The ubiquitin thioesterase YOD1 ameliorates mutant Huntingtin induced pathology in Drosophila

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Location: Deutsche Nationalbibliothek Frankfurt am Main

Extent: 1 Online-Ressource.

Language: Englisch

Bibliographic citation: The ubiquitin thioesterase YOD1 ameliorates mutant Huntingtin induced pathology in Drosophila ; volume:13 ; number:1 ; day:11 ; month:12 ; year:2023 ; pages:1-13 ; date:12.2023
Scientific reports ; 13, Heft 1 (11.12.2023), 1-13, 12.2023

Creator: Farkas, Anita
Zsindely, Nóra
Nagy, Gábor
Kovács, Levente
Deák, Péter
Bodai, László

Contributor: SpringerLink (Online service)

DOI: 10.1038/s41598-023-49241-8

URN: urn:nbn:de:101:1-2024022614293305065856

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

Last update: 14.08.2025, 11:01 AM CEST

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Associated

Farkas, Anita
Zsindely, Nóra
Nagy, Gábor
Kovács, Levente
Deák, Péter
Bodai, László
SpringerLink (Online service)

Other Objects (12)

Dynamic recruitment of ubiquitin to mutant huntingtin inclusion bodies

Quantifying mutant huntingtin protein in human cerebrospinal fluid to support the development of huntingtin-lowering therapies

Truncation of mutant huntingtin in knock-in mice demonstrates exon1 huntingtin is a key pathogenic form

A Specific Mini‐Intrabody Mediates Lysosome Degradation of Mutant Huntingtin

Human-to-mouse prion-like propagation of mutant huntingtin protein

Comparative Analysis of Mutant Huntingtin Binding Partners in Yeast Species

Mutant Huntingtin toxicity modifiers revealed by a spatiotemporal proteomic profiling

Targeting Tyro3 ameliorates a model of PGRN-mutant FTLD-TDP via tau-mediated synaptic pathology

Author Correction: Truncation of mutant huntingtin in knock-in mice demonstrates exon1 huntingtin is a key pathogenic form

ROCK-phosphorylated vimentin modifies mutant huntingtin aggregation via sequestration of IRBIT

Hochschulschrift

Generation and charactarization of BACHD rats expressing full-length human mutant huntingtin

Soluble mutant huntingtin drives early human pathogenesis in Huntington’s disease

Dynamic recruitment of ubiquitin to mutant huntingtin inclusion bodies

Quantifying mutant huntingtin protein in human cerebrospinal fluid to support the development of huntingtin-lowering therapies

Truncation of mutant huntingtin in knock-in mice demonstrates exon1 huntingtin is a key pathogenic form

A Specific Mini‐Intrabody Mediates Lysosome Degradation of Mutant Huntingtin

Human-to-mouse prion-like propagation of mutant huntingtin protein

Comparative Analysis of Mutant Huntingtin Binding Partners in Yeast Species

Mutant Huntingtin toxicity modifiers revealed by a spatiotemporal proteomic profiling

Targeting Tyro3 ameliorates a model of PGRN-mutant FTLD-TDP via tau-mediated synaptic pathology

Author Correction: Truncation of mutant huntingtin in knock-in mice demonstrates exon1 huntingtin is a key pathogenic form

ROCK-phosphorylated vimentin modifies mutant huntingtin aggregation via sequestration of IRBIT

Hochschulschrift

Generation and charactarization of BACHD rats expressing full-length human mutant huntingtin

Soluble mutant huntingtin drives early human pathogenesis in Huntington’s disease

Dynamic recruitment of ubiquitin to mutant huntingtin inclusion bodies

Quantifying mutant huntingtin protein in human cerebrospinal fluid to support the development of huntingtin-lowering therapies

Truncation of mutant huntingtin in knock-in mice demonstrates exon1 huntingtin is a key pathogenic form

A Specific Mini‐Intrabody Mediates Lysosome Degradation of Mutant Huntingtin

Human-to-mouse prion-like propagation of mutant huntingtin protein

Comparative Analysis of Mutant Huntingtin Binding Partners in Yeast Species

Mutant Huntingtin toxicity modifiers revealed by a spatiotemporal proteomic profiling

