Mostrando 41 - 60 Resultados de 4,339 Para Buscar '"Prion"', tiempo de consulta: 0.55s Limitar resultados
  1. 41
    “…Many questions surround the underlying mechanism for the differential metabolic processing observed for the prion protein (PrP) in healthy and prion-infected mammals. …”
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  2. 42
    por Ma, Jiyan, Zhang, Jingjing, Yan, Runchuan
    Publicado 2022
    “…Generating a prion with exogenously produced recombinant prion protein is widely accepted as the ultimate proof of the prion hypothesis. …”
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  3. 43
    “…Previous studies have revealed that the infectious scrapie isoform of prion protein (PrP(Sc)) harbored in the skin tissue of patients or animals with prion diseases can be amplified and detected through the serial protein misfolding cyclic amplification (sPMCA) or real-time quaking-induced conversion (RT-QuIC) assays. …”
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  4. 44
    por Eraña, Hasier
    Publicado 2019
    “…However, instead of encompassing all these amyloidogenic proteins under the umbrella term "prion", new terminology has raised including the terms prion-like, prionoid, quasi-prion or propagon. …”
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  5. 45
    “…Prion diseases and the prion protein are only partially understood so far in many aspects. …”
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  7. 47
    “…The four glycoforms of the cellular prion protein (PrP(C)) variably glycosylated at the two N-linked glycosylation sites are converted into their pathological forms (PrP(Sc)) in most cases of sporadic prion diseases. …”
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  10. 50
    por Ma, Qian, Hu, Ji-Ying, Chen, Jie, Liang, Yi
    Publicado 2013
    “…Prion diseases and prion- like protein misfolding diseases are related to the accumulation of abnormal aggregates of the normal host proteins including prion proteins and Tau protein. …”
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  11. 51
    “…BACKGROUND: Prions are a particular type of amyloids related to a large variety of important processes in cells, but also responsible for serious diseases in mammals and humans. …”
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  12. 52
    por Dong, Xiao-Ping
    Publicado 2014
    “…Through human prion disease cases, infectious animal models, cell models and prion proteins, the neuropathological and pathogenic characteristics of prion diseases, the cytotoxicity of pathological prion, the conversion and replication of prion and the infectivity of prion strains were comprehensively evaluated. …”
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  13. 53
    “…INTRODUCTION: The prion protein (PrP) binds to various molecular partners, but little is known about their potential impact on the pathogenesis of prion diseases RESULTS: Here, we show that PrP can interact in vitro with acetylcholinesterase (AChE), a key protein of the cholinergic system in neural and non-neural tissues. …”
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  14. 54
    “…Antibodies targeting the globular domain (GD) of the cellular prion protein PrP(C) trigger a neurotoxic syndrome morphologically and molecularly similar to prion disease. …”
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  15. 55
    “…Prions are unique infectious agents that replicate without a genome and cause neurodegenerative diseases that include chronic wasting disease (CWD) of cervids. …”
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  16. 56
    “…We found that prions can convert, but the efficiency of conversion is affected by polymorphic variation in the cervid and human prion protein genes. …”
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  18. 58
    “…The progressive spreading of these inclusions from initially affected sites to interconnected brain areas is reminiscent of the behavior of bona fide prions in transmissible spongiform encephalopathies (TSEs), hence the term prion-like proteins has been coined. …”
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  19. 59
    por Hara, Hideyuki, Sakaguchi, Suehiro
    Publicado 2020
    “…The normal cellular isoform of prion protein, designated PrP(C), is constitutively converted to the abnormally folded, amyloidogenic isoform, PrP(Sc), in prion diseases, which include Creutzfeldt-Jakob disease in humans and scrapie and bovine spongiform encephalopathy in animals. …”
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  20. 60
    por Cherry, Pearl, Gilch, Sabine
    Publicado 2020
    “…Prion diseases are fatal and transmissible neurodegenerative diseases in which the cellular form of the prion protein ‘PrP(c)’, misfolds into an infectious and aggregation prone isoform termed PrP(Sc), which is the primary component of prions. …”
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