Prion diseases of humans and animals: their causes and molecular basis.

@article{Collinge2001PrionDO,
  title={Prion diseases of humans and animals: their causes and molecular basis.},
  author={John Collinge},
  journal={Annual review of neuroscience},
  year={2001},
  volume={24},
  pages={
          519-50
        }
}
  • J. Collinge
  • Published 2001
  • Medicine, Biology
  • Annual review of neuroscience
Prion diseases are transmissible neurodegenerative conditions that include Creutzfeldt-Jakob disease (CJD) in humans and bovine spongiform encephalopathy (BSE) and scrapie in animals. Prions appear to be composed principally or entirely of abnormal isoforms of a host-encoded glycoprotein, prion protein. Prion propagation involves recruitment of host cellular prion protein, composed primarily of alpha-helical structure, into a disease specific isoform rich in beta-sheet structure. The existence… Expand
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  • J. Collinge
  • Medicine, Biology
  • Journal of Neurology, Neurosurgery & Psychiatry
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Treatment of Prion Disease with Heterologous Prion Proteins
TLDR
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References

SHOWING 1-10 OF 182 REFERENCES
Human prion diseases and bovine spongiform encephalopathy (BSE).
  • J. Collinge
  • Biology, Medicine
  • Human molecular genetics
  • 1997
TLDR
Molecular analysis of prion strains suggests that new variant Creutzfeldt-Jakob disease is caused by BSE exposure, and the novel biology of prions propagation may not be unique to these rare degenerative brain diseases. Expand
Molecular biology of prion diseases
TLDR
Understanding prion diseases may advance investigations of other neurodegenerative disorders and of the processes by which neurons differentiate, function for decades, and then grow senescent. Expand
Unaltered susceptibility to BSE in transgenic mice expressing human prion protein
TLDR
It is shown that transgenic mice expressing human PrP in addition to mouse PrP can generatehuman PrPSc and 'human' prions, and provide a model to study experimentally the species barrier limiting BSE transmission to humans. Expand
Strain-specific prion-protein conformation determined by metal ions
TLDR
It is shown that two different human PrPSc types, seen in clinically distinct subtypes of classical Creutzfeldt–Jakob disease, can be interconverted in vitro by altering their metal-ion occupancy and represents a new mechanism for post-translational modification of PrP. Expand
Prion protein is necessary for normal synaptic function
TLDR
It is argued that loss of function of PrPc may contribute to the early synaptic loss3 and neuronal degeneration seen in Creutzfeldt–Jakob disease and scrapie and bovine spongiform encephalopathy in animals. Expand
Evidence for two prions in yeast: [URE3] and [PSI].
TLDR
A prion is an infectious protein, a concept that has its origins in studies of scrapie of sheep, kuru, and Creutzfeldt-Jakob disease of humans and similar spongiform encephalopathies of other mammals, and an impressive body of evidence supporting this idea has built up. Expand
Homozygous prion protein genotype predisposes to sporadic Creutzfeldt–Jakob disease
TLDR
It is argued that homozygosity predisposes towards sporadic CJD and that this directly supports the hypothesis that interaction between prion protein molecules underlies the disease process. Expand
Linkage of a prion protein missense variant to Gerstmann–Sträussler syndrome
TLDR
It is shown here that PrP codon 102 is linked to the putative gene for the syndrome in two pedigrees, providing the best evidence to date that this familial condition is inherited despite also being infectious, and that substitution of leucine for proline at PrPcodon 102 may lead to the development of Gerstmann–Sträussler syndrome. Expand
Evidence for the Conformation of the Pathologic Isoform of the Prion Protein Enciphering and Propagating Prion Diversity
TLDR
The results presented indicate that the conformation of PrP sc functions as a template in directing the formation of nascent PrPSc and suggest a mechanism to explain strains of prions where diversity is encrypted in the conformed PrP Sc. Expand
Non-genetic propagation of strain-specific properties of scrapie prion protein
TLDR
Self-propagation of PrPSc polymers with distinct three-dimensional structures could be the molecular basis of scrapie strains, providing evidence that the protein-only model of infectious agents causing scrapie and other transmissible spon-giform encephalopathies is feasible. Expand
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