ArticlePloS one2010
Preclinical deposition of pathological prion protein in muscle of experimentally infected primates.
Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 22 citations in OpenAlex.
- Presymptomatic pharmacological inhibition of mGluR5 improves survival in a mouse model of prion diseases.Acta neuropathologica communications · 2026Article
- In Vitro and In Vivo Evidence towards Fibronectin's Protective Effects against Prion Infection.International journal of molecular sciences · 2023Article
- Abnormal prion protein, infectivity and neurofilament light-chain in blood of macaques with experimental variant Creutzfeldt-Jakob disease.The Journal of general virology · 2022Article
- Detection of Pathognomonic Biomarker PrPBiomolecules · 2020Review
- The real-time quaking-induced conversion assay for detection of human prion disease and study of other protein misfolding diseases.Nature protocols · 2016Article
- The presence of disease-associated prion protein in skeletal muscle of cattle infected with classical bovine spongiform encephalopathy.The Journal of veterinary medical science · 2014Article
- Myositis facilitates preclinical accumulation of pathological prion protein in muscle.Acta neuropathologica communications · 2013Article
- Evaluation of the zoonotic potential of transmissible mink encephalopathy.Pathogens (Basel, Switzerland) · 2013Article
- BSE-associated prion-amyloid cardiomyopathy in primates.Emerging infectious diseases · 2013Article
- Inactivation of template-directed misfolding of infectious prion protein by ozone.Applied and environmental microbiology · 2012Article
- Infectivity in skeletal muscle of cattle with atypical bovine spongiform encephalopathy.PloS one · 2012Article
- Molecular structure of amyloid fibrils controls the relationship between fibrillar size and toxicity.PloS one · 2011Article
Corrections and comments
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Authors and funding
9 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Prion diseases are transmissible fatal neurodegenerative disorders affecting humans and animals. A central step in disease progression is the accumulation of a misfolded form (PrP(Sc)) of the host encoded prion protein (PrP(C)) in neuronal and non-neuronal tissues. The involvement of peripheral tissues in preclinical states increases the risk of accidental transmission. On the other hand, detection of PrP(Sc) in non-neuronal easy-accessible compartments such as muscle may offer a novel diagnostic tool. Primate models have proven invaluable to investigate prion diseases. We have studied the deposition of PrP(Sc) in muscle and central nervous system of rhesus monkeys challenged with sporadic Creutzfeldt-Jakob disease (sCJD), variant CJD (vCJD) and bovine spongiform encephalopathy (BSE) in preclinical and clinical stage using biochemical and morphological methods. Here, we show the preclinical presence of PrP(Sc) in muscle and central nervous system of rhesus monkeys experimentally infected with vCJD.
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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.