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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Living Neurons with Tau Filaments Aberrantly Expose Phosphatidylserine and Are Phagocytosed by Microglia.
TL;DR: It is reported that living neurons with tau inclusions from P301S-tau mice expose abnormally high amounts of phosphatidylserine because of the production of reactive oxygen species (ROS).
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Cell-Mediated Neuroprotection in a Mouse Model of Human Tauopathy
David W. Hampton,Daniel J. Webber,Bilada Bilican,Michel Goedert,Maria Grazia Spillantini,Siddharthan Chandran +5 more
TL;DR: It is shown that a previously described mouse line transgenic for human P301S tau exhibits an age-related, layer-specific loss of superficial cortical neurons, similar to what has been observed in human frontotemporal dementias, and that focal neural precursor cell implantation, resulting in glial cell differentiation, leads to the sustained rescue of cortical neurons.
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Reduced binding of protein phosphatase 2A to tau protein with frontotemporal dementia and parkinsonism linked to chromosome 17 mutations.
Michel Goedert,Sivapong Satumtira,Ross Jakes,Michael J. Smith,Craig Kamibayashi,Charles L. White,Estelle Sontag +6 more
TL;DR: In vitro results indicate that FTDP‐17 mutations induce a significant decrease in the binding affinity of tau for PP2A in vivo, and it is proposed that altered protein‐protein interactions betweenPP2A and tau may contribute to FTDP•17 pathogenesis.
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Stress- and mitogen-induced phosphorylation of the synapse-associated protein SAP90/PSD-95 by activation of SAPK3/p38gamma and ERK1/ERK2.
Guadalupe Sabio,Guadalupe Sabio,Suzana Reuver,Carmen Feijoo,Masato Hasegawa,Gareth M. Thomas,Francisco Centeno,Sven Kuhlendahl,Sergio Leal-Ortiz,Michel Goedert,Craig C. Garner,Craig C. Garner,Ana Cuenda +12 more
TL;DR: It is demonstrated that SAP90 is a novel binding partner for SAPK3/p38gamma, a first physiological substrate described for SAP kenase and a novel substrate for ERK1/ERK2, and that phosphorylation of SAP90 may play a role in regulating protein-protein interactions at the synapse in response to adverse stress- or mitogen-related stimuli.
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Lewy body diseases and multiple system atrophy as alpha-synucleinopathies.
TL;DR: Genetics came to the rescue, taking us straight to the very core of the Lewy body filament, and settled this controversy in favour of the relevance of a-synuclein for the aetiology and pathogenesis of some familial cases of Parkinson’s disease.