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Treatment of Prion Disease with Heterologous Prion ProteinsInteractions between the Conserved Hydrophobic Region of the Prion Protein and Dodecylphosphocholine MicellesRNA-silencing enzymes Pol IV and Pol V in maize: more than one flavor?Human prion diseases in the United States.Expectations, validity, and reality in gene expression profiling.Strain specific resistance to murine scrapie associated with a naturally occurring human prion protein polymorphism at residue 171.Sequence-dependent prion protein misfolding and neurotoxicity.Proteomics analysis of amyloid and nonamyloid prion disease phenotypes reveals both common and divergent mechanisms of neuropathogenesisChaperoning osteogenesis: new protein-folding disease paradigms.Discovering putative prion sequences in complete proteomes using probabilistic representations of Q/N-rich domains.Candidate cell substrates, vaccine production, and transmissible spongiform encephalopathies.Mouse-adapted scrapie strains 139A and ME7 overcome species barrier to induce experimental scrapie in hamsters and changed their pathogenic features.Therapeutic effect of CHF5074, a new γ-secretase modulator, in a mouse model of scrapie.Dissociation of recombinant prion protein fibrils into short protofilaments: implications for the endocytic pathway and involvement of the N-terminal domain.Identification and removal of proteins that co-purify with infectious prion protein improves the analysis of its secondary structure.Comparative profiling of highly enriched 22L and Chandler mouse scrapie prion protein preparations.Prion diseases as transmissible zoonotic diseases.Minocycline as a potential therapeutic agent in neurodegenerative disorders characterised by protein misfoldingRole of prions in neuroprotection and neurodegeneration: a mechanism involving glutamate receptors?Basic mechanisms of neurodegeneration: a critical update.Proteomics applications in prion biology and structure.Analysis of core region from egg white lysozyme forming amyloid fibrils.Perspective Insights of Exosomes in Neurodegenerative Diseases: A Critical Appraisal.Do prion protein gene polymorphisms induce apoptosis in non-mammals?Enhanced neural progenitor/stem cells self-renewal via the interaction of stress-inducible protein 1 with the prion protein.The Role of Post-Translational Modifications on Prion-Like Aggregation and Liquid-Phase Separation of FUS.Exploration of the Main Sites for the Transformation of Normal Prion Protein (PrP) into Pathogenic Prion Protein (PrP)
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description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 20 January 2009
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Prion protein misfolding and disease.
@en
Prion protein misfolding and disease.
@nl
type
label
Prion protein misfolding and disease.
@en
Prion protein misfolding and disease.
@nl
prefLabel
Prion protein misfolding and disease.
@en
Prion protein misfolding and disease.
@nl
P2093
P2860
P1476
Prion protein misfolding and disease.
@en
P2093
Lara M Taubner
Roger A Moore
Suzette A Priola
P2860
P356
10.1016/J.SBI.2008.12.007
P577
2009-01-20T00:00:00Z