Restoring functional TDP-43 oligomers in ALS and laminopathic cellular models through baicalein-induced reconfiguration of TDP-43 aggregates

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Location: Deutsche Nationalbibliothek Frankfurt am Main

Extent: 1 Online-Ressource.

Language: Englisch

Bibliographic citation: Restoring functional TDP-43 oligomers in ALS and laminopathic cellular models through baicalein-induced reconfiguration of TDP-43 aggregates ; volume:14 ; number:1 ; day:26 ; month:2 ; year:2024 ; pages:1-9 ; date:12.2024
Scientific reports ; 14, Heft 1 (26.2.2024), 1-9, 12.2024

Creator: Chang, Hsiang-Yu
Wang, I-Fan

Contributor: SpringerLink (Online service)

DOI: 10.1038/s41598-024-55229-9

URN: urn:nbn:de:101:1-2405021313363.237932328510

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

Last update: 14.08.2025, 10:44 AM CEST

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Chang, Hsiang-Yu
Wang, I-Fan
SpringerLink (Online service)

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Antibody against TDP-43 phosphorylated at serine 375 suggests conformational differences of TDP-43 aggregates among FTLD–TDP subtypes

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Mechanisms and models of TDP-43 proteinopathies

TDP-43 regulates cancer-associated microRNAs

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Antibody against TDP-43 phosphorylated at serine 375 suggests conformational differences of TDP-43 aggregates among FTLD–TDP subtypes

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

Restoring expression of Stathmin-2: a novel strategy to treat TDP-43 proteinopathies

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

Mechanisms and models of TDP-43 proteinopathies

TDP-43 regulates cancer-associated microRNAs

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Restoring functional TDP-43 oligomers in ALS and laminopathic cellular models through baicalein-induced reconfiguration of TDP-43 aggregates

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Other Objects (12)

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

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

Restoring expression of Stathmin-2: a novel strategy to treat TDP-43 proteinopathies

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

TDP-43 regulates cancer-associated microRNAs

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

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

Restoring expression of Stathmin-2: a novel strategy to treat TDP-43 proteinopathies

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

TDP-43 regulates cancer-associated microRNAs

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

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

Restoring expression of Stathmin-2: a novel strategy to treat TDP-43 proteinopathies

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

TDP-43 regulates cancer-associated microRNAs

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