ArticleThe EMBO journal2001
Sulfated glycans and elevated temperature stimulate PrP(Sc)-dependent cell-free formation of protease-resistant prion protein.
Article in The EMBO journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers.
What it found
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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.
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Who cites it
91 citing papers in PubMed, 233 citations in OpenAlex.
- Prions and protein aggregates as pathogens, self-propagating structures, biomarkers, and therapeutic targets.Microbiology and molecular biology reviews : MMBR · 2025Review
- Spontaneous generation of diverse recombinant prion strains: sulfated glycan cofactors facilitate strain emergence but do not determine specific strain properties.Acta neuropathologica communications · 2025Article
- A charged tail on anti-α-Synuclein antibodies does not enhance their affinity to α-Synuclein fibrils.PloS one · 2024Article
- Understanding the key features of the spontaneous formation of bona fide prions through a novel methodology that enables their swift and consistent generation.Acta neuropathologica communications · 2023Article
- Neuronal Ndst1 depletion accelerates prion protein clearance and slows neurodegeneration in prion infection.PLoS pathogens · 2023Article
- Phospholipid cofactor solubilization inhibits formation of native prions.Journal of neurochemistry · 2023Article
- Cell biology of prion strains in vivo and in vitro.Cell and tissue research · 2023Review
- Prion therapeutics: Lessons from the past.Prion · 2022Review
- Cryo-EM of prion strains from the same genotype of host identifies conformational determinants.PLoS pathogens · 2022Article
- Review
- Review
- Interaction of Prion Peptides with DNA Structures.ACS omega · 2022Article
- The G127V variant of the prion protein interferes with dimer formation in vitro but not in cellulo.Scientific reports · 2021Article
- Enzymatic degradation of RNA causes widespread protein aggregation in cell and tissue lysates.EMBO reports · 2020Article
- The Role of Vesicle Trafficking Defects in the Pathogenesis of Prion and Prion-Like Disorders.International journal of molecular sciences · 2020Review
- Prion protein post-translational modifications modulate heparan sulfate binding and limit aggregate size in prion disease.Neurobiology of disease · 2020Article
- Prion protein glycans reduce intracerebral fibril formation and spongiosis in prion disease.The Journal of clinical investigation · 2020Article
- Shortening heparan sulfate chains prolongs survival and reduces parenchymal plaques in prion disease caused by mobile, ADAM10-cleaved prions.Acta neuropathologica · 2020Article
- Cofactor molecules: Essential partners for infectious prions.Progress in molecular biology and translational science · 2020Review
- Article
31 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
A conformational conversion of the normal, protease- sensitive prion protein (PrP-sen or PrP(C)) to a protease-resistant form (PrP-res or PrP(Sc)) is commonly thought to be required in transmissible spongiform encephalopathies (TSEs). Endogenous sulfated glycosaminoglycans are associated with PrP-res deposits in vivo, suggesting that they may facilitate PrP-res formation. On the other hand, certain exogenous sulfated glycans can profoundly inhibit PrP-res accumulation and serve as prophylactic anti-TSE compounds in vivo. To investigate the seemingly paradoxical effects of sulfated glycans on PrP-res formation, we have assayed their direct effects on PrP conversion under physiologically compatible cell-free conditions. Heparan sulfate and pentosan polysulfate stimulated PrP-res formation. Conversion was stimulated further by increased temperature. Both elevated temperature and pentosan polysulfate promoted interspecies PrP conversion. Circular dichroism spectropolarimetry measurements showed that pentosan polysulfate induced a conformational change in PrP-sen that may potentiate its PrP-res-induced conversion. These results show that certain sulfated glycosaminoglycans can directly affect the PrP conversion reaction. Therefore, depending upon the circumstances, sulfated glycans may be either cofactors or inhibitors of this apparently pathogenic process.
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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.