ArticleThe Journal of biological chemistry2010
Low density subcellular fractions enhance disease-specific prion protein misfolding.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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Who cites it
12 citing papers in PubMed, 17 citations in OpenAlex.
- PrP aggregation can be seeded by pre-formed recombinant PrP amyloid fibrils without the replication of infectious prions.Acta neuropathologica · 2016Article
- Complex folding and misfolding effects of deer-specific amino acid substitutions in the β2-α2 loop of murine prion protein.Scientific reports · 2015Article
- The glycosylation status of PrPC is a key factor in determining transmissible spongiform encephalopathy transmission between species.Journal of virology · 2015Article
- Is tau ready for admission to the prion club?Prion · 2012Review
- Dissociation of infectivity from seeding ability in prions with alternate docking mechanism.PLoS pathogens · 2011Article
- Article
- Monoacylated cellular prion protein modifies cell membranes, inhibits cell signaling, and reduces prion formation.The Journal of biological chemistry · 2011Article
- Na+/K+-ATPase is present in scrapie-associated fibrils, modulates PrP misfolding in vitro and links PrP function and dysfunction.PloS one · 2011Article
- Defining sporadic Creutzfeldt-Jakob disease strains and their transmission properties.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Complement protein C1q forms a complex with cytotoxic prion protein oligomers.The Journal of biological chemistry · 2010Article
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- Review
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Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
Abstract
The production of prion particles in vitro by amplification with or without exogenous seed typically results in infectivity titers less than those associated with PrP(Sc) isolated ex vivo and highlights the potential role of co-factors that can catalyze disease-specific prion protein misfolding in vivo. We used a cell-free conversion assay previously shown to replicate many aspects of transmissible spongiform encephalopathy disease to investigate the cellular location of disease-specific co-factors using fractions derived from gradient centrifugation of a scrapie-susceptible cell line. Fractions from the low density region of the gradient doubled the efficiency of conversion of recombinant PrP. These fractions contain plasma membrane and cytoplasmic proteins, and conversion enhancement can be achieved using PrP(Sc) derived from two different strains of mouse-passaged scrapie as seed. Equivalent fractions from a second scrapie-susceptible cell line also stimulate conversion. We also show that subcellular fractions enhancing disease-specific prion protein conversion prevent in vitro fibrillization of recombinant prion protein, suggesting the existence of separate, competing mechanisms of disease-specific and nonspecific misfolding in vivo.
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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.