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The toxicity of antiprion antibodies is mediated by the flexible tail of the prion protein
Prion infections cause lethal neurodegeneration. This process requires the cellular prion protein (PrPC; ref. 1), which contains a globular domain hinged to a long amino-proximal flexible tail. HereExpand
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Prion Infections and Anti-PrP Antibodies Trigger Converging Neurotoxic Pathways
Prions induce lethal neurodegeneration and consist of PrPSc, an aggregated conformer of the cellular prion protein PrPC. Antibody-derived ligands to the globular domain of PrPC (collectively termedExpand
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Prion Pathogenesis Is Faithfully Reproduced in Cerebellar Organotypic Slice Cultures
Prions cause neurodegeneration in vivo, yet prion-infected cultured cells do not show cytotoxicity. This has hampered mechanistic studies of prion-induced neurodegeneration. Here we report thatExpand
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Structure-based drug design identifies polythiophenes as antiprion compounds
The targeted chemical design of luminescent conjugated polythiophenes may yield new therapeutic compounds for treating prion diseases. Putting prions in their place In a mouse model of prion disease,Expand
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Differential Toxicity of Antibodies to the Prion Protein
Antibodies against the prion protein PrPC can antagonize prion replication and neuroinvasion, and therefore hold promise as possible therapeutics against prion diseases. However, the safety profileExpand
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Triggering receptor expressed on myeloid cells-2 is involved in prion-induced microglial activation but does not contribute to prion pathogenesis in mouse brains
Dysfunctional variants of the innate immune cell surface receptor TREM2 (triggering receptor expressed on myeloid cells-2) were identified as major genetic risk factors for Alzheimer's disease andExpand
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Neurodegeneration and Unfolded-Protein Response in Mice Expressing a Membrane-Tethered Flexible Tail of PrP
The cellular prion protein (PrPC) consists of a flexible N-terminal tail (FT, aa 23–128) hinged to a membrane-anchored globular domain (GD, aa 129–231). Ligation of the GD with antibodies inducesExpand
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A neuroprotective role for microglia in prion diseases
Microglial activation is a hallmark of most neurodegenerative disorders, yet it is not clear if it plays beneficial or deleterious roles. Zhu et al. provide evidence for a general protective role ofExpand
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Correction: Prion Infections and Anti-PrP Antibodies Trigger Converging Neurotoxic Pathways
[This corrects the article DOI: 10.1371/journal.ppat.1004662.].
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