Mathilde Wauters Ruddy Wattiez Laurence Ris

Tau protein is mainly intracellular. However, several studies have demonstrated that full-length Tau can be released into the interstitial fluid of the brain. The physiological or pathological function of this extracellular Tau remains unknown. Moreover, as evidence suggests, extracellular Tau aggregates can be internalized by neurons, seeding Tau aggregation. However, much less is known about ...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1975
M D Weingarten A H Lockwood S Y Hwo M W Kirschner

A heat stable protein essentail for microtubule assembly has been isolated. This protein, which we designate tau (tau), is present in association with tubulin purified from porcine brain by repeated cycles of polymerization. Tau is separated from tubulin by ion exchange chromatography on phosphocellulose. In the absence of tau, tubulin exists entirely as a 6S dimer of two polypeptide chains (al...

Journal: :Neuron 1996
Estelle Sontag Viyada Nunbhakdi-Craig Gloria Lee George S. Bloom Marc C. Mumby

Recently, we reported that a pool of protein phosphatase 2A (PP2A) is associated with microtubules. Here, we demonstrate that specific isoforms of PP2A bind and dephosphorylate the neuronal microtubule-associated protein tau. Coexpression of tau and SV40 small t, a specific inhibitor of PP2A, in CV-1, NIH 3T3, or NT2 cells induced the phosphorylation of tau at multiple sites, including Ser-199,...

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