Interaction of torsinA with its major binding partners is impaired by the dystonia-associated DeltaGAG deletion. - Test2 - elhamkhani - TriplyDB

Interaction of torsinA with its major binding partners is impaired by the dystonia-associated DeltaGAG deletion.

Interaction of torsinA with its major binding partners is impaired by the dystonia-associated DeltaGAG deletion.

http://www.wikidata.org/entity/Q37459854

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Relative tissue expression of homologous torsinB correlates with the neuronal specific importance of DYT1 dystonia-associated torsinA Arresting a Torsin ATPase reshapes the endoplasmic reticulum Regulation of Torsin ATPases by LAP1 and LULL1 Lamina-associated polypeptide 1: protein interactions and tissue-selective functions Torsins: not your typical AAA+ ATPases The nuclear envelope at a glance A molecular mechanism underlying the neural-specific defect in torsinA mutant mice TorsinA hypofunction causes abnormal twisting movements and sensorimotor circuit neurodegeneration The BiP molecular chaperone plays multiple roles during the biogenesis of torsinA, an AAA+ ATPase associated with the neurological disease early-onset torsion dystonia.Torsin ATPases: Harnessing Dynamic Instability for Function.The nuclear envelope localization of DYT1 dystonia torsinA-ΔE requires the SUN1 LINC complex component.Current Gaps in the Understanding of the Subcellular Distribution of Exogenous and Endogenous Protein TorsinA.A unique redox-sensing sensor II motif in TorsinA plays a critical role in nucleotide and partner binding.The zebrafish homologue of the human DYT1 dystonia gene is widely expressed in CNS neurons but non-essential for early motor system development The mechanism of Torsin ATPase activation.Untethering the nuclear envelope and cytoskeleton: biologically distinct dystonias arising from a common cellular dysfunction Genetic and clinical features of primary torsion dystonia.The nuclear envelope protein, LAP1B, is a novel protein phosphatase 1 substrate.Intracellular complexes of the early-onset torsion dystonia-associated AAA+ ATPase TorsinA.Stable isotope labeling with amino acids in cell culture based mass spectrometry approach to detect transient protein interactions using substrate trapping.How lamina-associated polypeptide 1 (LAP1) activates Torsin.Static retention of the lumenal monotopic membrane protein torsinA in the endoplasmic reticulum.Inherited isolated dystonia: clinical genetics and gene function.The pathogenic human Torsin A in Drosophila activates the unfolded protein response and increases susceptibility to oxidative stress.An anticholinergic reverses motor control and corticostriatal LTD deficits in Dyt1 ΔGAG knock-in mice.Access of torsinA to the inner nuclear membrane is activity dependent and regulated in the endoplasmic reticulum.TorsinA participates in endoplasmic reticulum-associated degradation Structures of TorsinA and its disease-mutant complexed with an activator reveal the molecular basis for primary dystonia.Neuronal Nuclear Membrane Budding Occurs during a Developmental Window Modulated by Torsin Paralogs.Molecular pathways in dystonia.Milestones in dystonia.Early-onset torsion dystonia: a novel high-throughput yeast genetic screen for factors modifying protein levels of torsinAΔE.Torsin ATPases: structural insights and functional perspectives.TorsinA controls TAN line assembly and the retrograde flow of dorsal perinuclear actin cables during rearward nuclear movement.Nuclear envelope breakdown induced by herpes simplex virus type 1 involves the activity of viral fusion proteins.Diseases of the Nucleoskeleton.Membrane defects and genetic redundancy: Are we at a turning point for DYT1 dystonia?Update on the Genetics of Dystonia.Lamina Associated Polypeptide 1 (LAP1) Interactome and Its Functional Features.LINCing defective nuclear-cytoskeletal coupling and DYT1 dystonia.

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P2860

Interaction of torsinA with its major binding partners is impaired by the dystonia-associated DeltaGAG deletion.

http://www.wikidata.org/entity/Q37459854

description

article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

@tr

scientific article published on 03 August 2009

@en

vedecký článok

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vetenskaplig artikel

@sv

videnskabelig artikel

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vědecký článek

@cs

name

Interaction of torsinA with it ...... -associated DeltaGAG deletion.

@en

Interaction of torsinA with it ...... -associated DeltaGAG deletion.

@nl

type

label

Interaction of torsinA with it ...... -associated DeltaGAG deletion.

@en

Interaction of torsinA with it ...... -associated DeltaGAG deletion.

@nl

prefLabel

Interaction of torsinA with it ...... -associated DeltaGAG deletion.

@en

Interaction of torsinA with it ...... -associated DeltaGAG deletion.

@nl

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JBC.M109.020164

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Journal of Biological Chemistry

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Interaction of torsinA with it ...... -associated DeltaGAG deletion.

@en

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Phyllis I Hanson

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

Seema Dalal

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

Teresa V Naismith

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P2860

TorsinB--perinuclear location and association with torsinA

TorsinA in PC12 cells: localization in the endoplasmic reticulum and response to stress

The dystonia-associated protein torsinA modulates synaptic vesicle recycling

Biosynthesis of the dystonia-associated AAA+ ATPase torsinA at the endoplasmic reticulum

Effect of torsinA on membrane proteins reveals a loss of function and a dominant-negative phenotype of the dystonia-associated DeltaE-torsinA mutant

LULL1 retargets TorsinA to the nuclear envelope revealing an activity that is impaired by the DYT1 dystonia mutation

TorsinA binds the KASH domain of nesprins and participates in linkage between nuclear envelope and cytoskeleton

The inner nuclear membrane protein LAP1 forms a native complex with B-type lamins and partitions with spindle-associated mitotic vesicles.

The AAA+ protein torsinA interacts with a conserved domain present in LAP1 and a novel ER protein

Mutant torsinA, responsible for early-onset torsion dystonia, forms membrane inclusions in cultured neural cells

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27866-27874

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scholarly article

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10.1074/JBC.M109.020164

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41

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284

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2009-08-03T00:00:00Z

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19651773

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2788837

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