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Prion Protein-Related Diseases Of Man And Animals
1998Abstract Scrapie, Creutzfeldt-Jakob disease (CJD), Gerstmann- Straussler-Sheinker (GSS) syndrome and related diseases of mink (transmissible mink encephalopathy), mule deer, and elk (chronic wasting disease) are the founder members of a group of diseases called the transmissible degenerative (or spongiform) encephalopathies (TSE); the
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Analysis of 2000 consecutive UK tonsillectomy specimens for disease-related prion protein
The Lancet, 2004Variant Creutzfeldt-Jakob disease (CJD) is thought to be caused by dietary or other exposure to bovine spongiform encephalopathy (BSE) prions. The prevalence of preclinical or subclinical prion infection in the UK is currently unknown. Since clinical variant CJD is uniformly associated with tonsillar prion infection, we screened 2000 anonymous surgical
Adam, Frosh +6 more
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The Prion Diseases: Creutzfeldt-Jakob, Gerstmann-Sträussler-Scheinker, and Related Disorders
Journal of Geriatric Psychiatry and Neurology, 1998The prion diseases are an interesting group of neurodegenerative disorders for a variety of reasons. The most obvious is their property of transmissibility, but beyond that they constitute a fascinating example of the diversity of disease expression possible from a common etiologic factor.
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Chapter 11. Mouse Models of Prion Protein Related Diseases
2011Prion protein (PrP) related diseases are a heterogeneous group of fatal neurodegenerative conditions featuring aberrancies in the metabolism of the cellular prion protein (PrPC) that lead to the formation of neurotoxic or propagative conformers. Commonly referred to as transmissible spongiform encephalopaties or prion disorders, these diseases can be ...
María Gasset, Adriano Aguzzi
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Mini-Reviews in Medicinal Chemistry, 2008
Nucleic acids catalyse the conversion of alpha-helical prion protein to the beta-structured protein oligomers and amyloids structurally similar to the infectious isoform of protein. Simultaneously, the prion protein, similar to gene regulating proteins, bends, unwinds and condenses nucleic acid.
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Nucleic acids catalyse the conversion of alpha-helical prion protein to the beta-structured protein oligomers and amyloids structurally similar to the infectious isoform of protein. Simultaneously, the prion protein, similar to gene regulating proteins, bends, unwinds and condenses nucleic acid.
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1994
"Prionlar, nükleik asitleri modifiye eden işlemlerle inaktive edilemeyen,temel ve gerekli komponent olan hücresel bir proteinin anormal bir izoformundanoluşan küçük, proteinden zengin, infeksiyöz partiküller" olaraktanımlanabilirler (42).Genetik bilginin nükleik asitlerden proteinlere dönüşümü , molekülerbiyolojinin temel doktrini olarak ...
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"Prionlar, nükleik asitleri modifiye eden işlemlerle inaktive edilemeyen,temel ve gerekli komponent olan hücresel bir proteinin anormal bir izoformundanoluşan küçük, proteinden zengin, infeksiyöz partiküller" olaraktanımlanabilirler (42).Genetik bilginin nükleik asitlerden proteinlere dönüşümü , molekülerbiyolojinin temel doktrini olarak ...
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2000
In humans, familial forms of transmissible spongiform encephalopathies (TSE; "prion diseases") have been shown to segregate with the exchange of individual amino acids in the prion protein (PrP) sequence. We used the NMR structure of the globular domain of mouse PrP in the cellular form (PrP(C)) as a starting point for investigations by long-time ...
M, Billeter, K, Wüthrich
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In humans, familial forms of transmissible spongiform encephalopathies (TSE; "prion diseases") have been shown to segregate with the exchange of individual amino acids in the prion protein (PrP) sequence. We used the NMR structure of the globular domain of mouse PrP in the cellular form (PrP(C)) as a starting point for investigations by long-time ...
M, Billeter, K, Wüthrich
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Localization of disease-related PrP in Danish patients with different subtypes of prion disease.
Clinical neuropathology, 2009The transmissible spongiform encephalopathies are characterized by vacuolization, neuronal loss, gliosis and deposition of a misfolded and Proteinase K resistant isoform of the prion protein (PrP(Sc)) in the central nervous system. METHODS MATERIALS AND PATIENTS: Paraffin-embedded tissue blot (PET-blot), immunohistochemistry (IHC) and Western blotting (
Bergstrom, A.L. +4 more
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New Structural Approaches to Understand the Disease Related Forms of the Prion Protein
2005Abstract : Expression constructs have been prepared in order to generate the 89-143 fragment of the prion protein with isotopic labels using either in vitro translation or expression in E.coli cells. Initial testing of expression has been done.
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