Targeting the glycine-rich domain of TDP-43 with antibodies prevents its aggregation in vitro and reduces neurofilament levels in vivo

Targeting the glycine-rich domain of TDP-43 with antibodies prevents its aggregation in vitro and reduces neurofilament levels in vivo

Abstract Cytoplasmic aggregation and concomitant nuclear clearance of the RNA-binding protein TDP-43 are found in ~ 90% of cases of amyotrophic lateral sclerosis and ~ 45% of patients living with frontotemporal lobar degeneration, but no disease-modifying therapy is available. Antibody therapy targe...

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Bibliographic Details
Main Authors: Henrick Riemenschneider, Francesca Simonetti, Udit Sheth, Eszter Katona, Stefan Roth, Saskia Hutten, Daniel Farny, Meike Michaelsen, Brigitte Nuscher, Michael K. Schmidt, Andrew Flatley, Aloys Schepers, Lara A. Gruijs da Silva, Qihui Zhou, Thomas Klopstock, Arthur Liesz, Thomas Arzberger, Jochen Herms, Regina Feederle, Tania F. Gendron, Dorothee Dormann, Dieter Edbauer
Format: Article
Language:English
Published: BMC 2023-07-01
Series:Acta Neuropathologica Communications
Subjects:
Neurodegeneration
Amyotrophic lateral sclerosis
Frontotemporal dementia
TDP-43
Immunotherapy
Phase separation
Online Access:https://doi.org/10.1186/s40478-023-01592-z

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