2002
DOI: 10.1136/jnnp.72.6.788
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Rapidly progressive dementia syndrome associated with a novel four extra repeat mutation in the prion protein gene

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Cited by 17 publications
(12 citation statements)
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“…The duration of illness in our patient is also compatible with the findings of Van Harten et al, who described a disease duration of 7 years. 20 9 1 MM 32 72+…”
Section: Discussionmentioning
confidence: 99%
See 1 more Smart Citation
“…The duration of illness in our patient is also compatible with the findings of Van Harten et al, who described a disease duration of 7 years. 20 9 1 MM 32 72+…”
Section: Discussionmentioning
confidence: 99%
“…8 The insertions identified so far comprised one, two, and four to nine extra octapeptide repeats. 9 Expansion of an octapeptide repeat or 24-nucleotide repeat region is rare, but expansion of trinucleotide repeats are found in other neurodegenerative disorders, including Huntington's disease and the spinal cerebellar ataxias. [10][11][12] The expansion of the polyglutamine tract in these disorders is associated with accumulation and higher toxicity of the protein.…”
mentioning
confidence: 99%
“…It would, in addition, appear that a concept of evolving molecular processing of the prion protein would implicate structural changes related to extraoctapeptide repeat insertions within the PrP gene. Such a mechanism would help explain a basic phenomenon of binding of prion protein across a potentially highly variable spectrum of protein molecular species (Yanagihara et al, 2002).…”
Section: Prion Particle Template Replication As An Inherited Neuronalmentioning
confidence: 99%
“…It has been proposed that neuronal death can be triggered by accumulation of PrP in the cytosol due to impairment of proteasomal degradation of misfolded PrP molecules retrotranslocated from the endoplasmic reticulum [9]. In previous work, transgenic (Tg) mouse models expressing PrP C with four or nine octapeptide insertional mutations showed a prion-like disease characterized by gliosis, and apoptotic loss of cerebellar granule cells [10,11] analogous to the disease observed in patients with a four extra repeat mutation in the PrP C gene [6]. Furthermore, it has been shown that PrP C with insertional mutations acquires special properties that may be reminiscent from PrP Sc : ligand-binding, oxidative attack susceptibility, detergent insolubility, increased protease resistance, and aggregation capacity [5,[12][13][14][15].…”
Section: Introductionmentioning
confidence: 99%
“…Prion diseases such as scrapie in sheep, bovine spongiform encephalopathy (BSE) in cattle, and Creutzfeldt-Jakob disease in man, may be of an infectious origin. Inherited prion diseases has been only described in humans and have been associated with both point mutations and an increased number of octarepeats in the PrP C open reading frame (ORF) [5][6][7][8]. The cellular mechanism by which mutations in the prion protein gene causes neurological dysfunction is unknown.…”
Section: Introductionmentioning
confidence: 99%