A transient protein folding response targets aggregation in the early phase of TDP-43-mediated neurodegeneration

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Location: Deutsche Nationalbibliothek Frankfurt am Main

Extent: 1 Online-Ressource.

Language: Englisch

Bibliographic citation: A transient protein folding response targets aggregation in the early phase of TDP-43-mediated neurodegeneration ; volume:15 ; number:1 ; day:19 ; month:2 ; year:2024 ; pages:1-23 ; date:12.2024
Nature Communications ; 15, Heft 1 (19.2.2024), 1-23, 12.2024

Creator: San Gil, Rebecca
Pascovici, Dana
Venturato, Juliana
Brown-Wright, Heledd
Mehta, Prachi
Madrid San Martin, Lidia
Wu, Jemma
Luan, Wei
Chui, Yi Kit
Bademosi, Adekunle T.
Swaminathan, Shilpa
Naidoo, Serey
Berning, Britt A.
Wright, Amanda L.
Keating, Sean S.
Curtis, Maurice A.
Faull, Richard L. M.
Lee, John D.
Ngo, Shyuan T.
Lee, Albert
Morsch, Marco
Chung, Roger S.
Scotter, Emma
Lisowski, Leszek
Mirzaei, Mehdi
Walker, Adam K.

Contributor: SpringerLink (Online service)

DOI: 10.1038/s41467-024-45646-9

URN: urn:nbn:de:101:1-2404260724109.166206476958

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

Last update: 14.08.2025, 11:02 AM CEST

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Associated

San Gil, Rebecca
Pascovici, Dana
Venturato, Juliana
Brown-Wright, Heledd
Mehta, Prachi
Madrid San Martin, Lidia
Wu, Jemma
Luan, Wei
Chui, Yi Kit
Bademosi, Adekunle T.
Swaminathan, Shilpa
Naidoo, Serey
Berning, Britt A.
Wright, Amanda L.
Keating, Sean S.
Curtis, Maurice A.
Faull, Richard L. M.
Lee, John D.
Ngo, Shyuan T.
Lee, Albert
Morsch, Marco
Chung, Roger S.
Scotter, Emma
Lisowski, Leszek
Mirzaei, Mehdi
Walker, Adam K.
SpringerLink (Online service)

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Aggregation of TDP-43 fragments triggers cellular aberrant function: implication in neurodegeneration

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

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Does a loss of TDP-43 function cause neurodegeneration?

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m1A in CAG repeat RNA binds to TDP-43 and induces neurodegeneration

Aggregation of TDP-43 fragments triggers cellular aberrant function: implication in neurodegeneration

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

Rodent Models of TDP-43 Proteinopathy: Investigating the Mechanisms of TDP-43-Mediated Neurodegeneration

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Aggregation-prone TDP-43 sequesters and drives pathological transitions of free nuclear TDP-43

Reducing TDP-43 aggregation does not prevent its cytotoxicity

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ALS-linked TDP-43M337V knock-in mice exhibit splicing deregulation without neurodegeneration

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A transient protein folding response targets aggregation in the early phase of TDP-43-mediated neurodegeneration

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Other Objects (12)

Aggregation of TDP-43 fragments triggers cellular aberrant function: implication in neurodegeneration

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

Rodent Models of TDP-43 Proteinopathy: Investigating the Mechanisms of TDP-43-Mediated Neurodegeneration

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

Does a loss of TDP-43 function cause neurodegeneration?

Folding and aggregation of amyloid peptides

Aggregation-prone TDP-43 sequesters and drives pathological transitions of free nuclear TDP-43

Reducing TDP-43 aggregation does not prevent its cytotoxicity

Regulated protein aggregation: stress granules and neurodegeneration

Untersuchungen zur Aggregation des ALS-relevanten TDP-43(307-347)

ALS-linked TDP-43M337V knock-in mice exhibit splicing deregulation without neurodegeneration

m1A in CAG repeat RNA binds to TDP-43 and induces neurodegeneration

Aggregation of TDP-43 fragments triggers cellular aberrant function: implication in neurodegeneration

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

Rodent Models of TDP-43 Proteinopathy: Investigating the Mechanisms of TDP-43-Mediated Neurodegeneration

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

Does a loss of TDP-43 function cause neurodegeneration?

Folding and aggregation of amyloid peptides

Aggregation-prone TDP-43 sequesters and drives pathological transitions of free nuclear TDP-43

Reducing TDP-43 aggregation does not prevent its cytotoxicity

Regulated protein aggregation: stress granules and neurodegeneration

Untersuchungen zur Aggregation des ALS-relevanten TDP-43(307-347)

ALS-linked TDP-43M337V knock-in mice exhibit splicing deregulation without neurodegeneration

m1A in CAG repeat RNA binds to TDP-43 and induces neurodegeneration

Aggregation of TDP-43 fragments triggers cellular aberrant function: implication in neurodegeneration

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

Rodent Models of TDP-43 Proteinopathy: Investigating the Mechanisms of TDP-43-Mediated Neurodegeneration

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

Does a loss of TDP-43 function cause neurodegeneration?

Folding and aggregation of amyloid peptides

Aggregation-prone TDP-43 sequesters and drives pathological transitions of free nuclear TDP-43

Reducing TDP-43 aggregation does not prevent its cytotoxicity

Regulated protein aggregation: stress granules and neurodegeneration

Untersuchungen zur Aggregation des ALS-relevanten TDP-43(307-347)

ALS-linked TDP-43M337V knock-in mice exhibit splicing deregulation without neurodegeneration

m1A in CAG repeat RNA binds to TDP-43 and induces neurodegeneration

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