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  1. 81
    por Requena, Jesús R.
    Publicado 2020
    “…The prion protein, PrP, can adopt at least 2 conformations, the overwhelmingly prevalent cellular conformation (PrP(C)) and the scrapie conformation (PrP(Sc)). …”
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    The protean prion protein
  2. 82
    por Li, Bei, Chen, Meiling, Zhu, Caihong
    Publicado 2021
    “…Neuroinflammation, typically manifest as microglial activation and astrogliosis accompanied by transcriptomic alterations, represents a common hallmark of various neurodegenerative conditions including prion diseases. Microglia play an overall neuroprotective role in prion disease, whereas reactive astrocytes with aberrant phenotypes propagate prions and contribute to prion-induced neurodegeneration. …”
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    Neuroinflammation in Prion Disease
  3. 83
    por Will, Robert G
    Publicado 1999
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    Prion Related Disorders
  4. 84
    por King, Chih-Yen
    Publicado 2022
    “…The question of whether prions are prone to mis-templating is not completely answered. …”
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    The Mutability of Yeast Prions
  5. 85
    “…The conversion of cellular prion protein (PrP(C)) into pathogenic prion isoforms (PrP(Sc)) and the mutation of PRNP are definite causes of prion diseases. …”
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    Radotinib Decreases Prion Propagation and Prolongs Survival Times in Models of Prion Disease
  6. 86
    “…Prions are composed of PrP(Sc), the disease specific conformation of the host encoded prion protein. …”
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    Evidence for preexisting prion substrain diversity in a biologically cloned prion strain
  7. 87
    “…Experimental obstacles have impeded our ability to study prion transmission within and, more particularly, between species. …”
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    Accelerated High Fidelity Prion Amplification Within and Across Prion Species Barriers
  8. 88
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    Correction: Glycoform-Selective Prion Formation in Sporadic and Familial Forms of Prion Disease
  9. 89
    “…Prion diseases, also known as transmissible spongiform encephalopathies (TSEs), are a group of fatal neurodegenerative disorders affecting humans and other mammalian species. …”
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    Prion Protein Misfolding, Strains, and Neurotoxicity: An Update from Studies on Mammalian Prions
  10. 90
    por Olsthoorn, René C.L.
    Publicado 2014
    “…Cellular ribonucleic acid (RNA) plays a crucial role in the initial conversion of cellular prion protein PrP(C) to infectious PrP(Sc) or scrapie. …”
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    G-quadruplexes within prion mRNA: the missing link in prion disease?
  11. 91
    “…Recent studies introduced two experimental protocols for converting full-length recombinant prion protein (rPrP) purified from E.coli into the infectious prion state (PrP(Sc)) with high infectivity titers. …”
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    Contrasting Effects of Two Lipid Cofactors of Prion Replication on the Conformation of the Prion Protein
  12. 92
    “…The budding yeast Saccharomyces cerevisiae is a valuable model system for studying prion-prion interactions as it contains multiple prion proteins. …”
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    An insight into the complex prion-prion interaction network in the budding yeast Saccharomyces cerevisiae
  13. 93
    “…Prion or PrP(Sc) is a proteinaceous infectious agent that consists of a misfolded and aggregated form of a sialoglycoprotein called prion protein or PrP(C). …”
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    Sialylation of the prion protein glycans controls prion replication rate and glycoform ratio
  14. 94
    por Nyström, Sofie, Hammarström, Per
    Publicado 2015
    “…Prion diseases are lethal, infectious diseases associated with prion protein (PrP) misfolding. …”
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    Generic amyloidogenicity of mammalian prion proteins from species susceptible and resistant to prions
  15. 95
    “…According to the protein-only hypothesis, infectious mammalian prions, which exist as distinct strains with discrete biological properties, consist of multichain assemblies of misfolded cellular prion protein (PrP). …”
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    A systematic investigation of production of synthetic prions from recombinant prion protein
  16. 96
    “…Moreover, brains and spleens of animals from the latter group were completely cleared of prions. The current work established that the ability of prions to infect the host via intracerebral administration depends on PrP(Sc) sialylation status. …”
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    Reversible off and on switching of prion infectivity via removing and reinstalling prion sialylation
  17. 97
    “…Prion diseases are fatal infectious neurodegenerative disorders in humans and other animals and are caused by misfolding of the cellular prion protein (PrP(C)) into the pathological isoform PrP(Sc). …”
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    Overexpression of quality control proteins reduces prion conversion in prion-infected cells
  18. 98
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    Publisher Correction: Early preclinical detection of prions in the skin of prion-infected animals
  19. 99
    “…This review focuses on the molecular basis of the strain phenomenon in prion and prion-like proteins.…”
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    Prion and Prion-Like Protein Strains: Deciphering the Molecular Basis of Heterogeneity in Neurodegeneration
  20. 100
    “…So far, experimental studies have been limited in directly analyzing the earliest events of the conformational change of cellular prion protein (PrP(C)) into scrapie prion protein (PrP(Sc)) that further propagates PrP(C) misfolding and aggregation at the cellular membrane, the initial site of prion infection, and PrP misfolding, by a lack of suitably modified PrP variants. …”
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    Prion protein—Semisynthetic prion protein (PrP) variants with posttranslational modifications
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