Familial Neurological Disease Associated With Spongiform Encephalopathy

Rosenthal, N. Paul; Keesey, John; Crandall, Barbara F.; Brown, W. Jann

doi:10.1001/archneur.1976.00500040036005

Cited by 72 publications

(25 citation statements)

References 30 publications

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“…5). Features of amyotrophy with muscle fasiculations and fibrillations have been reported in an Italian kindred with GSS (PI02L) (Kretzschmar et al 1992), and the proband from a large English pedigree with GSS, in addition to neurogenic atrophy, showed muscle pathologic changes (Rosenthal et al 1976). Immunostaining studies have localized PrP at neuromus cular junctions in humans (Askanas et al 1993) but mice deficient for PrP^ have been shown to exhibit normal electrical transmission at the neuromuscular junction (Brenner et al 1992).…”

Section: The Pioil Mutation Causes Neurodegeneration and Neuromyopathymentioning

confidence: 95%

Interactions between wild-type and mutant prion proteins modulate neurodegeneration in transgenic mice.

Telling¹,

Haga²,

Torchia³

et al. 1996

Genes Dev.

242

197

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Section: The Pioil Mutation Causes Neurodegeneration and Neuromyopathymentioning

confidence: 95%

Interactions between wild-type and mutant prion proteins modulate neurodegeneration in transgenic mice.

Telling¹,

Haga²,

Torchia³

et al. 1996

Genes Dev.

242

197

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“…In a Finnish family with CJD (Haltia M: personal communication, 1978), one affected member had resided in Holland for about thirty years, having little contact with the other affected members of the family living in Helsinki. In another family [40] the father migrated from England to the United States at the age of 24 and died 28 years later of a chronic neurological disease that was not typical of CJD. A son died with transmissible CJD thirty-one years after the death of his father; several relatives living in England also died from CJD.…”

Section: Familial Clustering Of Cjdmentioning

confidence: 99%

Creutzfeldt‐Jakob disease: Patterns of worldwide occurrence and the significance of familial and sporadic clustering

Cl¹,

Jo²,

Dc³

et al. 1979

Annals of Neurology

583

276

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The worldwide epidemiology of Creutzfeldt-Jakob disease (CJD) is presented from an analysis of 1,435 patients. In the United States, the average annual mortality rate is at least 0.26 deaths per million. Temporal-spatial clustering of cases was not found in the United States, but reports from other countries indicate that such clustering does occur. Fifteen percent of the cases were of the familial type, suggesting a genetic susceptibility to infection. Iatrogenic transmission by corneal transplantation and neurosurgical operations has occurred, and the possibility is raised that previous surgery or preexisting neurological operations has occurred, and the possibility is raised that previous surgery or preexisting neurological disease may be associated with an increased risk of developing CJD. It remains to be determined whether the virus of CJD is maintained only by patient-to-patient transmission, has a zoonotic reservoir such as scrapie, or causes widespread latent infection of man that is occasionally activated.

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“…4B). Familial CJD cases suggested that genetic factors might influence pathogenesis (1,2,244), but this was difficult to reconcile with the transmissibility of fCJD and GSS (3). The discovery of genetic linkage between the PrP gene and scrapie incubation times in mice (213) raised the possibility that mutation might feature in the hereditary human prion diseases.…”

mentioning

confidence: 99%

Molecular characterization of proteolytic cleavage sites of the Pseudomonas syringae effector AvrRpt2

Chisholm

Dahlbeck

Krishnamurthy

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

137

138

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Prions are unprecedented infectious pathogens that cause a group of invariably fatal neurodegenerative diseases by an entirely novel mechanism. Prion diseases may present as genetic, infectious, or sporadic disorders, all of which involve modification of the prion protein (PrP). Bovine spongiform encephalopathy (BSE), scrapie of sheep, and Creutzfeldt-Jakob disease (CJD) of humans are among the most notable prion diseases. Prions are transmissible particles that are devoid of nucleic acid and seem to be composed exclusively of a modified protein (PrP Sc ). The normal, cellular PrP (PrP C ) is converted into PrP Sc through a posttranslational process during which it acquires a high ␤-sheet content. The species of a particular prion is encoded by the sequence of the chromosomal PrP gene of the mammals in which it last replicated. In contrast to pathogens carrying a nucleic acid genome, prions appear to encipher strain-specific properties in the tertiary structure of PrP Sc . Transgenetic studies argue that PrP Sc acts as a template upon which PrP C is refolded into a nascent PrP Sc molecule through a process facilitated by another protein. Miniprions generated in transgenic mice expressing PrP, in which nearly half of the residues were deleted, exhibit unique biological properties and should facilitate structural studies of PrP Sc . While knowledge about prions has profound implications for studies of the structural plasticity of proteins, investigations of prion diseases suggest that new strategies for the prevention and treatment of these disorders may also find application in the more common degenerative diseases.

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Familial Neurological Disease Associated With Spongiform Encephalopathy

Cited by 72 publications

References 30 publications

Interactions between wild-type and mutant prion proteins modulate neurodegeneration in transgenic mice.

Interactions between wild-type and mutant prion proteins modulate neurodegeneration in transgenic mice.

Creutzfeldt‐Jakob disease: Patterns of worldwide occurrence and the significance of familial and sporadic clustering

Molecular characterization of proteolytic cleavage sites of the Pseudomonas syringae effector AvrRpt2

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