Mutant torsinA interferes with protein processing through the secretory pathway in DYT1 dystonia cells. - Wikidata - wikimedia - TriplyDB

Mutant torsinA interferes with protein processing through the secretory pathway in DYT1 dystonia cells.

Mutant torsinA interferes with protein processing through the secretory pathway in DYT1 dystonia cells.

http://www.wikidata.org/entity/Q34578567

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The early-onset torsion dystonia-associated protein, torsinA, displays molecular chaperone activity in vitro p58IPK is an inhibitor of the eIF2α kinase GCN2 and its localization and expression underpin protein synthesis and ER processing capacity LULL1 retargets TorsinA to the nuclear envelope revealing an activity that is impaired by the DYT1 dystonia mutation A pathway sensor for genome-wide screens of intracellular proteolytic cleavage TorsinA binds the KASH domain of nesprins and participates in linkage between nuclear envelope and cytoskeleton Activated Rac1 GTPase translocates protein phosphatase 5 to the cell membrane and stimulates phosphatase activity in vitro Dtorsin, the Drosophila ortholog of the early-onset dystonia TOR1A (DYT1), plays a novel role in dopamine metabolism Torsins: not your typical AAA+ ATPases Mutations in PNKD causing paroxysmal dyskinesia alters protein cleavage and stability Endoplasmic reticulum stress and unfolded protein response in renal pathophysiology: Janus faces A Highly Immunogenic and Protective Middle East Respiratory Syndrome Coronavirus Vaccine Based on a Recombinant Measles Virus Vaccine Platform.Earlier onset of motor deficits in mice with double mutations in Dyt1 and Sgce.Impaired striatal D2 receptor function leads to enhanced GABA transmission in a mouse model of DYT1 dystonia.TorsinA hypofunction causes abnormal twisting movements and sensorimotor circuit neurodegeneration In vivo imaging reveals impaired connectivity across cortical and subcortical networks in a mouse model of DYT1 dystonia.A highly sensitive assay for monitoring the secretory pathway and ER stress.Secreted Gaussia luciferase as a biomarker for monitoring tumor progression and treatment response of systemic metastases.Chemical enhancement of torsinA function in cell and animal models of torsion dystonia.The BiP molecular chaperone plays multiple roles during the biogenesis of torsinA, an AAA+ ATPase associated with the neurological disease early-onset torsion dystonia.Secreted luciferase for in vivo evaluation of systemic protein delivery in mice TorsinA and the torsinA-interacting protein printor have no impact on endoplasmic reticulum stress or protein trafficking in yeast.Motor deficits and decreased striatal dopamine receptor 2 binding activity in the striatum-specific Dyt1 conditional knockout mice Biochemical and cellular analysis of human variants of the DYT1 dystonia protein, TorsinA/TOR1A The early-onset torsion dystonia-associated protein, torsinA, is a homeostatic regulator of endoplasmic reticulum stress response.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 4-Phenylbutyrate attenuates the ER stress response and cyclic AMP accumulation in DYT1 dystonia cell models.Untethering the nuclear envelope and cytoskeleton: biologically distinct dystonias arising from a common cellular dysfunction Genetic and clinical features of primary torsion dystonia.Decreased dopamine receptor 1 activity and impaired motor-skill transfer in Dyt1 ΔGAG heterozygous knock-in mice.Pre-synaptic release deficits in a DYT1 dystonia mouse model.Commentary: Dopaminergic dysfunction in DYT1 dystonia.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.Forebrain deletion of the dystonia protein torsinA causes dystonic-like movements and loss of striatal cholinergic neurons.Improved motor performance in Dyt1 ΔGAG heterozygous knock-in mice by cerebellar Purkinje-cell specific Dyt1 conditional knocking-out A predictable worm: application of Caenorhabditis elegans for mechanistic investigation of movement disorders.Altered activation of protein kinase PKR and enhanced apoptosis in dystonia cells carrying a mutation in PKR activator protein PACT.Mouse models of neurodevelopmental disease of the basal ganglia and associated circuits.

P2860

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P2860

Mutant torsinA interferes with protein processing through the secretory pathway in DYT1 dystonia cells.

http://www.wikidata.org/entity/Q34578567

description

2007 nî lūn-bûn

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2007 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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2007 թվականի ապրիլին հրատարակված գիտական հոդված

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2007年の論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年论文

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name

Mutant torsinA interferes with ...... athway in DYT1 dystonia cells.

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Mutant torsinA interferes with ...... athway in DYT1 dystonia cells.

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Mutant torsinA interferes with ...... athway in DYT1 dystonia cells.

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Proceedings of the National Academy of Sciences of the United States of America

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Mutant torsinA interferes with ...... athway in DYT1 dystonia cells.

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P2093

Bakhos Tannous

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Brian P Niland

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Flavia C Nery

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Jeffrey W Hewett

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Juan Zeng

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Xandra O Breakefield

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

Yuqing Li

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

P2860

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

Dystonia-causing mutant torsinA inhibits cell adhesion and neurite extension through interference with cytoskeletal dynamics

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

Structural organization of the endoplasmic reticulum.

N-ethylmaleimide-sensitive fusion protein: a trimeric ATPase whose hydrolysis of ATP is required for membrane fusion

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

Crystal structure of the Aequorea victoria green fluorescent protein

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

AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes

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104

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