Mutant huntingtin protein: a substrate for transglutaminase 1, 2, and 3. - Wikidata - awgldk - TriplyDB

Mutant huntingtin protein: a substrate for transglutaminase 1, 2, and 3.

Mutant huntingtin protein: a substrate for transglutaminase 1, 2, and 3.

http://www.wikidata.org/entity/Q40457537

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Mitochondrial aconitase is a transglutaminase 2 substrate: transglutamination is a probable mechanism contributing to high-molecular-weight aggregates of aconitase and loss of aconitase activity in Huntington disease brain Neuroprotective effects of calmodulin peptide 76-121aa: disruption of calmodulin binding to mutant huntingtin.DNA methylation status of nuclear-encoded mitochondrial genes underlies the tissue-dependent mitochondrial functions Inhibition of transglutaminase 2 mitigates transcriptional dysregulation in models of Huntington disease.Transglutaminase 2 is secreted from smooth muscle cells by transamidation-dependent microparticle formation.Proteins with Intrinsically Disordered Domains Are Preferentially Recruited to Polyglutamine Aggregates.Tissue transglutaminase crosslinks ataxin-1: possible role in SCA1 pathogenesis.γ-Glutamylamines and neurodegenerative diseases Transglutaminase induces protofibril-like amyloid beta-protein assemblies that are protease-resistant and inhibit long-term potentiation Transglutaminase activity is present in highly purified nonsynaptosomal mouse brain and liver mitochondria.Tissue-type transglutaminase and the effects of cystamine on intracerebral hemorrhage-induced brain edema and neurological deficits.Transglutaminase activation in neurodegenerative diseases.Transglutaminases and neurodegeneration.Screening of therapeutic strategies for Huntington's disease in YAC128 transgenic mice.Evidences for a role of protein cross-links in transglutaminase-related disease.Transglutaminase 2 and neuroinflammation.Receptor-stimulated transamidation induces activation of Rac1 and Cdc42 and the regulation of dendritic spines.Transglutaminase-catalyzed transamidation: a novel mechanism for Rac1 activation by 5-hydroxytryptamine2A receptor stimulation Déjà vu with a twist: transglutaminases in bioenergetics and transcriptional dysfunction in Huntington's disease.Treatment of YAC128 mice and their wild-type littermates with cystamine does not lead to its accumulation in plasma or brain: implications for the treatment of Huntington disease.Cystamine treatment is neuroprotective in the YAC128 mouse model of Huntington disease.Towards an Understanding of Energy Impairment in Huntington's Disease Brain.

P2860

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P2860

Mutant huntingtin protein: a substrate for transglutaminase 1, 2, and 3.

http://www.wikidata.org/entity/Q40457537

description

2005 nî lūn-bûn

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2005年の論文

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2005年論文

@yue

2005年論文

@zh-hant

2005年論文

@zh-hk

2005年論文

@zh-mo

2005年論文

@zh-tw

2005年论文

@wuu

2005年论文

@zh

2005年论文

@zh-cn

name

Mutant huntingtin protein: a substrate for transglutaminase 1, 2, and 3.

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type

label

Mutant huntingtin protein: a substrate for transglutaminase 1, 2, and 3.

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prefLabel

Mutant huntingtin protein: a substrate for transglutaminase 1, 2, and 3.

@en

P1433

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P1433

Journal of Neuropathology & Experimental Neurology

P1476

Mutant huntingtin protein: a substrate for transglutaminase 1, 2, and 3.

@en

P2093

Gina M Zainelli

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

Nichole L Dudek

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

Soo-Youl Kim

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

P2860

Intron-exon swapping of transglutaminase mRNA and neuronal Tau aggregation in Alzheimer's disease

Differential expression of multiple transglutaminases in human brain. Increased expression and cross-linking by transglutaminases 1 and 2 in Alzheimer's disease

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

Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain

Formic acid dissolves aggregates of an N-terminal huntingtin fragment containing an expanded polyglutamine tract: applying to quantification of protein components of the aggregates.

Pathogenesis of inclusion bodies in (CAG)n/Qn-expansion diseases with special reference to the role of tissue transglutaminase and to selective vulnerability.

Transglutaminases in disease.

Tissue transglutaminase-induced aggregation of alpha-synuclein: Implications for Lewy body formation in Parkinson's disease and dementia with Lewy bodies.

Brain transglutaminase: in vitro crosslinking of human neurofilament proteins into insoluble polymers

Transglutaminase aggregates huntingtin into nonamyloidogenic polymers, and its enzymatic activity increases in Huntington's disease brain nuclei.

P304

58-65

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scholarly article

P356

10.1093/JNEN/64.1.58

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1

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64

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Christopher A Ross

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2005-01-01T00:00:00Z

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P5875

8018249

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P698

15715085

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