25 results for “prion”. Showing 25 of 39,449.
Astrocyte in prion disease: a double-edged sword.
prion disease are depositions of pathological prion protein PrPSc, neuronal
RNA-seq and network analysis reveal unique glial gene expression signatures during prion infection.
Prion diseases and prion-like disorders, including Alzheimer's disease
Prion disease modelled in Drosophila.
prion is considered responsible for transmission of these conditions. Prion
Genetic risk factors for Creutzfeldt-Jakob disease.
prion protein (PrP, gene PRNP) in their pathogenesis. Prions are infectious
Protein Misfolding in Prion and Prion-Like Diseases: Reconsidering a Required Role for Protein Loss-of-Function.
prion-like. Prion-like diseases involve the spread of degeneration
Prion and Prion-Like Protein Strains: Deciphering the Molecular Basis of Heterogeneity in Neurodegeneration.
prions. These observations have led to the terminology of "prion
Incomplete glycosylation during prion infection unmasks a prion protein epitope that facilitates prion detection and strain discrimination.
prion protein (PrPC) into its infectious counterpart (PrPSc) during prion
Genetically engineered cellular models of prion propagation.
prion replication and the identification of candidate therapeutics for prion
Prion disease is accelerated in mice lacking stress-induced heat shock protein 70 (HSP70).
prions. Prions are composed of PrPSc, a misfolded version of the cellular
Ablation of progranulin augments microglial activation and accelerates prion progression.
prion diseases. We observed that prion infection upregulated microglial PGRN
Quaternary structure of pathological prion protein as a determining factor of strain-specific prion replication dynamics.
prion replication. This has important implications for fundamental studies on prions
The cell biology of prion-like spread of protein aggregates: mechanisms and implication in neurodegeneration.
prion diseases. Among these, only prion diseases are 'infectious'. By seeding
The role of microglia in the prion-like transmission of protein aggregates in neurodegeneration.
prion-like manner. A protein/peptide that adopts a prion-like
Expanding spectrum of prion diseases.
prion disorder: both Aβ and tau prions feature in this
Antisense oligonucleotides extend survival of prion-infected mice.
Prion disease is a fatal, incurable neurodegenerative disease of humans
Molecular Mechanism of the Misfolding and Oligomerization of the Prion Protein: Current Understanding and Its Implications.
prion diseases and for developing anti-prion therapeutics. This review
The importance of prion research.
prion diseases have received considerable research attention owing to their
Neurodegeneration and oxidative stress: prion disease results from loss of antioxidant defence.
prion protein expression is switched off during the course of prion
Disease-associated prion protein oligomers inhibit the 26S proteasome.
prion protein. We report that disease-associated prion protein specifically
Spontaneous generation of rapidly transmissible prions in transgenic mice expressing wild-type bank vole prion protein.
prion disorder, sporadic Creutzfeldt-Jakob disease (CJD), in which prions
Therapeutic Trajectories in Human Prion Diseases.
Prion diseases are rare yet devastating neurodegenerative disorders that result
Acute Neurotoxicity Models of Prion Disease.
prion disease patho-biology. Prion animal models are arguably the most
Treatment with efavirenz extends survival in a Creutzfeldt-Jakob disease model by regulating brain cholesterol metabolism.
prions often fail in human prion diseases, and a relation
Creutzfeldt-Jakob disease and other prion diseases.
prion protein. The characteristic features of prion diseases are long
Tau prions from Alzheimer's disease and chronic traumatic encephalopathy patients propagate in cultured cells.
prions. These results allowed us to determine the levels of tau prions