ArticlePLoS pathogens2011
Down-regulation of Shadoo in prion infections traces a pre-clinical event inversely related to PrP(Sc) accumulation.
Article in PLoS pathogens, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
26 citing papers in PubMed, 41 citations in OpenAlex.
- The First Genetic Characterization of theAnimals : an open access journal from MDPI · 2024Article
- Membrane Domain Localization and Interaction of the Prion-Family Proteins, Prion and Shadoo with Calnexin.Membranes · 2021Article
- Mice Treated Subcutaneously with Mouse LPS-Converted PrPVeterinary sciences · 2021Article
- Quaternary Structure Changes for PrPMolecular neurobiology · 2021Article
- RNA as the stone guest of protein aggregation.Nucleic acids research · 2020Review
- Proteasomal Inhibition Redirects the PrP-Like Shadoo Protein to the Nucleus.Molecular neurobiology · 2019Article
- Regulation of sub-compartmental targeting and folding properties of the Prion-like protein Shadoo.Scientific reports · 2017Article
- Purification and Refolding to Amyloid Fibrils of (His)6-tagged Recombinant Shadoo Protein Expressed as Inclusion Bodies in E. coli.Journal of visualized experiments : JoVE · 2015Article
- Prion Infectivity Plateaus and Conversion to Symptomatic Disease Originate from Falling Precursor Levels and Increased Levels of Oligomeric PrPSc Species.Journal of virology · 2015Article
- Interaction between Shadoo and PrP Affects the PrP-Folding Pathway.Journal of virology · 2015Article
- Article
- Progress on low susceptibility mechanisms of transmissible spongiform encephalopathies.Dong wu xue yan jiu = Zoological research · 2014Review
- Negative purifying selection drives prion and doppel protein evolution.Journal of molecular evolution · 2014Article
- Disruption of glycosylation enhances ubiquitin-mediated proteasomal degradation of Shadoo in Scrapie-infected rodents and cultured cells.Molecular neurobiology · 2014Article
- Prion disease tempo determined by host-dependent substrate reduction.The Journal of clinical investigation · 2014Article
- Prion protein (PrP) gene-knockout cell lines: insight into functions of the PrP.Frontiers in cell and developmental biology · 2014Review
- Unchanged survival rates of Shadoo knockout mice after infection with mouse-adapted scrapie.Prion · 2014Article
- LIV-1 ZIP ectodomain shedding in prion-infected mice resembles cellular response to transition metal starvation.Journal of molecular biology · 2012Article
- Knockout of the prion protein (PrP)-like Sprn gene does not produce embryonic lethality in combination with PrP(C)-deficiency.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Advances in biotechnology and linking outputs to variation in complex traits: Plant and Animal Genome meeting January 2012.Functional & integrative genomics · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
18 authors at 6 institutions in 3 countries.
Funding
Abstract
During prion infections of the central nervous system (CNS) the cellular prion protein, PrP(C), is templated to a conformationally distinct form, PrP(Sc). Recent studies have demonstrated that the Sprn gene encodes a GPI-linked glycoprotein Shadoo (Sho), which localizes to a similar membrane environment as PrP(C) and is reduced in the brains of rodents with terminal prion disease. Here, analyses of prion-infected mice revealed that down-regulation of Sho protein was not related to Sprn mRNA abundance at any stage in prion infection. Down-regulation was robust upon propagation of a variety of prion strains in Prnp(a) and Prnp(b) mice, with the exception of the mouse-adapted BSE strain 301 V. In addition, Sho encoded by a TgSprn transgene was down-regulated to the same extent as endogenous Sho. Reduced Sho levels were not seen in a tauopathy, in chemically induced spongiform degeneration or in transgenic mice expressing the extracellular ADan amyloid peptide of familial Danish dementia. Insofar as prion-infected Prnp hemizygous mice exhibited accumulation of PrP(Sc) and down-regulation of Sho hundreds of days prior to onset of neurologic symptoms, Sho depletion can be excluded as an important trigger for clinical disease or as a simple consequence of neuronal damage. These studies instead define a disease-specific effect, and we hypothesize that membrane-associated Sho comprises a bystander substrate for processes degrading PrP(Sc). Thus, while protease-resistant PrP detected by in vitro digestion allows post mortem diagnosis, decreased levels of endogenous Sho may trace an early response to PrP(Sc) accumulation that operates in the CNS in vivo. This cellular response may offer new insights into the homeostatic mechanisms involved in detection and clearance of the misfolded proteins that drive prion disease pathogenesis.
Indexed as
Identifiers
What OpenQuestion holds
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.