ReviewPathogens (Basel, Switzerland)2013
Prions in variably protease-sensitive prionopathy: an update.
Review in Pathogens (Basel, Switzerland), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 26 citations in OpenAlex.
- Phosphatidic Acid Vesicles Convert the Prion Protein into β-Sheet Fibrils with a Thermostable Structure but Temperature-Sensitive Packing.International journal of molecular sciences · 2026Article
- Variably Protease-Sensitive Prionopathy: Two New Cases With Motor Neuron-Dementia Syndrome.Annals of clinical and translational neurology · 2026Article
- Variably protease-sensitive prionopathy: mass spectrometry analysis of the pathogenic prion protein provides a new perspective.Acta neuropathologica communications · 2025Article
- Characterization of variably protease-sensitive prionopathy by capillary electrophoresis.Scientific reports · 2024Article
- Updated global epidemiology atlas of human prion diseases.Frontiers in public health · 2024Article
- Non-human primates in prion diseases.Cell and tissue research · 2023Review
- Phenotypic Heterogeneity of Variably Protease-Sensitive Prionopathy: A Report of Three Cases Carrying Different Genotypes atViruses · 2022Article
- Selective vulnerability to atrophy in sporadic Creutzfeldt-Jakob disease.Annals of clinical and translational neurology · 2021Article
- Review
- Further Characterization of Glycoform-Selective Prions of Variably Protease-Sensitive Prionopathy.Pathogens (Basel, Switzerland) · 2021Article
- In Vitro Seeding Activity of Glycoform-Deficient Prions from Variably Protease-Sensitive Prionopathy and Familial CJD Associated with PrPMolecular neurobiology · 2019Article
- Variably protease-sensitive prionopathy: A differential diagnostic consideration for dementia.Neurology. Clinical practice · 2019Review
- Soluble polymorphic bank vole prion proteins induced by co-expression of quiescin sulfhydryl oxidase in E. coli and their aggregation behaviors.Microbial cell factories · 2017Article
- Prions: Beyond a Single Protein.Clinical microbiology reviews · 2016Review
- Synthetic Aβ peptides acquire prion-like properties in the brain.Oncotarget · 2015Article
Corrections and comments
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Authors and funding
6 authors at 5 institutions in 4 countries.
Funding
Abstract
Human prion diseases, including sporadic, familial, and acquired forms such as Creutzfeldt-Jakob disease (CJD), are caused by prions in which an abnormal prion protein (PrPSc) derived from its normal cellular isoform (PrPC) is the only known component. The recently-identified variably protease-sensitive prionopathy (VPSPr) is characterized not only by an atypical clinical phenotype and neuropathology but also by the deposition in the brain of a peculiar PrPSc. Like other forms of human prion disease, the pathogenesis of VPSPr also currently remains unclear. However, the findings of the peculiar features of prions from VPSPr and of the possible association of VPSPr with a known genetic prion disease linked with a valine to isoleucine mutation at residue 180 of PrP reported recently, may be of great importance in enhancing our understanding of not only this atypical human prion disease in particular, but also other prion diseases in general. In this review, we highlight the physicochemical and biological properties of prions from VPSPr and discuss the pathogenesis of VPSPr including the origin and formation of the peculiar prions.
Identifiers
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Registered trials
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.