Reducing mutant Huntingtin protein expression in living cells by a newly identified RNA CAG binder
- Standort
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Deutsche Nationalbibliothek Frankfurt am Main
- Umfang
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Online-Ressource
- Sprache
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Englisch
- Erschienen in
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In: ACS Chemical Neuroscience, 9, 6, S. 1399-1408
- Ereignis
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Veröffentlichung
- (wo)
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Augsburg
- (wer)
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Universität Augsburg
- (wann)
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2018
- Ereignis
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Veröffentlichung
- (wer)
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American Chemical Society (ACS)
- (wann)
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2018
- Urheber
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Matthes, Frank
Massari, Serena
Bochicchio, Anna
Schorpp, Kenji
Schilling, Judith
Weber, Stephanie
Offermann, Nina
Desantis, Jenny
Wanker, Erich
Carloni, Paolo
Hadian, Kamyar
Tabarrini, Oriana
Rossetti, Giulia
Krauss, Sybille
- DOI
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10.1021/acschemneuro.8b00027
- URN
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urn:nbn:de:bvb:384-opus4-1094356
- Rechteinformation
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Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
-
15.08.2025, 07:33 MESZ
Datenpartner
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Beteiligte
- Matthes, Frank
- Massari, Serena
- Bochicchio, Anna
- Schorpp, Kenji
- Schilling, Judith
- Weber, Stephanie
- Offermann, Nina
- Desantis, Jenny
- Wanker, Erich
- Carloni, Paolo
- Hadian, Kamyar
- Tabarrini, Oriana
- Rossetti, Giulia
- Krauss, Sybille
- Universität Augsburg
- American Chemical Society (ACS)
Entstanden
- 2018
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Truncation of mutant huntingtin in knock-in mice demonstrates exon1 huntingtin is a key pathogenic form
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Correction: Huntingtin HTT1a is generated in a CAG repeat-length-dependent manner in human tissues
Author Correction: Truncation of mutant huntingtin in knock-in mice demonstrates exon1 huntingtin is a key pathogenic form
Cell-type-specific CAG repeat expansions and toxicity of mutant Huntingtin in human striatum and cerebellum
Attenuated huntingtin gene CAG nucleotide repeat size in individuals with Lynch syndrome
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
Huntingtin HTT1a is generated in a CAG repeat-length-dependent manner in human tissues
A Specific Mini‐Intrabody Mediates Lysosome Degradation of Mutant Huntingtin
Human-to-mouse prion-like propagation of mutant huntingtin protein
Mutant Huntingtin toxicity modifiers revealed by a spatiotemporal proteomic profiling
Comparative Analysis of Mutant Huntingtin Binding Partners in Yeast Species
Correction: Huntingtin HTT1a is generated in a CAG repeat-length-dependent manner in human tissues
Author Correction: Truncation of mutant huntingtin in knock-in mice demonstrates exon1 huntingtin is a key pathogenic form
Cell-type-specific CAG repeat expansions and toxicity of mutant Huntingtin in human striatum and cerebellum
Attenuated huntingtin gene CAG nucleotide repeat size in individuals with Lynch syndrome
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
Huntingtin HTT1a is generated in a CAG repeat-length-dependent manner in human tissues
A Specific Mini‐Intrabody Mediates Lysosome Degradation of Mutant Huntingtin
Human-to-mouse prion-like propagation of mutant huntingtin protein
Mutant Huntingtin toxicity modifiers revealed by a spatiotemporal proteomic profiling
Comparative Analysis of Mutant Huntingtin Binding Partners in Yeast Species
Correction: Huntingtin HTT1a is generated in a CAG repeat-length-dependent manner in human tissues