Mutations Phe785Leu and Thr618Met in Na+,K+-ATPase, associated with familial rapid-onset dystonia parkinsonism, interfere with Na+ interaction by distinct mechanisms.
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Mutation I810N in the alpha3 isoform of Na+,K+-ATPase causes impairments in the sodium pump and hyperexcitability in the CNS.Cellular function and pathological role of ATP13A2 and related P-type transport ATPases in Parkinson's disease and other neurological disordersAlternating hemiplegia of childhood-related neural and behavioural phenotypes in Na+,K+-ATPase α3 missense mutant mice.Alternating Hemiplegia of Childhood: Retrospective Genetic Study and Genotype-Phenotype Correlations in 187 Subjects from the US AHCF RegistryThe rapid-onset dystonia parkinsonism mutation D923N of the Na+, K+-ATPase alpha3 isoform disrupts Na+ interaction at the third Na+ site.Relationship between Ca2+-affinity and shielding of bulk water in the Ca2+-pump from molecular dynamics simulations.Distinct neurological disorders with ATP1A3 mutationsMolecular cloning and characterization of porcine Na⁺/K⁺-ATPase isoforms α1, α2, α3 and the ATP1A3 promoter.α-synuclein assemblies sequester neuronal α3-Na+/K+-ATPase and impair Na+ gradientCapsazepine, a synthetic vanilloid that converts the Na,K-ATPase to Na-ATPase.Expression of mutant α1 Na/K-ATPase defective in conformational transition attenuates Src-mediated signal transduction.New roles for an old enzyme: Na,K-ATPase emerges as an interesting drug target.The genetics of dystonias.The structure of the Na+,K+-ATPase and mapping of isoform differences and disease-related mutations.A novel de novo mutation in ATP1A3 and childhood-onset schizophrenia.The C terminus of Na+,K+-ATPase controls Na+ affinity on both sides of the membrane through Arg935.Milestones in dystonia.The genetics of dystonia: new twists in an old tale.Sodium pump regulation of locomotor control circuits.Glial Na(+) -dependent ion transporters in pathophysiological conditions.Pathogenic mechanisms of prion protein, amyloid-β and α-synuclein misfolding: the prion concept and neurotoxicity of protein oligomers.Inhibition of phosphorylation of na+,k+-ATPase by mutations causing familial hemiplegic migraine.K+ congeners that do not compromise Na+ activation of the Na+,K+-ATPase: hydration of the ion binding cavity likely controls ion selectivity.Relationship between intracellular Na+ concentration and reduced Na+ affinity in Na+,K+-ATPase mutants causing neurological disease.A structural view on the functional importance of the sugar moiety and steroid hydroxyls of cardiotonic steroids in binding to Na,K-ATPase.Enhanced inhibitory neurotransmission in the cerebellar cortex of Atp1a3-deficient heterozygous mice.A C-terminal mutation of ATP1A3 underscores the crucial role of sodium affinity in the pathophysiology of rapid-onset dystonia-parkinsonism.Identification and function of a cytoplasmic K+ site of the Na+, K+ -ATPase.De novo ATP1A3 and compound heterozygous NLRP3 mutations in a child with autism spectrum disorder, episodic fatigue and somnolence, and muckle-wells syndrome.
P2860
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P2860
Mutations Phe785Leu and Thr618Met in Na+,K+-ATPase, associated with familial rapid-onset dystonia parkinsonism, interfere with Na+ interaction by distinct mechanisms.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年学术文章
@wuu
2006年学术文章
@zh-cn
2006年学术文章
@zh-hans
2006年学术文章
@zh-my
2006年学术文章
@zh-sg
2006年學術文章
@yue
2006年學術文章
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2006年學術文章
@zh-hant
name
Mutations Phe785Leu and Thr618 ...... action by distinct mechanisms.
@en
Mutations Phe785Leu and Thr618 ...... action by distinct mechanisms.
@nl
type
label
Mutations Phe785Leu and Thr618 ...... action by distinct mechanisms.
@en
Mutations Phe785Leu and Thr618 ...... action by distinct mechanisms.
@nl
prefLabel
Mutations Phe785Leu and Thr618 ...... action by distinct mechanisms.
@en
Mutations Phe785Leu and Thr618 ...... action by distinct mechanisms.
@nl
P2860
P356
P1476
Mutations Phe785Leu and Thr618 ...... raction by distinct mechanisms
@en
P2093
Vivien Rodacker
P2860
P304
18539-18548
P356
10.1074/JBC.M601780200
P407
P577
2006-04-21T00:00:00Z