Progranulin reduces insoluble TDP-43 levels, slows down axonal degeneration and prolongs survival in mutant TDP-43 mice

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Location: Deutsche Nationalbibliothek Frankfurt am Main

ISSN: 1750-1326

Extent: Online-Ressource

Language: Englisch

Notes: online resource.

Bibliographic citation: 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

Creator: Beel, Sander

Contributor: 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: urn:nbn:de:101:1-2018112122345928809796

Rights: Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.

Last update: 14.08.2025, 10:51 AM CEST

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Associated

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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Progranulin and TDP-43: Mechanistic Links and Future Directions

Disease‐linked TDP‐43 hyperphosphorylation suppresses TDP‐43 condensation and aggregation

The effect of TDP-43 antibodies on TDP-43 aggregation and toxicity

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

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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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Mechanisms and models of TDP-43 proteinopathies

Progranulin and TDP-43: Mechanistic Links and Future Directions

Disease‐linked TDP‐43 hyperphosphorylation suppresses TDP‐43 condensation and aggregation

The effect of TDP-43 antibodies on TDP-43 aggregation and toxicity

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

Cytotoxic immune cells do not affect TDP-43 and p62 sarcoplasmic aggregation but influence TDP-43 localisation

Mechanisms and models of TDP-43 proteinopathies

Progranulin and TDP-43: Mechanistic Links and Future Directions

Disease‐linked TDP‐43 hyperphosphorylation suppresses TDP‐43 condensation and aggregation

The effect of TDP-43 antibodies on TDP-43 aggregation and toxicity

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

Cytotoxic immune cells do not affect TDP-43 and p62 sarcoplasmic aggregation but influence TDP-43 localisation

Mechanisms and models of TDP-43 proteinopathies

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Progranulin reduces insoluble TDP-43 levels, slows down axonal degeneration and prolongs survival in mutant TDP-43 mice

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Other Objects (12)

Progranulin and TDP-43: Mechanistic Links and Future Directions

Disease‐linked TDP‐43 hyperphosphorylation suppresses TDP‐43 condensation and aggregation

The effect of TDP-43 antibodies on TDP-43 aggregation and toxicity

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

Cytotoxic immune cells do not affect TDP-43 and p62 sarcoplasmic aggregation but influence TDP-43 localisation

Mechanisms and models of TDP-43 proteinopathies

Progranulin and TDP-43: Mechanistic Links and Future Directions

Disease‐linked TDP‐43 hyperphosphorylation suppresses TDP‐43 condensation and aggregation

The effect of TDP-43 antibodies on TDP-43 aggregation and toxicity

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

Cytotoxic immune cells do not affect TDP-43 and p62 sarcoplasmic aggregation but influence TDP-43 localisation

Mechanisms and models of TDP-43 proteinopathies

Progranulin and TDP-43: Mechanistic Links and Future Directions

Disease‐linked TDP‐43 hyperphosphorylation suppresses TDP‐43 condensation and aggregation

The effect of TDP-43 antibodies on TDP-43 aggregation and toxicity

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

Cytotoxic immune cells do not affect TDP-43 and p62 sarcoplasmic aggregation but influence TDP-43 localisation

Mechanisms and models of TDP-43 proteinopathies

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