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
Cytosolic Fc receptor TRIM21 inhibits seeded tau aggregation.
William A. McEwan,Benjamin Falcon,Marina Vaysburd,Dean Clift,Adrian L. Oblak,Bernardino Ghetti,Michel Goedert,Leo C. James +7 more
TL;DR: In this article, the authors show that when misfolded tau assemblies enter the cell, they can be detected and neutralized via a danger response mediated by tau-associated antibodies and the cytosolic Fc receptor tripartite motif protein 21 (TRIM21).
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A role for FKBP52 in Tau protein function
Béatrice Chambraud,Elodie Sardin,Julien Giustiniani,Omar Dounane,Michael Schumacher,Michel Goedert,Etienne-Emile Baulieu +6 more
TL;DR: It was found that FKBP52, which is abundant in brain, binds directly and specifically to Tau, especially in its hyperphosphorylated form, which indicates a role for FK BP52 in Tau function and may help to decipher and modulate the events involved in Tau-induced neurodegeneration.
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Pathogenesis of the Tauopathies
TL;DR: The hyperphosphorylated sites are similar between diseases, but filament morphologies and tau isoform compositions vary, consistent with the existence of multiple tau conformers and recent findings have provided experimental support for this concept.
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Analysis of tau phosphorylation and truncation in a mouse model of human tauopathy.
Patrice Delobel,Isabelle Lavenir,Graham Fraser,Esther Ingram,Max Holzer,Bernardino Ghetti,Maria Grazia Spillantini,R. Anthony Crowther,Michel Goedert +8 more
TL;DR: The late appearance and low abundance of tau ending at D421 indicate that it is unlikely that truncation at this site is necessary for the assembly of t Tau into filaments in Alzheimer's disease and other tauopathies.
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Expression of APP in transgenic mice: a comparison of neuron-specific promoters.
Kerstin Andrä,Dorothee Abramowski,Mairead Duke,Alphonse Probst,Karl-Heinz Wiederhold,Kurt Bürki,Michel Goedert,Bernd Sommer,Matthias Staufenbiel +8 more
TL;DR: Although the initial histological examinations did not reveal any alterations characteristic of AD, further studied will be required, variable reactivity of human APP in cell bodies was shown by immunocytochemistry and protein levels paralleled mRNA levels reaching or exceeding the amount of endogenous APP.