M
Michel Goedert
Researcher at Laboratory of Molecular Biology
Publications - 353
Citations - 72555
Michel Goedert is an academic researcher from Laboratory of Molecular Biology. The author has contributed to research in topics: Tau protein & Frontotemporal dementia and parkinsonism linked to chromosome 17. The author has an hindex of 125, co-authored 337 publications receiving 64671 citations. Previous affiliations of Michel Goedert include University of Pisa & Max Planck Society.
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Filamentous nerve cell inclusions in neurodegenerative diseases: tauopathies and alpha-synucleinopathies.
TL;DR: It is established that tauopathies and alpha-synucleinopathies account for most late-onset neurodegenerative diseases in man and the formation of intracellular filamentous inclusions might be the gain of toxic function that leads to the demise of affected brain cells.
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Tau proteins and neurofibrillary degeneration.
TL;DR: The paired helical filament is the major fibrous component of neurofibrillary pathology in Alzheimer's disease and the microtubule‐associated protein tau forms an important, if not the sole, constituent of the pairedHelical filament.
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Tau protein and neurodegeneration
TL;DR: The identification of mutations in Tau as the cause of FTDP-17 established that dysfunction or misregulation of tau protein is sufficient to cause neurodegeneration and dementia and is leading to the development of good transgenic animal models of the tauopathies.
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Pick's disease : hyperphosphorylated tau protein segregates to the somatoaxonal compartment
TL;DR: It is shown that hyperphosphorylated tau segregates to different neuronal compartments in the two diseases, with a somatoaxonal distribution in Pick’s disease and a somatodendritic distribution in Alzheimer's disease.
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Characterization of mAb AP422, a novel phosphorylation-dependent monoclonal antibody against tau protein.
Masato Hasegawa,Masato Hasegawa,Ross Jakes,R.A. Crowther,Virginia M.-Y. Lee,Yasuo Ihara,Michel Goedert +6 more
TL;DR: It is shown that AP422 is the most specific anti‐tau antibody available for detecting the neurofibrillary lesions of Alzheimer's disease and that Ser‐422 in tau is a good in vitro substrate for mitogen‐activated protein kinase, but not for glycogen synthase kinase‐3 or neuronal cdc2‐like kinase.