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  1. 181
    “…Prion diseases reflect conformational conversion of benign isoforms of prion protein (PrP(C)) to malignant PrP(Sc) isoforms. …”
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    The Prion Disease Database: a comprehensive transcriptome resource for systems biology research in prion diseases
  2. 182
    “…Prion disease is a neurodegenerative malady, which is believed to be transmitted via a prion protein in its abnormal conformation (PrP(Sc)). …”
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    Recombinant prion protein induces a new transmissible prion disease in wild-type animals
  3. 183
    “…Prion interactions with soil may play an important role in the transmission of chronic wasting disease (CWD) and scrapie. …”
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    Effects of Solution Chemistry and Aging Time on Prion Protein Adsorption and Replication of Soil-Bound Prions
  4. 184
    “…The transmissible agent of prion disease consists of a prion protein in its abnormal, β-sheet rich state (PrP(Sc)), which is capable of replicating itself according to the template-assisted mechanism. …”
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    Genesis of Mammalian Prions: From Non-infectious Amyloid Fibrils to a Transmissible Prion Disease
  5. 185
    “…Bovine spongiform encephalopathy (BSE) and BSE-related disorders have been associated with a single major prion strain. Recently, 2 atypical, presumably sporadic forms of BSE have been associated with 2 distinct prion strains that are characterized mainly by distinct Western blot profiles of abnormal protease-resistant prion protein (PrP(res)), named high-type (BSE-H) and low-type (BSE-L), that also differed from classical BSE. …”
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    Classical Bovine Spongiform Encephalopathy by Transmission of H-Type Prion in Homologous Prion Protein Context
  6. 186
    “…In prion disease, a profound microglial activation that precedes neurodegeneration has been observed in the CNS. …”
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    Prion Peptide Uptake in Microglial Cells – The Effect of Naturally Occurring Autoantibodies against Prion Protein
  7. 187
    “…The existence of prion strains has been well documented in mammalian prion diseases. …”
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    Spontaneous Variants of the [RNQ+] Prion in Yeast Demonstrate the Extensive Conformational Diversity Possible with Prion Proteins
  8. 188
    por Harbi, Djamel, Harrison, Paul M.
    Publicado 2014
    “…Prions are transmissible, propagating alternative states of proteins. …”
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    Interaction Networks of Prion, Prionogenic and Prion-Like Proteins in Budding Yeast, and Their Role in Gene Regulation
  9. 189
    “…The conversion of the prion protein (PrP(C)) into prions plays a key role in transmissible spongiform encephalopathies. …”
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    The non-octarepeat copper binding site of the prion protein is a key regulator of prion conversion
  10. 190
    “…High social impact diseases such as Alzheimer's and Parkinson's belong to prion-like diseases. Accumulating evidence suggests that the exposure to environmental metals is a risk factor for the development of prion and prion-like diseases and that metal ions can directly bind to prion and prion-like proteins affecting the amount of amyloid aggregates. …”
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    Metal Dyshomeostasis and Their Pathological Role in Prion and Prion-Like Diseases: The Basis for a Nutritional Approach
  11. 191
    “…Detection of proteinase K-resistant prion protein (PrP(Sc)) still represents the diagnostic gold standard for prion diseases in humans, sheep and cattle. …”
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    Protease resistance of infectious prions is suppressed by removal of a single atom in the cellular prion protein
  12. 192
    “…Prion diseases are infectious neurodegenerative disorders of humans and animals caused by misfolded forms of the cellular prion protein PrP(C). …”
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    Destabilizing polymorphism in cervid prion protein hydrophobic core determines prion conformation and conversion efficiency
  13. 193
    “…A number of fungal proteins are capable of adopting multiple alternative, self-perpetuating prion conformations. These prion variants are associated with functional alterations of the prion-forming protein and thus the generation of new, heritable traits that can be detrimental or beneficial. …”
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    Prion-dependent proteome remodeling in response to environmental stress is modulated by prion variant and genetic background
  14. 194
    “…Prion diseases are fatal transmissible neurodegenerative conditions of humans and animals that arise through neurotoxicity induced by PrP misfolding. …”
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    Transcriptional signature of prion-induced neurotoxicity in a Drosophila model of transmissible mammalian prion disease
  15. 195
    “…The interaction of prion protein (PrP) and α-synuclein (αSyn) oligomers causes synaptic impairment that might trigger Parkinson’s disease and other synucleinopathies. …”
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    Clustering of human prion protein and α-synuclein oligomers requires the prion protein N-terminus
  16. 196
    “…Prion diseases are caused by misfolded prion protein (PrP(Sc)) and are accompanied by spongiform vacuolation of brain lesions. …”
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    Identification of Prion Disease-Related Somatic Mutations in the Prion Protein Gene (PRNP) in Cancer Patients
  17. 197
    “…Examples of such protein misfolding diseases include Alzheimer’s disease, Parkinson’s disease, Huntington’s disease, amyotrophic lateral sclerosis, and prion diseases. The misfolded proteins involved in these diseases form self-templating oligomeric assemblies that recruit further correctly folded protein and induce their conversion. …”
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    From Seeds to Fibrils and Back: Fragmentation as an Overlooked Step in the Propagation of Prions and Prion-Like Proteins
  18. 198
    “…The studies of prions and prion disease usually need many special platforms and techniques that differ from those for classical microbes. …”
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    Establishment of a Special Platform for the Research of Prion and the Diagnosis of Human Prion Disease — China’s Studies
  19. 199
    “…This study examines the effect of various infectious prion titers within the dynamic range as measured by ELISA on incubation period. …”
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    Effect of inoculation with prion dilutions within the dynamic range of ELISA absorbance on prion incubation period
  20. 200
    Publicado 2013
    Materias: “…Prion 2013…”
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    Introduction: Invited Speakers
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