Targeting Tyro3 ameliorates a model of PGRN-mutant FTLD-TDP via tau-mediated synaptic pathology

Author Correction: Truncation of mutant huntingtin in knock-in mice demonstrates exon1 huntingtin is a key pathogenic form

ROCK-phosphorylated vimentin modifies mutant huntingtin aggregation via sequestration of IRBIT

Hochschulschrift

Generation and charactarization of BACHD rats expressing full-length human mutant huntingtin

Soluble mutant huntingtin drives early human pathogenesis in Huntington’s disease

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The ubiquitin thioesterase YOD1 ameliorates mutant Huntingtin induced pathology in Drosophila

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Other Objects (12)

Dynamic recruitment of ubiquitin to mutant huntingtin inclusion bodies

Quantifying mutant huntingtin protein in human cerebrospinal fluid to support the development of huntingtin-lowering therapies

Truncation of mutant huntingtin in knock-in mice demonstrates exon1 huntingtin is a key pathogenic form

A Specific Mini‐Intrabody Mediates Lysosome Degradation of Mutant Huntingtin

Human-to-mouse prion-like propagation of mutant huntingtin protein

Comparative Analysis of Mutant Huntingtin Binding Partners in Yeast Species

Mutant Huntingtin toxicity modifiers revealed by a spatiotemporal proteomic profiling

Targeting Tyro3 ameliorates a model of PGRN-mutant FTLD-TDP via tau-mediated synaptic pathology

Author Correction: Truncation of mutant huntingtin in knock-in mice demonstrates exon1 huntingtin is a key pathogenic form

ROCK-phosphorylated vimentin modifies mutant huntingtin aggregation via sequestration of IRBIT

Generation and charactarization of BACHD rats expressing full-length human mutant huntingtin

Soluble mutant huntingtin drives early human pathogenesis in Huntington’s disease

Dynamic recruitment of ubiquitin to mutant huntingtin inclusion bodies

Quantifying mutant huntingtin protein in human cerebrospinal fluid to support the development of huntingtin-lowering therapies

Truncation of mutant huntingtin in knock-in mice demonstrates exon1 huntingtin is a key pathogenic form

A Specific Mini‐Intrabody Mediates Lysosome Degradation of Mutant Huntingtin

Human-to-mouse prion-like propagation of mutant huntingtin protein

Comparative Analysis of Mutant Huntingtin Binding Partners in Yeast Species

Mutant Huntingtin toxicity modifiers revealed by a spatiotemporal proteomic profiling

Targeting Tyro3 ameliorates a model of PGRN-mutant FTLD-TDP via tau-mediated synaptic pathology

Author Correction: Truncation of mutant huntingtin in knock-in mice demonstrates exon1 huntingtin is a key pathogenic form

ROCK-phosphorylated vimentin modifies mutant huntingtin aggregation via sequestration of IRBIT

Generation and charactarization of BACHD rats expressing full-length human mutant huntingtin

Soluble mutant huntingtin drives early human pathogenesis in Huntington’s disease

Dynamic recruitment of ubiquitin to mutant huntingtin inclusion bodies

Quantifying mutant huntingtin protein in human cerebrospinal fluid to support the development of huntingtin-lowering therapies

Truncation of mutant huntingtin in knock-in mice demonstrates exon1 huntingtin is a key pathogenic form

A Specific Mini‐Intrabody Mediates Lysosome Degradation of Mutant Huntingtin

Human-to-mouse prion-like propagation of mutant huntingtin protein

Comparative Analysis of Mutant Huntingtin Binding Partners in Yeast Species

Mutant Huntingtin toxicity modifiers revealed by a spatiotemporal proteomic profiling

Targeting Tyro3 ameliorates a model of PGRN-mutant FTLD-TDP via tau-mediated synaptic pathology

Author Correction: Truncation of mutant huntingtin in knock-in mice demonstrates exon1 huntingtin is a key pathogenic form

ROCK-phosphorylated vimentin modifies mutant huntingtin aggregation via sequestration of IRBIT

Generation and charactarization of BACHD rats expressing full-length human mutant huntingtin

Soluble mutant huntingtin drives early human pathogenesis in Huntington’s disease

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