Dimerization of the DYT6 dystonia protein, THAP1, requires residues within the coiled-coil domain. - sprookjes - yvandenbroek - TriplyDB

Dimerization of the DYT6 dystonia protein, THAP1, requires residues within the coiled-coil domain.

Dimerization of the DYT6 dystonia protein, THAP1, requires residues within the coiled-coil domain.

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NMR studies of a new family of DNA binding proteins: the THAP proteins Genotype-phenotype correlations in THAP1 dystonia: molecular foundations and description of new cases.Dystonia type 6 gene product Thap1: identification of a 50 kDa DNA-binding species in neuronal nuclear fractions Inherited isolated dystonia: clinical genetics and gene function.Neural expression of the transcription factor THAP1 during development in rat.Abnormalities of motor function, transcription and cerebellar structure in mouse models of THAP1 dystonia.The genetics of dystonias.Combined occurrence of a novel TOR1A and a THAP1 mutation in primary dystonia.A rare sequence variant in intron 1 of THAP1 is associated with primary dystonia.THAP1: Role in Mouse Embryonic Stem Cell Survival and Differentiation.In-depth Characterization of the Homodimerization Domain of the Transcription Factor THAP1 and Dystonia-Causing Mutations Therein.The DYT6 Dystonia Protein THAP1 Regulates Myelination within the Oligodendrocyte Lineage.

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P2860

Dimerization of the DYT6 dystonia protein, THAP1, requires residues within the coiled-coil domain.

http://www.wikidata.org/entity/Q38294642

description

2011 nî lūn-bûn

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2011年の論文

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2011年論文

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2011年論文

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name

Dimerization of the DYT6 dysto ...... within the coiled-coil domain.

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type

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Dimerization of the DYT6 dysto ...... within the coiled-coil domain.

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prefLabel

Dimerization of the DYT6 dysto ...... within the coiled-coil domain.

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J.1471-4159.2011.07386.X

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Journal of Neurochemistry

P1476

Dimerization of the DYT6 dysto ...... within the coiled-coil domain.

@en

P2093

Cem Sengel

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D Cristopher Bragg

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Laurie J Ozelius

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Nutan Sharma

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Sophie Gavarini

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P2860

Towards a proteome-scale map of the human protein–protein interaction network

THAP proteins target specific DNA sites through bipartite recognition of adjacent major and minor grooves

Interactions between heterologous helix-loop-helix proteins generate complexes that bind specifically to a common DNA sequence

The THAP domain of THAP1 is a large C2CH module with zinc-dependent sequence-specific DNA-binding activity

Structure-function analysis of the THAP zinc finger of THAP1, a large C2CH DNA-binding module linked to Rb/E2F pathways

The THAP-zinc finger protein THAP1 regulates endothelial cell proliferation through modulation of pRB/E2F cell-cycle target genes

Mutations in the THAP1 gene are responsible for DYT6 primary torsion dystonia

Ronin is essential for embryogenesis and the pluripotency of mouse embryonic stem cells

Classification of human B-ZIP proteins based on dimerization properties

NLSdb: database of nuclear localization signals

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1087-1100

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10.1111/J.1471-4159.2011.07386.X

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