Prion Diseases and Protein Misfolding

The paper evaluates the feasibility of using non-human primate models to assess prion disease therapeutic efficacy by analyzing incubation times and model characteristics.

The paper identifies early translatome changes in specific neural cell types before EEG and neuropathological signs of prion disease in mice.

This study identifies an H-latch conformational switch in PrPC that drives prion toxicity and shows that disrupting this switch can protect against prion-related neurodegeneration.

This study shows that complete microglia deficiency accelerates CNS prion disease without increasing prion accumulation, suggesting microglia protect against astrocyte-driven pathology rather than clearing prions.

The paper develops a field-deployable diagnostic assay, MN-QuIC, for visual detection of misfolded prions in CWD-infected deer, showing 100% consistency with established tests.

The paper investigates the transcriptomic response of Prnp and Sprn double knockout mouse embryos to ShRNA lentiviral inoculation, finding reduced apoptosis and interferon responses in the double knockout compared to single knockouts.

The paper introduces a Drosophila model expressing human PrP to study intrinsic and extrinsic factors mediating its toxicity, identifying key cellular mechanisms and protective mutations.

This study develops a bank vole glia cell assay that can propagate multiple rodent-adapted scrapie prions, showing comparable or faster propagation than traditional host cell models.

The paper shows that ligands binding to PrPC induce its proteolytic release, which has neuroprotective effects, and identifies mechanisms and exceptions in this process.

The paper shows viral ligand-receptor interactions enhance the spread of protein misfolding via extracellular vesicles and direct cell contact.

This study uses RT-QuIC to detect CWD prion seeding activity in skeletal muscles of infected white-tailed deer, finding prions in consumption-relevant tissues and highlighting their broader distribution.

The paper shows that loss of PIKfyve contributes to spongiform degeneration in prion diseases by linking prion infection to PIKfyve destabilization and vacuolation.

This study investigates the role of Msr1 in prion clearance and pathogenesis, finding that Msr1 deficiency does not affect prion disease progression or neuroinflammation.

The paper assesses genomic variation and PRNP gene diversity in white-tailed deer to infer susceptibility to chronic wasting disease and demographic history.

This study uses ribosome profiling to show that prion disease causes minor translational changes in neurons but significant changes in glia, overlapping with other neurodegenerative diseases.

The paper identifies protective anti-prion antibodies in human immunoglobulin repertoires and finds they are present in healthy individuals without associated pathologies.

This study shows that lowering prion protein expression with ASOs is effective in treating prion disease across different strains, treatment times, and endpoints.

The paper describes a human cell line, hovS, that can be infected with sheep-derived prions and exhibits prion-related cytopathology, offering a safer alternative to human prion studies.

The paper identifies early molecular changes in prion-infected mice, suggesting glial pathophysiology as a key driver and potential targets for intervention.

The paper introduces a mathematical model to study prion propagation in yeast, revealing a bi-stable switch mechanism and new insights into prion curing and aggregate replication.

The paper examines how sequence variation in prion-like domains (PrLDs) affects aggregation propensity in human proteins, identifying mutations linked to increased aggregation and disease.

The paper quantifies the geographic distribution of PRNP variants in white-tailed deer to assess CWD susceptibility and management implications.

The paper develops a targeted mass spectrometry method to quantify prion protein in CSF, confirming that reduced PrP levels in prion disease are due to the disease process, not ELISA artifacts.

This study demonstrates that peptoid-conjugated beads can capture and transmit prion infectivity from blood, validating a sensitive assay for prion detection.

This paper quantifies the challenges of designing preventive clinical trials for genetic prion disease due to high variability in age of onset, suggesting the need for biomarker-based trials.

The paper maps amyloid cores of 26 [PSI+] prion isolates and identifies two distinct structural classes based on digestion patterns and phenotypic effects.

This study evaluates ELISA-based quantification of PrP in CSF as a biomarker for PrP-reducing therapeutics, showing its reliability and CNS origin.

This study shows that SARM1 deficiency accelerates prion disease progression by upregulating XAF1, leading to increased neuronal apoptosis.

The paper reviews advances in understanding the structures of Tau and Syn amyloids and discusses their implications for prion strain diversity mechanisms.

This study investigates the role of Del-1 in prion disease progression and finds that its absence does not affect prion pathogenesis, clearance, or neuroinflammation in mice.