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Molecular Pathogenesis of the Tauopathies

Annual Review of Pathology: Mechanisms of Disease, 2019
The tauopathies constitute a group of diseases that have Tau inclusions in neurons or glia as their common denominator. In this review, we describe the biochemical and histological differences in Tau pathology that are characteristic of the spectrum of frontotemporal lobar degeneration as primary tauopathies and of Alzheimer's disease as a secondary ...
Götz, Jürgen   +2 more
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Tauopathy: An overview

Neuropathology, 2006
In this symposium, cutting‐edge data on neuropathology, pathological biochemistry and molecular biology of sporadic and familial tauopathies, as well as on the development of model animals, were presented and discussed by five expert neuropathologists.
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Tauopathies

2014
Tauopathies are neurodegenerative disorders characterized by the deposition of abnormal tau protein in the brain. The spectrum of tau pathologies expands beyond the traditionally discussed disease forms like Pick disease, progressive supranuclear palsy, corticobasal degeneration, and argyrophilic grain disease. Emerging entities and pathologies include
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Anatamopathological spectrum of tauopathies

Movement Disorders, 2003
The presence of tau-positive intraneuronal filamentous inclusions with or without additional inclusions in glial cells has been recognised as a major neuropathological feature in a significant group of neurodegenerative diseases, which are described as tauopathies.
Tamas, Revesz, Janice L, Holton
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Treatment Options for Tauopathies

Current Treatment Options in Neurology, 2012
To date, there are no approved and established pharmacologic treatment options for tauopathies, a very heterogenous group of neuropsychiatric diseases often leading to dementia and clinically diagnosed as atypical Parkinson syndromes. Among these so-called Parkinson plus syndromes are progressive supranuclear palsy (PSP), also referred to as Steele ...
Tarik, Karakaya   +3 more
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Animal models of tauopathies

Neuropathology, 2006
Intracellular fibrillar amyloid lesions comprised of tau proteins are pathological hallmarks in diverse neurodegenerative disorders. As models of these tauopathies, transgenic mice overexpressing tau with or without mutations discovered in familial tauopathies were generated.
Makoto, Higuchi   +2 more
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Clinicopathological features of the tauopathies

Biochemical Society Transactions, 2005
Developments in molecular neuropathology have led to protein-based classification systems for neurodegenerative disorders. Key proteins include α-synuclein, amyloid and tau. Alternative mRNA splicing and post-translational change, induced by a bewildering variety of protein modifying processes such as phosphorylation and ubiquitination, have generated ...
B, Murray, T, Lynch, M, Farrell
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Imaging biomarkers in tauopathies

Parkinsonism & Related Disorders, 2016
Abnormally aggregated tau protein is central to the pathophysiology of Alzheimer's disease, frontotemporal dementia variants, progressive supranuclear palsy, corticobasal degeneration and chronic traumatic encephalopathy. The post-mortem cortical density of hyperphosphorylated tau tangles correlates with pre-morbid cognitive dysfunction and neuron loss.
Dani, Melanie   +2 more
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Frontotemporal dementia and tauopathy

Current Neurology and Neuroscience Reports, 2001
The presence of abundant neurofibrillary lesions made of hyperphosphorylated tau proteins is the characteristic neuropathology of a subset of neurodegenerative disorders classified as "tauopathies." The discovery of mutations in the tau gene in frontotemporal dementia and parkinsonism linked to chromosome 17 (FTDP-17) constitutes convincing evidence ...
Y, Yoshiyama, V M, Lee, J Q, Trojanowski
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New classification of tauopathies

Revue Neurologique, 2018
Tauopathies are a group of neurodegenerative diseases characterized by pathological intracellular deposits of the protein tau. Isoform composition, morphology and anatomical distribution of cellular tau-immunoreactivities are defining distinct tauopathies as molecular pathological disease entities.
Höglinger, G. U.   +2 more
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