Znf179 E3 ligase-mediated TDP-43 polyubiquitination is involved in TDP-43- ubiquitinated inclusions (UBI) (+)-related neurodegenerative pathology

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Standort: Deutsche Nationalbibliothek Frankfurt am Main

ISSN: 1423-0127

Umfang: Online-Ressource

Sprache: Englisch

Anmerkungen: online resource.

Erschienen in: Znf179 E3 ligase-mediated TDP-43 polyubiquitination is involved in TDP-43- ubiquitinated inclusions (UBI) (+)-related neurodegenerative pathology ; volume:25 ; number:1 ; day:8 ; month:11 ; year:2018 ; pages:1-17 ; date:12.2018
Journal of biomedical science ; 25, Heft 1 (8.11.2018), 1-17, 12.2018

Urheber: Lee, Yi-Chao
Huang, Wan-Chen
Lin, Jiann-Her
Kao, Tzu-Jen
Lin, Hui-Ching
Lee, Kuen-Haur
Lin, Hsin-Chuan
Shen, Che-Kun James
Chang, Wen-Chang
Huang, Chi-Chen

Beteiligte Personen und Organisationen: SpringerLink (Online service)

DOI: 10.1186/s12929-018-0479-4

URN: urn:nbn:de:101:1-2018122619153413999494

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

Letzte Aktualisierung: 14.08.2025, 10:48 MESZ

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Beteiligte

Lee, Yi-Chao
Huang, Wan-Chen
Lin, Jiann-Her
Kao, Tzu-Jen
Lin, Hui-Ching
Lee, Kuen-Haur
Lin, Hsin-Chuan
Shen, Che-Kun James
Chang, Wen-Chang
Huang, Chi-Chen
SpringerLink (Online service)

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Znf179 E3 ligase-mediated TDP-43 polyubiquitination is involved in TDP-43- ubiquitinated inclusions (UBI) (+)-related neurodegenerative pathology

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Ähnliche Objekte (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

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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

Role of acetylation in TDP-43 pathophysiology

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

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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

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TDP-43 regulates cancer-associated microRNAs

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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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