ArticleBrain pathology (Zurich, Switzerland)2012
Mechanism of PrP-amyloid formation in mice without transmissible spongiform encephalopathy.
Article in Brain pathology (Zurich, Switzerland), 2012. 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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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
12 citing papers in PubMed, 21 citations in OpenAlex.
- Review
- Infectious prions and proteinopathies.Prion · 2017Article
- Distribution of Misfolded Prion Protein Seeding Activity Alone Does Not Predict Regions of Neurodegeneration.PLoS biology · 2016Article
- PrP aggregation can be seeded by pre-formed recombinant PrP amyloid fibrils without the replication of infectious prions.Acta neuropathologica · 2016Article
- Insights into Mechanisms of Chronic Neurodegeneration.International journal of molecular sciences · 2016Review
- Evaluation of infective property of recombinant prion protein amyloids in cultured cells overexpressing cellular prion protein.Journal of Korean medical science · 2014Article
- Complex proteinopathy with accumulations of prion protein, hyperphosphorylated tau, α-synuclein and ubiquitin in experimental bovine spongiform encephalopathy of monkeys.The Journal of general virology · 2014Article
- Glycosylphosphatidylinositol anchoring directs the assembly of Sup35NM protein into non-fibrillar, membrane-bound aggregates.The Journal of biological chemistry · 2014Article
- Pathology of SSLOW, a transmissible and fatal synthetic prion protein disorder, and comparison with naturally occurring classical transmissible spongiform encephalopathies.Neuropathology and applied neurobiology · 2014Article
- Dissociation of prion protein amyloid seeding from transmission of a spongiform encephalopathy.Journal of virology · 2013Article
- Review
- Prion protein misfolding, strains, and neurotoxicity: an update from studies on Mammalian prions.International journal of cell biology · 2013Review
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
Gerstmann-Sträussler-Scheinker (GSS) P102L disease is a familial form of a transmissible spongiform encephalopathy (TSE) that can present with or without vacuolation of neuropil. Inefficient disease transmission into 101LL transgenic mice was previously observed from GSS P102L without vacuolation. However, several aged, healthy mice had large plaques composed of abnormal prion protein (PrP(d)). Here we perform the ultrastructural characterization of such plaques and compare them with PrP(d) aggregates found in TSE caused by an infectious mechanism. PrP(d) plaques in 101LL mice varied in maturity, with some being composed of deposits without visible amyloid fibrils. PrP(d) was present on cell membranes in the vicinity of all types of plaques. In contrast to the unicentric plaques seen in infectious murine scrapie, the plaques seen in the current model were multicentric and were initiated by protofibrillar forms of PrP(d) situated on oligodendroglia, astrocytes and neuritic cell membranes. We speculate that the initial conversion process leading to plaque formation begins with membrane-bound PrP(C) but that subsequent fibrillization does not require membrane attachment. We also observed that the membrane alterations consistently seen in murine scrapie and other infectious TSEs were not present in 101LL mice with plaques, suggesting differences in the pathogenesis of these conditions.
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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.