ReviewAmerican journal of neurodegenerative disease2013
Therapies for human prion diseases.
Review in American journal of neurodegenerative disease, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 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
18 citing papers in PubMed, 32 citations in OpenAlex.
- Treatment with pentosan polysulphate in patients with MPS I: results from an open label, randomized, monocentric phase II study.Journal of inherited metabolic disease · 2016Trial
- Delayed progression of prion disease in mice by polyarginine-facilitated prevention of PrPNeurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2025Article
- Screening of Anti-Prion Compounds Using the Protein Misfolding Cyclic Amplification Technology.Biomolecules · 2024Article
- Recent developments in intranasal drug delivery of nanomedicines for the treatment of neuropsychiatric disorders.Frontiers in medicine · 2024Review
- Human prion diseases and the prion protein - what is the current state of knowledge?Translational neuroscience · 2023Review
- The Effect ofInternational journal of molecular sciences · 2022Article
- Elucidating Critical Proteinopathic Mechanisms and Potential Drug Targets in Neurodegeneration.Cellular and molecular neurobiology · 2020Review
- BMD42-2910, a Novel Benzoxazole Derivative, Shows a Potent Anti-prion Activity and Prolongs the Mean Survival in an Animal Model of Prion Disease.Experimental neurobiology · 2020Article
- Neurotheranostics as personalized medicines.Advanced drug delivery reviews · 2019Review
- Pentosan Polysulfate Treatment of Mucopolysaccharidosis Type IIIA Mice.JIMD reports · 2019Article
- High Dose and Delayed Treatment with Bile Acids Ineffective in RML Prion-Infected Mice.Antimicrobial agents and chemotherapy · 2018Article
- Review
- Article
- Neuroradiology of human prion diseases, diagnosis and differential diagnosis.La Radiologia medica · 2017Review
- The 37/67 kDa laminin receptor (LR) inhibitor, NSC47924, affects 37/67 kDa LR cell surface localization and interaction with the cellular prion protein.Scientific reports · 2016Article
- Prion diseases: immunotargets and therapy.ImmunoTargets and therapy · 2016Review
- Transgenic over-expression of mammalian heparanase delays prion disease onset and progression.Biochemical and biophysical research communications · 2015Article
- Analysis of the advantage features of Beijing surveillance network for Creutzfeldt-Jakob disease.Prion · 2015Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The pathological foundation of human prion diseases is a result of the conversion of the physiological form of prion protein (PrP(c)) to the pathological protease resistance form PrP(res). Most patients with prion disease have unknown reasons for this conversion and the subsequent development of a devastating neurodegenerative disorder. The conversion of PrP(c) to PrP(res), with resultant propagation and accumulation results in neuronal death and amyloidogenesis. However, with increasing understanding of neurodegenerative processes it appears that protein-misfolding and subsequent propagation of these rouge proteins, is a generic phenomenon shared with diseases caused by tau, α-synucleins and β-amyloid proteins. Consequently, effective anti-prion agents may have wider implications. A number of therapeutic approaches include polyanionic, polycyclic drugs such as pentosan polysulfate (PPS), which prevent the conversion of PrP(c) to PrP(res) and might also sequester and down-regulate PrP(res). Polyanionic compounds might also help to clear PrP(res). Treatments aimed at the laminin receptor, which is an important accessory molecule in the conversion of PrP(c) to PrP(res) - neuroprotection, immunotherapy, siRNA and antisense approaches have provided some experimental promise.
Indexed as
Identifiers
24093082PMC3783831W84392511What 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.