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Human prion diseases with variant prion protein
Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences, 1994Abstract Recent molecular genetic studies revealed that the human prion protein (PrP) gene has a large repertoire of polymorphisms and mutations. Each variant PrP seems to correspond to a distinct type of prion diseases. W e report herein that it is useful to classify prion diseases into plaque type or non-plaque type, based on the ...
T, Kitamoto, J, Tateishi
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Prion Protein Functions and Dysfunction in Prion Diseases
Current Medicinal Chemistry, 2009Prion diseases are zoonotic infectious diseases caused by infectious particles, termed prions. Main component of prions is presumably a misfolded, partially protease-resistant conformer (PrP(Sc)) of a normal cell surface protein, the cellular prion protein (PrP(C)), whose anti-oxidative role is presumed by studies using prion protein (PrP)-knockout ...
Akikazu, Sakudo, Kazuyoshi, Ikuta
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Current Alzheimer Research, 2008
The PrP propensity to adopt different structures is tightly linked to transmissible spongiform encephalopathies (TSE) which include Creutzfeldt-Jakob disease (CJD), Gerstmann-Sträussler-Scjeinker (GSS) and Kuru syndrome. In most cases, TSE is associated with the accumulation in the brain of an abnormally folded protease-resistant protein, PrP Sc or ...
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The PrP propensity to adopt different structures is tightly linked to transmissible spongiform encephalopathies (TSE) which include Creutzfeldt-Jakob disease (CJD), Gerstmann-Sträussler-Scjeinker (GSS) and Kuru syndrome. In most cases, TSE is associated with the accumulation in the brain of an abnormally folded protease-resistant protein, PrP Sc or ...
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Immunology of Prion Protein and Prions
2017Many natural prion diseases are acquired peripherally, such as following the oral consumption of contaminated food or pasture. After peripheral exposure many prion isolates initially accumulate to high levels within the host's secondary lymphoid tissues. The replication of prions within these tissues is essential for their efficient spread to the brain
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FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 1991
Neurodegenerative diseases of animals and humans including scrapie, bovine spongiform encephalopathy, and Creutzfeldt-Jakob disease are caused by unusual infectious pathogens called prions. There is no evidence for a nucleic acid in the prion, but diverse experimental results indicate that a host-derived protein called PrPSc is a component of the ...
N, Stahl, S B, Prusiner
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Neurodegenerative diseases of animals and humans including scrapie, bovine spongiform encephalopathy, and Creutzfeldt-Jakob disease are caused by unusual infectious pathogens called prions. There is no evidence for a nucleic acid in the prion, but diverse experimental results indicate that a host-derived protein called PrPSc is a component of the ...
N, Stahl, S B, Prusiner
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Current Opinion in Structural Biology, 2000
The past two years have seen the extension of our knowledge on the cellular prion protein structure with new NMR data on both the hamster and human proteins. In addition, the folding dynamics of two cellular prion proteins have been elucidated. There are now several examples of recombinant prion proteins that are able to adopt different conformations ...
Jackson, GS, Clarke, AR
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The past two years have seen the extension of our knowledge on the cellular prion protein structure with new NMR data on both the hamster and human proteins. In addition, the folding dynamics of two cellular prion proteins have been elucidated. There are now several examples of recombinant prion proteins that are able to adopt different conformations ...
Jackson, GS, Clarke, AR
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Physiology of the Prion Protein
Physiological Reviews, 2008Prion diseases are transmissible spongiform encephalopathies (TSEs), attributed to conformational conversion of the cellular prion protein (PrPC) into an abnormal conformer that accumulates in the brain. Understanding the pathogenesis of TSEs requires the identification of functional properties of PrPC.
Rafael, Linden +5 more
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Cellular and Molecular Life Sciences, 2007
From Creutzfeldt-Jakob disease (CJD) to variant CJD through Gerstmann-Sträussler-Scheinker syndrome, kuru and fatal familial insomnia, the journey leading to current understanding of the basic aspects of human prion diseases has been full of unexpected, but often dramatic and always fascinating twists.
W Q, Zou, P, Gambetti
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From Creutzfeldt-Jakob disease (CJD) to variant CJD through Gerstmann-Sträussler-Scheinker syndrome, kuru and fatal familial insomnia, the journey leading to current understanding of the basic aspects of human prion diseases has been full of unexpected, but often dramatic and always fascinating twists.
W Q, Zou, P, Gambetti
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Prion Protein Disease and Neuropathology of Prion Disease
Neuroimaging Clinics of North America, 2008Human prion diseases, in common with other neurodegenerative diseases, may be sporadic or inherited and are characterized by the accumulation of cellular proteins accompanied by neuronal death and synaptic loss. Prion diseases are, however, unique in being transmissible.
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Infective Proteins: The Prion Puzzle
Current Protein & Peptide Science, 2001According to the Koch postulates an infectious organism is the one that can be isolated from an host suffering from a disorder, can be propagated in laboratory, can cause the same disease when introduced in another host, and finally, can be re-isolated from the host itself.
F. Ceciliani, P. Pergami
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