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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Journal ArticleDOI
Vascular variant of prion protein cerebral amyloidosis with tau-positive neurofibrillary tangles: the phenotype of the stop codon 145 mutation in PRNP.
Bernardino Ghetti,Pedro Piccardo,Maria Grazia Spillantini,Yousuke Ichimiya,M. Porro,Francesco Perini,Tetsuyuki Kitamoto,Jun Tateishi,Charles Seiler,Blas Frangione,Orso Bugiani,Giorgio Giaccone,Frances Prelli,Michel Goedert,Stephen R. Dlouhy,Fabrizio Tagliavini +15 more
TL;DR: A PrP cerebral amyloid angiopathy (PrP-CAA) has been reported in diseases caused by PRNP mutations or in human transmissible spongiform encephalopathies as discussed by the authors.
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Tau mutations cause frontotemporal dementias.
TL;DR: The likely primary effect of the exonic mutations scribed atrophy of the frontal and temporal lobes of Pick’s disease is thus a reduced ability of mutated tau to interact with the cerebral cortex, often with additional, subcortical microtubules.
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Effects of frontotemporal dementia FTDP-17 mutations on heparin-induced assembly of tau filaments
TL;DR: Findings indicate that missense mutations in tau lead to frontotemporal dementia through potentially multiple mechanisms, namely the stimulation of heparin‐induced filament assembly of recombinant tau, despite the absence of any change in structure indicated by circular dichroism.
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Paradoxical activation of Raf by a novel Raf inhibitor.
Clare A Hall-Jackson,Patrick A. Eyers,Philip Cohen,Michel Goedert,F Tom Boyle,Neil Hewitt,Helen Plant,Philip Hedge +7 more
TL;DR: Raf appears to suppress its own activation by a novel feedback loop, such that inhibition is always counterbalanced by reactivation, implying that some agonists reported to trigger the cellular activation of c-Raf might actually be inhibitors of this enzyme, and that compounds which inhibit the kinase activity of Raf might not be useful as anticancer drugs.
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Structure-based classification of tauopathies
Yang Shi,Wenjuan Zhang,Yang Yang,Alexey G. Murzin,Benjamin Falcon,Abhay Kotecha,Mike van Beers,Airi Tarutani,Fuyuki Kametani,Holly J. Garringer,Ruben Vidal,G.I. Hallinan,Tammaryn Lashley,Yuko Saito,Shigeo Murayama,Mari Yoshida,H. Tanaka,Akiyoshi Kakita,Takeshi Ikeuchi,Andrew C Robinson,David M. A. Mann,Gabor G. Kovacs,Gabor G. Kovacs,Tamas Revesz,Bernardino Ghetti,Masato Hasegawa,Michel Goedert,Sjors H.W. Scheres +27 more
TL;DR: In this paper, the structures of tau filaments from progressive supranuclear palsy (PSP) define a new three-layered fold, which is similar to those from argyrophilic grain disease (AGD).