Results 251 to 260 of about 48,246 (290)
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Yeast Prions Compared to Functional Prions and Amyloids.
Journal of Molecular Biology, 2018Saccharomyces cerevisiae is an occasional host to an array of prions, most based on self-propagating, self-templating amyloid filaments of a normally soluble protein. [URE3] is a prion of Ure2p, a regulator of nitrogen catabolism, while [PSI+] is a prion
R. Wickner +5 more
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Post-conversion sialylation of prions in lymphoid tissues
Proceedings of the National Academy of Sciences of the United States of America, 2015 Ilia Baskakov +2 more
exaly +2 more sources
1996
List of Contents.- Human Prion Diseases and Neurodegeneration.- Fatal Familial Insomnia and Familial Creutzfeldt-Jakob Disease: A Tale of Two Diseases with the Same Genetic Mutation.- Human Prion Disease and Human Prion Protein Disease.- Prion Strains.- Structures of Prion Proteins and Conformational Models for Prion Diseases.- The Folding Intermediate
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List of Contents.- Human Prion Diseases and Neurodegeneration.- Fatal Familial Insomnia and Familial Creutzfeldt-Jakob Disease: A Tale of Two Diseases with the Same Genetic Mutation.- Human Prion Disease and Human Prion Protein Disease.- Prion Strains.- Structures of Prion Proteins and Conformational Models for Prion Diseases.- The Folding Intermediate
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The Lancet Neurology, 2005
Prion diseases are degenerative disorders of the nervous system caused by transmissible particles that contain a pathogenic isoform of the prion protein, a normal constituent of cell membranes. The most common human prion disease is Creutzfeldt-Jakob disease (CJD). Most cases are sporadic with unknown mode of transmission, 10-15% of cases are inherited,
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Prion diseases are degenerative disorders of the nervous system caused by transmissible particles that contain a pathogenic isoform of the prion protein, a normal constituent of cell membranes. The most common human prion disease is Creutzfeldt-Jakob disease (CJD). Most cases are sporadic with unknown mode of transmission, 10-15% of cases are inherited,
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Aptamers against prion proteins and prions
Cellular and Molecular Life Sciences, 2009Prion diseases are fatal neurodegenerative and infectious disorders of humans and animals, characterized by structural transition of the host-encoded cellular prion protein (PrP(c)) into the aberrantly folded pathologic isoform PrP(Sc). RNA, DNA or peptide aptamers are classes of molecules which can be selected from complex combinatorial libraries for ...
Sabine, Gilch, Hermann M, Schätzl
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Prion Diseases and Emerging Prion Diseases
Current Medicinal Chemistry, 2008Transmissible spongiform encephalopathies (TSEs), also called prion diseases, are fatal neurodegenerative disorders. An abnormal isoform of the prion protein (PrP(Sc)) generated by post-translational modification of the cellular prion protein (PrP(C)) is believed to be the main component of this infectious agent.
Takashi, Yokoyama, Shirou, Mohri
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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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Cell biology. A Unifying Role for Prions in Neurodegenerative Diseases
Science, 2012A profound change in thinking about the etiologies of many neurodegenerative diseases has far-reaching implications for developing therapeutics. Many neurodegenerative diseases—including Creutzfeldt-Jakob disease, Alzheimer's disease (AD), Parkinson's ...
S. Prusiner
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Prion and Non-prion Amyloids of the HET-s Prion forming Domain
Journal of Molecular Biology, 2007HET-s is a prion protein of the fungus Podospora anserina. A plausible structural model for the infectious amyloid fold of the HET-s prion-forming domain, HET-s(218-289), makes it an attractive system to study structure-function relationships in amyloid assembly and prion propagation.
Sabate, R. +9 more
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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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