ReviewJournal of molecular neuroscience : MN2006
Prions: protein only or something more? Overview of potential prion cofactors.
Review in Journal of molecular neuroscience : MN, 2006. 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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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
15 citing papers in PubMed, 28 citations in OpenAlex.
- Production of seedable Amyloid-β peptides in model of prion diseases upon PrPNature communications · 2019Article
- Prions: Beyond a Single Protein.Clinical microbiology reviews · 2016Review
- Unchanged survival rates of Shadoo knockout mice after infection with mouse-adapted scrapie.Prion · 2014Article
- Introducing a rigid loop structure from deer into mouse prion protein increases its propensity for misfolding in vitro.PloS one · 2013Article
- Infrared microspectroscopy: a multiple-screening platform for investigating single-cell biochemical perturbations upon prion infection.ACS chemical neuroscience · 2011Article
- Na+/K+-ATPase is present in scrapie-associated fibrils, modulates PrP misfolding in vitro and links PrP function and dysfunction.PloS one · 2011Article
- Mapping the interaction site of prion protein and Sho.Molecular biology reports · 2010Article
- Redox control of prion and disease pathogenesis.Antioxidants & redox signaling · 2010Review
- Low density subcellular fractions enhance disease-specific prion protein misfolding.The Journal of biological chemistry · 2010Article
- Interactome analyses identify ties of PrP and its mammalian paralogs to oligomannosidic N-glycans and endoplasmic reticulum-derived chaperones.PLoS pathogens · 2009Article
- The variant Creutzfeldt-Jakob Disease: Risk, uncertainty or safety in the use of blood and blood derivatives?International archives of medicine · 2008Article
- Characterization of the genomic region containing the Shadow of Prion Protein (SPRN) gene in sheep.BMC genomics · 2007Article
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Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Transmissible spongiform encephalopathies (TSEs) in humans and animals are attributed to protein-only infectious agents, called prions. Prions have been proposed to arise from the conformational conversion of the cellular protein PrP(C) into a misfolded form (e.g., PrP(Sc) for scrapie), which precipitates into aggregates and fibrils. It has been proposed that the conversion process is triggered by the interaction of the infectious form (PrP(Sc)) with the cellular form (PrP(C)) or might result from a mutation in the gene for PrP(C). However, until recently, all efforts to reproduce this process in vitro had failed, suggesting that host factors are necessary for prion replication. In this review we discuss recent findings such as the cellular factors that might be involved in the conformational conversion of prion proteins and the potential mechanisms by which they could operate.
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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.