Truncated Forms of the Human Prion Protein in Normal Brain and in Prion Diseases
نویسندگان
چکیده
منابع مشابه
Structural studies of truncated forms of the prion protein PrP.
Prions are proteins that adopt self-propagating aberrant folds. The self-propagating properties of prions are a direct consequence of their distinct structures, making the understanding of these structures and their biophysical interactions fundamental to understanding prions and their related diseases. The insolubility and inherent disorder of prions have made their structures difficult to stu...
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Prion diseases are a group of infectious fatal neurodegenerative diseases. The conformational conversion of a cellular prion protein (PrP(C)) into an abnormal misfolded isoform (PrP(Sc)) is the key event in prion diseases pathology. Under normal conditions, the high-energy barrier separates PrP(C) from PrP(Sc) isoform. However, pathogenic mutations, modifications as well as some cofactors, such...
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After the finding that anti-prion antibodies stain sensory and sympathetic ganglia in variant Creutzfeldt-Jakob disease (vCJD), it was suggested that this localization supported the oral route of entry. However, prion accumulation subsequently also appeared in the peripheral nervous system (PNS) in sporadic cases. This study aims at evaluating the extent of prion protein accumulation in the PNS...
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Introduction. Genetic prion diseases, such as Creutzfeldt-Jakob disease (CJD), Gerstmann-Straussler-Scheinker disease (GSS), Fatal Familial Insomnia (FFI), are associated with the mutations of prion (PRNP) gene. More than 30 pathogenic PRNP mutations were identified. Since Alzheimer disease (AD) and prion diseases have many similarities in the neuropathological and physiological symptoms, we te...
متن کاملPrion protein NMR structure and species barrier for prion diseases.
The structural basis of species specificity of transmissible spongiform encephalopathies, such as bovine spongiform encephalopathy or "mad cow disease" and Creutzfeldt-Jakob disease in humans, has been investigated using the refined NMR structure of the C-terminal domain of the mouse prion protein with residues 121-231. A database search for mammalian prion proteins yielded 23 different sequenc...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1995
ISSN: 0021-9258
DOI: 10.1074/jbc.270.32.19173