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These results support our hypothesis that KIF5A is responsible for collagen transportation and secretion from HPMCs.
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This study identified three pathogenic KIF5A mutations in Korean Charcot-Marie-Tooth neuropathy type 2 patients by whole exome sequencing. Two mutations (p.Arg204Trp and p.Arg280His) were previously reported, but p.Leu558Pro was determined to be a novel de novo mutation.
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We conclude that reduced expression of axonal motor KIF5A may have important implications in determining axonal transport deficits and ongoing neurodegeneration in multiple sclerosis
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Kinesin family member 5A protein (Kif5A) with hereditary spastic paraplegia (HSP)-causing mutations showed a variety of significantly reduced catalytic and mechanical activities as a result of each mutation, with the shared phenotype from each that motility was significantly reduced.
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Variants in SPAST and KIF5A were the most common causes of autosomal dominant hereditary spastic paraplegia in Greece. The first nonsense mutation in KIF5A was identified in HSP patient.
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De novo stop-loss frameshift variants in KIF5A result in a novel phenotype that includes severe infantile onset myoclonus, hypotonia, optic nerve abnormalities, dysphagia, apnea, and early developmental arrest.
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KIF5A p.Ser974fs de novo mutation associated with myoclonic seizures and neonatal onset progressive leukoencephalopathy.
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Zinc ion-mediated inhibition of KIF5A activity might be one molecular cause contributing to impaired transport processes within brain and other organs in cases of zinc dyshomeostasis.
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This report describes the first known Asian family with a KIF5A mutation and broadens the clinical and electrophysiological spectrum associated with KIF5A-SPG10 mutations.
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study describes 2 Spanish families with an adult onset complicated autosomal dominant hereditary spastic paraplegia with a mild sensory neuropathy; identified 2 novel mutations c.773 C>T and c.833 C>T in the KIF5A gene resulting in the P258L and P278L substitutions; both were located in the highly conserved kinesin motor domain of the protein
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Kinesin-14 blocks microtubule nucleation in yeast and reveal that this inhibition is countered by the kinesin-5 protein, Cut7.[Cut7, Pkl1]
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the novel mutation p.Leu259Gln in two siblings affected by Hereditary spastic paraplegia (HSP) complicated by deafness and in their father with a pure form of HSP.
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Combining next-generation sequencing and conventional sequencing, study confirms that KIF5A mutations can cause variable phenotypes ranging from hereditary spastic paraplegia to Charcot-Marie-Tooth disease type 2
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Conformations of microtubule-bound human kinesin-5 motor domain were visualised at successive steps in its ATPase cycle.
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A review of the mechanism of pathogenesis involved in spastic paraplegia type 10 when KIF5A is inactivated by mutations.
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Data suggest that the impairment of the microtubule-kinesin function by alpha-synuclein oligomers drives early neurite pathology.
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This study extends the phenotype of SPG10 and argues for abnormalities in the axonal vesicular transport.
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These results provide an insight into the molecular mechanisms of KIF5A, which regulate inhibitory neural transmission and KIF5A deletion causes epilepsy.
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The results obtained indicate a KIF5A mutation frequency of 8.8% in the Italian HSP population and identify a region of the kinesin protein, the stalk domain, as a novel target for mutation.
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Molecular genetic analysis identified a new missense mutation of KIF5A gene causing hereditary spastic paraplegia
