A plant-based mutant huntingtin model-driven discovery of impaired expression of GTPCH and DHFR

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Location: Deutsche Nationalbibliothek Frankfurt am Main

ISSN: 1420-9071

Extent: Online-Ressource

Language: Englisch

Notes: online resource.

Bibliographic citation: A plant-based mutant huntingtin model-driven discovery of impaired expression of GTPCH and DHFR ; volume:79 ; number:11 ; day:17 ; month:10 ; year:2022 ; pages:1-19 ; date:11.2022
Cellular and molecular life sciences ; 79, Heft 11 (17.10.2022), 1-19, 11.2022

Creator: Hung, Chiu-Yueh
Zhu, Chuanshu
Kittur, Farooqahmed S.
He, Maotao
Arning, Erland
Zhang, Jianhui
Johnson, Asia J.
Jawa, Gurpreet S.
Thomas, Michelle D.
Ding, Tomas T.
Xie, Jiahua

Contributor: SpringerLink (Online service)

DOI: 10.1007/s00018-022-04587-6

URN: urn:nbn:de:101:1-2023020921162017669243

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

Last update: 14.08.2025, 10:53 AM CEST

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Associated

Hung, Chiu-Yueh
Zhu, Chuanshu
Kittur, Farooqahmed S.
He, Maotao
Arning, Erland
Zhang, Jianhui
Johnson, Asia J.
Jawa, Gurpreet S.
Thomas, Michelle D.
Ding, Tomas T.
Xie, Jiahua
SpringerLink (Online service)

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Dynamic recruitment of ubiquitin to mutant huntingtin inclusion bodies

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A plant-based mutant huntingtin model-driven discovery of impaired expression of GTPCH and DHFR

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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

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

The ubiquitin thioesterase YOD1 ameliorates mutant Huntingtin induced pathology in Drosophila

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

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

The ubiquitin thioesterase YOD1 ameliorates mutant Huntingtin induced pathology in Drosophila

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

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

The ubiquitin thioesterase YOD1 ameliorates mutant Huntingtin induced pathology in Drosophila

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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