ArticlePrion
Prion pathogenesis and secondary lymphoid organs (SLO): tracking the SLO spread of prions to the brain.
Article in Prion. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
11 citing papers in PubMed, 17 citations in OpenAlex.
- Cases of Creutzfeldt-Jakob disease in young individuals: open questions regarding aetiology.Frontiers in cellular neuroscience · 2025Article
- Environmental and host factors that contribute to prion strain evolution.Acta neuropathologica · 2021Review
- The Effects of Immune System Modulation on Prion Disease Susceptibility and Pathogenesis.International journal of molecular sciences · 2020Review
- Appendectomy, Tonsillectomy and Parkinson's Disease Risk: A Swedish Register-Based Study.Frontiers in neurology · 2020Article
- Limited understanding of the functional diversity of N-linked glycans as a major gap of prion biology.Prion · 2017Article
- Sialylation Controls Prion FateThe Journal of biological chemistry · 2017Article
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- Sialylation of prion protein controls the rate of prion amplification, the cross-species barrier, the ratio of PrPSc glycoform and prion infectivity.PLoS pathogens · 2014Article
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Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
Prion diseases are subacute neurodegenerative diseases that affect humans and a range of domestic and free-ranging animal species. These diseases are characterized by the accumulation of PrP (Sc), an abnormally folded isoform of the cellular prion protein (PrP (C)), in affected tissues. The pathology during prion disease appears to occur almost exclusively within the central nervous system. The extensive neurodegeneration which occurs ultimately leads to the death of the host. An intriguing feature of the prion diseases, when compared with other protein-misfolding diseases, is their transmissibility. Following peripheral exposure, some prion diseases accumulate to high levels within lymphoid tissues. The replication of prions within lymphoid tissue has been shown to be important for the efficient spread of disease to the brain. This article describes recent progress in our understanding of the cellular mechanisms that influence the propagation of prions from peripheral sites of exposure (such as the lumen of the intestine) to the brain. A thorough understanding of these events will lead to the identification of important targets for therapeutic intervention, or alternatively, reveal additional processes that influence disease susceptibility to peripherally-acquired prion diseases.
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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.