ArticleAnnals of neurology2010
Variably protease-sensitive prionopathy: a new sporadic disease of the prion protein.
Article in Annals of neurology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 113 papers.
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Who cites it
113 citing papers in PubMed, 286 citations in OpenAlex.
- The L108I polymorphism in mouse prion protein drives spontaneous disease and enhances transmission of atypical and classical prion strains.Brain pathology (Zurich, Switzerland) · 2026Article
- Enhanced Sensitivity of a Modified Quaking-Induced Conversion Diagnostic Test for the Broad Detection of Sporadic and Inherited Prion Diseases: A Retrospective Study.Annals of neurology · 2026Article
- Variably Protease-Sensitive Prionopathy: Two New Cases With Motor Neuron-Dementia Syndrome.Annals of clinical and translational neurology · 2026Article
- Prevalence and impact of comorbidities in amyotrophic lateral sclerosis.Journal of neural transmission (Vienna, Austria : 1996) · 2026Review
- Overexpression of bank vole PrP(I109) in mice induces a spontaneous atypical prion disease with sex-dependent onset, early NfL elevation, and universal prion strain permissiveness.Acta neuropathologica communications · 2026Article
- Variably protease-sensitive prionopathy: mass spectrometry analysis of the pathogenic prion protein provides a new perspective.Acta neuropathologica communications · 2025Article
- Search for a genetic cause of variably protease-sensitive prionopathy.PLoS pathogens · 2025Article
- Inducers and modulators of protein aggregation in Alzheimer's disease - Critical tools for understanding the foundations of aggregate structures.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2025Review
- Advancing Prion Diagnostics: RT-QuIC Applications in Peripheral Tissues.Sub-cellular biochemistry · 2025Review
- Detecting the Undetectable: Exploring the Diagnostic Potential of Protein Misfolding Cyclic Amplification in Human Prion Diseases.Sub-cellular biochemistry · 2025Review
- Biological Fluid Biomarkers in Human Prion Diseases with a Note on Biosafety.Sub-cellular biochemistry · 2025Review
- Characterization of variably protease-sensitive prionopathy by capillary electrophoresis.Scientific reports · 2024Article
- Convergent generation of atypical prions in knockin mouse models of genetic prion disease.The Journal of clinical investigation · 2024Article
- A Protein Misfolding Shaking Amplification-based method for the spontaneous generation of hundreds of bona fide prions.Nature communications · 2024Article
- Variably protease-sensitive prionopathy with methionine homozygosity at codon 129 in the prion protein gene.BMJ case reports · 2024Article
- Large-scale validation of skin prion seeding activity as a biomarker for diagnosis of prion diseases.Acta neuropathologica · 2024Article
- Anxiety in oncology outpatients is associated with perturbations in pathways identified in anxiety focused network pharmacology research.Supportive care in cancer : official journal of the Multinational Association of Supportive Care in Cancer · 2023Article
- Novel histotypes of sporadic Creutzfeldt-Jakob disease linked to 129MV genotype.Acta neuropathologica communications · 2023Article
- Pick's Disease, Seeding an Answer to the Clinical Diagnosis Conundrum.Biomedicines · 2023Review
- Prion strains: shining new light on old concepts.Cell and tissue research · 2023Review
53 more citing papers are in PubMed but not listed here.
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Authors and funding
29 authors at 14 institutions in 3 countries.
Funding
Abstract
objectiveThe objective of the study is to report 2 new genotypic forms of protease-sensitive prionopathy (PSPr), a novel prion disease described in 2008, in 11 subjects all homozygous for valine at codon 129 of the prion protein (PrP) gene (129VV). The 2 new PSPr forms affect individuals who are either homozygous for methionine (129MM) or heterozygous for methionine/valine (129MV).
methodsFifteen affected subjects with 129MM, 129MV, and 129VV underwent comparative evaluation at the National Prion Disease Pathology Surveillance Center for clinical, histopathologic, immunohistochemical, genotypical, and PrP characteristics.
resultsDisease duration (between 22 and 45 months) was significantly different in the 129VV and 129MV subjects. Most other phenotypic features along with the PrP electrophoretic profile were similar but distinguishable in the 3 129 genotypes. A major difference laid in the sensitivity to protease digestion of the disease-associated PrP, which was high in 129VV but much lower, or altogether lacking, in 129MV and 129MM. This difference prompted the substitution of the original designation with "variably protease-sensitive prionopathy" (VPSPr). None of the subjects had mutations in the PrP gene coding region.
interpretationBecause all 3 129 genotypes are involved, and are associated with distinguishable phenotypes, VPSPr becomes the second sporadic prion protein disease with this feature after Creutzfeldt-Jakob disease, originally reported in 1920. However, the characteristics of the abnormal prion protein suggest that VPSPr is different from typical prion diseases, and perhaps more akin to subtypes of Gerstmann-Sträussler-Scheinker disease.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.