Cell adhesion molecule CD44 is dispensable for reactive astrocyte activation during prion disease. [PDF]
Bradford BM +4 more
europepmc +2 more sources
Neurofilament Light Chain Levels in Serum and Cerebrospinal Fluid Do Not Correlate with Survival Times in Patients with Prion Disease. [PDF]
Shimamura M +9 more
europepmc +1 more source
Neuropathologically directed profiling of PRNP somatic and germline variants in sporadic human prion disease. [PDF]
McDonough GA +13 more
europepmc +1 more source
Fluid Biomarkers in Individuals at Risk for Genetic Prion Disease up to Disease Conversion. [PDF]
Vallabh SM +16 more
europepmc +1 more source
Molecular signatures in prion disease: altered death receptor pathways in a mouse model. [PDF]
Giri RK.
europepmc +1 more source
Expression of Toll-like receptors in the cerebellum during pathogenesis of prion disease. [PDF]
Liao X +5 more
europepmc +1 more source
Prion protein E219K polymorphism: from the discovery of the KANNO blood group to interventions for human prion disease. [PDF]
Wang SS +4 more
europepmc +1 more source
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AbstractPrion diseases are a phenotypically diverse set of disorders characterized by protease-resistant abnormally shaped proteins known as prions. There are three main groups of prion diseases, termed sporadic (Creutzfeldt–Jakob disease [CJD], sporadic fatal insomnia, and variably protease-sensitive prionopathy), genetic (genetic CJD, fatal familial ...
Kelly J, Baldwin, Cynthia M, Correll
openaire +3 more sources
Genetic prion diseases (gPrDs) are caused by autosomal-dominant mutations in the prion protein gene (PRNP). Although the first PRNP mutations identified, and most since, are PRNP missense, octapeptide repeat insertions, deletion and nonsense mutations have now also been shown to cause gPrD. Based on clinicopathologic features of familial disease, gPrDs
Leonel T, Takada +4 more
openaire +3 more sources

