ROCK-phosphorylated vimentin modifies mutant huntingtin aggregation via sequestration of IRBIT
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
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1750-1326
- Extent
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Online-Ressource
- Language
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Englisch
- Notes
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online resource.
- Bibliographic citation
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ROCK-phosphorylated vimentin modifies mutant huntingtin aggregation via sequestration of IRBIT ; volume:7 ; number:1 ; day:28 ; month:8 ; year:2012 ; pages:1-12 ; date:12.2012
Molecular neurodegeneration ; 7, Heft 1 (28.8.2012), 1-12, 12.2012
- Creator
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Bauer, Peter O.
- Contributor
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Hudec, Roman
Goswami, Anand
Kurosawa, Masaru
MATSUMOTO, GEN
Mikoshiba, Katsuhiko
Nukina, Nobuyuki
SpringerLink (Online service)
- DOI
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10.1186/1750-1326-7-43
- URN
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urn:nbn:de:1111-2016073069051
- Rights
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Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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14.08.2025, 10:44 AM CEST
Data provider
This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Bauer, Peter O.
- Hudec, Roman
- Goswami, Anand
- Kurosawa, Masaru
- MATSUMOTO, GEN
- Mikoshiba, Katsuhiko
- Nukina, Nobuyuki
- SpringerLink (Online service)
Other Objects (12)
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Cyclized NDGA modifies dynamic α-synuclein monomers preventing aggregation and toxicity
HAP40 modulates mutant Huntingtin aggregation and toxicity in Huntington’s disease mice
Huntingtin assoziierte Proteine
Huntingtin Lowering Strategies
Vimentin, Plectin
Nucleation of Huntingtin Aggregation Proceeds via Conformational Conversion of Pre‐Formed, Sparsely‐Populated Tetramers
Molekulare Analyse der Huntingtin-Aggregation und deren Modulation durch das eukaryontische Chaperonin TRiC
TBK1 phosphorylates mutant Huntingtin and suppresses its aggregation and toxicity in Huntington's disease models
The protein SS18L1 is a potent suppressor of polyQmediated huntingtin aggregation and toxicity
The protein SS18L1 is a potent suppressor of polyQ-mediated huntingtin aggregation and toxicity
Impact of frameshifting on aggregation of huntingtin exon 1
Conformational dynamics and aggregation of Huntingtin Exon 1 in living cells
Cyclized NDGA modifies dynamic α-synuclein monomers preventing aggregation and toxicity
HAP40 modulates mutant Huntingtin aggregation and toxicity in Huntington’s disease mice
Huntingtin assoziierte Proteine
Huntingtin Lowering Strategies
Vimentin, Plectin
Nucleation of Huntingtin Aggregation Proceeds via Conformational Conversion of Pre‐Formed, Sparsely‐Populated Tetramers
Molekulare Analyse der Huntingtin-Aggregation und deren Modulation durch das eukaryontische Chaperonin TRiC
TBK1 phosphorylates mutant Huntingtin and suppresses its aggregation and toxicity in Huntington's disease models
The protein SS18L1 is a potent suppressor of polyQmediated huntingtin aggregation and toxicity
The protein SS18L1 is a potent suppressor of polyQ-mediated huntingtin aggregation and toxicity
Impact of frameshifting on aggregation of huntingtin exon 1
Conformational dynamics and aggregation of Huntingtin Exon 1 in living cells
Cyclized NDGA modifies dynamic α-synuclein monomers preventing aggregation and toxicity
HAP40 modulates mutant Huntingtin aggregation and toxicity in Huntington’s disease mice
Huntingtin assoziierte Proteine
Huntingtin Lowering Strategies
Vimentin, Plectin
Nucleation of Huntingtin Aggregation Proceeds via Conformational Conversion of Pre‐Formed, Sparsely‐Populated Tetramers
Molekulare Analyse der Huntingtin-Aggregation und deren Modulation durch das eukaryontische Chaperonin TRiC
TBK1 phosphorylates mutant Huntingtin and suppresses its aggregation and toxicity in Huntington's disease models
The protein SS18L1 is a potent suppressor of polyQmediated huntingtin aggregation and toxicity