ArticlePLoS pathogens2011
Protease-resistant prions selectively decrease Shadoo protein.
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 28 papers.
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Who cites it
28 citing papers in PubMed, 45 citations in OpenAlex.
- Prion Protein Endoproteolysis: Cleavage Sites, Mechanisms and Connections to Prion Disease.Journal of neurochemistry · 2025Review
- The First Genetic Characterization of theAnimals : an open access journal from MDPI · 2024Article
- Beta-endoproteolysis of the cellular prion protein by dipeptidyl peptidase-4 and fibroblast activation protein.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Membrane Domain Localization and Interaction of the Prion-Family Proteins, Prion and Shadoo with Calnexin.Membranes · 2021Article
- Quaternary Structure Changes for PrPMolecular neurobiology · 2021Article
- Domain-specific Quantification of Prion Protein in Cerebrospinal Fluid by Targeted Mass Spectrometry.Molecular & cellular proteomics : MCP · 2019Article
- Proteasomal Inhibition Redirects the PrP-Like Shadoo Protein to the Nucleus.Molecular neurobiology · 2019Article
- Genetic resistance to transmissible spongiform encephalopathies (TSE) in goats.EFSA journal. European Food Safety Authority · 2017Article
- Regulation of sub-compartmental targeting and folding properties of the Prion-like protein Shadoo.Scientific reports · 2017Article
- Amyloid Fibrils from Hemoglobin.Biomolecules · 2017Article
- Expression of the Prion Protein Family Member Shadoo Causes Drug Hypersensitivity That Is Diminished by the Coexpression of the Wild Type Prion Protein.The Journal of biological chemistry · 2016Article
- 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
- Article
- Progress on low susceptibility mechanisms of transmissible spongiform encephalopathies.Dong wu xue yan jiu = Zoological research · 2014Review
- Disruption of glycosylation enhances ubiquitin-mediated proteasomal degradation of Shadoo in Scrapie-infected rodents and cultured cells.Molecular neurobiology · 2014Article
- Evidence that bank vole PrP is a universal acceptor for prions.PLoS pathogens · 2014Article
- Prion disease tempo determined by host-dependent substrate reduction.The Journal of clinical investigation · 2014Article
- Unchanged survival rates of Shadoo knockout mice after infection with mouse-adapted scrapie.Prion · 2014Article
- Prion protein (PrP) gene-knockout cell lines: insight into functions of the PrP.Frontiers in cell and developmental biology · 2014Review
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
The central event in prion diseases is the conformational conversion of the cellular prion protein (PrP(C)) into PrP(Sc), a partially protease-resistant and infectious conformer. However, the mechanism by which PrP(Sc) causes neuronal dysfunction remains poorly understood. Levels of Shadoo (Sho), a protein that resembles the flexibly disordered N-terminal domain of PrP(C), were found to be reduced in the brains of mice infected with the RML strain of prions [1], implying that Sho levels may reflect the presence of PrP(Sc) in the brain. To test this hypothesis, we examined levels of Sho during prion infection using a variety of experimental systems. Sho protein levels were decreased in the brains of mice, hamsters, voles, and sheep infected with different natural and experimental prion strains. Furthermore, Sho levels were decreased in the brains of prion-infected, transgenic mice overexpressing Sho and in infected neuroblastoma cells. Time-course experiments revealed that Sho levels were inversely proportional to levels of protease-resistant PrP(Sc). Membrane anchoring and the N-terminal domain of PrP both influenced the inverse relationship between Sho and PrP(Sc). Although increased Sho levels had no discernible effect on prion replication in mice, we conclude that Sho is the first non-PrP marker specific for prion disease. Additional studies using this paradigm may provide insight into the cellular pathways and systems subverted by PrP(Sc) during prion disease.
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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.