Déjà vu with a twist: transglutaminases in bioenergetics and transcriptional dysfunction in Huntington's disease.

Item

http://www.wikidata.org/entity/Q42204907

description

2010 nî lūn-bûn

@nan

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

2010年论文

@zh

2010年论文

@zh-cn

name

Déjà vu with a twist: transglu ...... ction in Huntington's disease.

@en

Déjà vu with a twist: transglu ...... ction in Huntington's disease.

@nl

type

Item

label

Déjà vu with a twist: transglu ...... ction in Huntington's disease.

@en

Déjà vu with a twist: transglu ...... ction in Huntington's disease.

@nl

prefLabel

Déjà vu with a twist: transglu ...... ction in Huntington's disease.

@en

Déjà vu with a twist: transglu ...... ction in Huntington's disease.

@nl

P1476

Déjà vu with a twist: transglu ...... ction in Huntington's disease.

@en

P2093

Albert R La Spada

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

Parsa Kazemi-Esfarjani

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

P2860

The glutamine residues reactive in transglutaminase-catalyzed cross-linking of involucrin

Inhibition of transglutaminase 2 mitigates transcriptional dysregulation in models of Huntington disease.

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

Transglutaminase-catalyzed inactivation of glyceraldehyde 3-phosphate dehydrogenase and alpha-ketoglutarate dehydrogenase complex by polyglutamine domains of pathological length

Peptides containing glutamine repeats as substrates for transglutaminase-catalyzed cross-linking: relevance to diseases of the nervous system.

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

Lysine-rich histone (H1) is a lysyl substrate of tissue transglutaminase: possible involvement of transglutaminase in the formation of nuclear aggregates in (CAG)(n)/Q(n) expansion diseases.

N(epsilon)-(gamma-L-glutamyl)-L-lysine (GGEL) is increased in cerebrospinal fluid of patients with Huntington's disease.

Prolonged survival and decreased abnormal movements in transgenic model of Huntington disease, with administration of the transglutaminase inhibitor cystamine.

Transcriptional repression of PGC-1alpha by mutant huntingtin leads to mitochondrial dysfunction and neurodegeneration.

P304

335-337

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

P31

scholarly article

P356

10.1002/EMMM.201000092

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

P433

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

P478

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

P577

2010-09-01T00:00:00Z

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

P5875

45801271

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

P698

20730854

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

P921

Huntington disease

P932

3377338

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