Progranulin reduces insoluble TDP-43 levels, slows down axonal degeneration and prolongs survival in mutant TDP-43 mice
- Standort
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Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
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1750-1326
- Umfang
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Online-Ressource
- Sprache
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Englisch
- Anmerkungen
-
online resource.
- Erschienen in
-
Progranulin reduces insoluble TDP-43 levels, slows down axonal degeneration and prolongs survival in mutant TDP-43 mice ; volume:13 ; number:1 ; day:16 ; month:10 ; year:2018 ; pages:1-9 ; date:12.2018
Molecular neurodegeneration ; 13, Heft 1 (16.10.2018), 1-9, 12.2018
- Urheber
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Beel, Sander
- Beteiligte Personen und Organisationen
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Herdewyn, Sarah
Fazal, Raheem
De Decker, Mathias
Moisse, Matthieu
Robberecht, Wim
Van Den Bosch, Ludo
Van Damme, Philip
SpringerLink (Online service)
- DOI
-
10.1186/s13024-018-0288-y
- URN
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urn:nbn:de:101:1-2018112122345928809796
- Rechteinformation
-
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
-
14.08.2025, 10:51 MESZ
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Beteiligte
- Beel, Sander
- Herdewyn, Sarah
- Fazal, Raheem
- De Decker, Mathias
- Moisse, Matthieu
- Robberecht, Wim
- Van Den Bosch, Ludo
- Van Damme, Philip
- SpringerLink (Online service)
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Disease‐linked TDP‐43 hyperphosphorylation suppresses TDP‐43 condensation and aggregation
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Antibody against TDP-43 phosphorylated at serine 375 suggests conformational differences of TDP-43 aggregates among FTLD–TDP subtypes
Progranulin haploinsufficiency mediates cytoplasmic TDP-43 aggregation with lysosomal abnormalities in human microglia
Evidence of cerebellar TDP-43 loss of function in FTLD-TDP
Aggregation-prone TDP-43 sequesters and drives pathological transitions of free nuclear TDP-43
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Cytotoxic immune cells do not affect TDP-43 and p62 sarcoplasmic aggregation but influence TDP-43 localisation
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Disease‐linked TDP‐43 hyperphosphorylation suppresses TDP‐43 condensation and aggregation
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Antibody against TDP-43 phosphorylated at serine 375 suggests conformational differences of TDP-43 aggregates among FTLD–TDP subtypes
Progranulin haploinsufficiency mediates cytoplasmic TDP-43 aggregation with lysosomal abnormalities in human microglia
Evidence of cerebellar TDP-43 loss of function in FTLD-TDP
Aggregation-prone TDP-43 sequesters and drives pathological transitions of free nuclear TDP-43
Rodent Models of TDP-43 Proteinopathy: Investigating the Mechanisms of TDP-43-Mediated Neurodegeneration
Heteromeric amyloid filaments of ANXA11 and TDP-43 in FTLD-TDP type C
Spreading of TDP-43 pathology via pyramidal tract induces ALS-like phenotypes in TDP-43 transgenic mice
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