Protein Misfolding and Aggregation as a Therapeutic Target for Polyglutamine Diseases.

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Glutamine Codon Usage and polyQ Evolution in Primates Depend on the Q Stretch Length.

P2860

Q55042053-28F2A018-BB86-4A38-A9F8-29F73FED3DCB

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Protein Misfolding and Aggregation as a Therapeutic Target for Polyglutamine Diseases.

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http://www.wikidata.org/entity/Q45735441

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2017 nî lūn-bûn

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2017年の論文

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2017年学术文章

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2017年学术文章

@zh

2017年学术文章

@zh-cn

2017年学术文章

@zh-hans

2017年学术文章

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2017年学术文章

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2017年學術文章

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2017年學術文章

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name

Protein Misfolding and Aggregation as a Therapeutic Target for Polyglutamine Diseases.

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Protein Misfolding and Aggregation as a Therapeutic Target for Polyglutamine Diseases.

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type

Item

label

Protein Misfolding and Aggregation as a Therapeutic Target for Polyglutamine Diseases.

@en

Protein Misfolding and Aggregation as a Therapeutic Target for Polyglutamine Diseases.

@nl

prefLabel

Protein Misfolding and Aggregation as a Therapeutic Target for Polyglutamine Diseases.

@en

Protein Misfolding and Aggregation as a Therapeutic Target for Polyglutamine Diseases.

@nl

P1476

Protein Misfolding and Aggregation as a Therapeutic Target for Polyglutamine Diseases.

@en

P2093

Toshihide Takeuchi

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P2860

The Huntington's disease protein interacts with p53 and CREB-binding protein and represses transcription

Nuclear localization or inclusion body formation of ataxin-2 are not necessary for SCA2 pathogenesis in mouse or human

CHIP protects from the neurotoxicity of expanded and wild-type ataxin-1 and promotes their ubiquitination and degradation

Human single-chain Fv intrabodies counteract in situ huntingtin aggregation in cellular models of Huntington's disease

Allele-specific silencing of mutant huntingtin in rodent brain and human stem cells

A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes.

CAG expansions in a novel gene for Machado-Joseph disease at chromosome 14q32.1

Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic for the HD mutation

Unstable expansion of CAG repeat in hereditary dentatorubral-pallidoluysian atrophy (DRPLA)

Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease

P31

scholarly article

P356

10.3390/BRAINSCI7100128

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P433

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P50

Yoshitaka Nagai

P577

2017-10-11T00:00:00Z

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P698

29019918

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P932

5664055

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Protein Misfolding and Aggregation as a Therapeutic Target for Polyglutamine Diseases.

about

P2860

P2860

Protein Misfolding and Aggregation as a Therapeutic Target for Polyglutamine Diseases.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P31

P356

P433

P478

P50

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P31

P356

P433

P478

P50

P577

P698

P932