ArticleScientific reports2025
A noninvasive test for human prion disease using hair roots and scalp.
Article in Scientific reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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Who cites it
1 citing paper in PubMed.
- From a prion seed to a tree of discoveries: Byron Caughey's RT-QuIC legacy in protein misfolding research.Acta neuropathologica · 2026Review
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30 authors.
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Abstract
Invasive tests like cerebrospinal fluid (CSF) examination are highly effective for diagnosing human prion disease (HPD). Real-time quaking-induced conversion (RT-QuIC) CSF assay demonstrates 80-90% sensitivity for HPD diagnosis. To establish a minimally invasive diagnostic approach, we evaluated RT-QuIC testing on hair root and scalp samples. We collected scalp samples from 22 HPD and 5 non-HPD patients during pathological examinations and analyzed them using RT-QuIC assay and neuropathological methods. In our prospective study, hair root and CSF samples from 300 patients were tested using RT-QuIC assay along with other biomarkers, including 14-3-3 protein, total tau protein, RT-QuIC CSF assay, and MRI findings. All 22 HPD patients demonstrated positive prion seeding activity in scalp and hair root RT-QuIC assays. Neuropathological examination in one HPD patient revealed abnormal prion protein in scalp tissue. Among 177 HPD patients diagnosed by Japan Prion Surveillance Committee and 123 non-HPD patients, RT-QuIC assay of hair roots demonstrated sensitivity and specificity of 45.8% and 100%, respectively. Sensitivities of 14-3-3 protein, total tau protein, RT-QuIC CSF assay, and MRI findings were 83.1%, 86.4%, 74.6%, and 100%, respectively, with specificities of 65.0%, 65.0%, 100%, and 56.1%, respectively. RT-QuIC assays could be developed into novel diagnostic methods for neurodegenerative diseases.
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