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Human prion diseases with variant prion protein
Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences, 1994Recent 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 distribution of PrP in the ...
Jun Tateishi, Tetsuyuki Kitamoto
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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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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 ...
Graham S. Jackson+2 more
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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 ...
Graham S. Jackson+2 more
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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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Journal of the Neurological Sciences, 2019
Sporadic Creutzfeldt-Jakob disease (sCJD) cases are classified according to the methionine/valine polymorphism at codon 129 of PRNP gene and the proteinase K (PK) digested abnormal prionprotein (PrPres) identified on western blotting (type 1 or type 2).
Alvina, H.+5 more
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Sporadic Creutzfeldt-Jakob disease (sCJD) cases are classified according to the methionine/valine polymorphism at codon 129 of PRNP gene and the proteinase K (PK) digested abnormal prionprotein (PrPres) identified on western blotting (type 1 or type 2).
Alvina, H.+5 more
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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 ...
Kazuyoshi Ikuta, Akikazu Sakudo
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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.
Pierluigi Gambetti, Wen-Quan Zou
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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.
Pierluigi Gambetti, Wen-Quan Zou
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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.
Martín Cammarota+5 more
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Prion Proteins Leading to Neurodegeneration
Current Alzheimer Research, 2008Prion diseases are fatal neurodegenerative disorders related to the conformational alteration of the prion protein (PrP C) into a pathogenic and protease-resistant isoform PrP(Sc). PrP(C) is a cell surface glycoprotein expressed mainly in the central nervous system and despite numerous efforts to elucidate its physiological role, the exact biological ...
D, La Mendola+5 more
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[URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae.
Science, 1994A cytoplasmically inherited element, [URE3], allows yeast to use ureidosuccinate in the presence of ammonium ion. Chromosomal mutations in the URE2 gene produce the same phenotype.
R. B. Wickner
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