ReviewNature reviews. Neurology2013
Immunotherapy in prion disease.
Review in Nature reviews. Neurology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 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
21 citing papers in PubMed, 43 citations in OpenAlex.
- Prion protein E219K polymorphism: from the discovery of the KANNO blood group to interventions for human prion disease.Frontiers in neurology · 2024Review
- Immunization with Genetically Modified Trypanosomes Provides Protection against Transmissible Spongiform Encephalopathies.International journal of molecular sciences · 2022Article
- Rapidly progressive dementias - aetiologies, diagnosis and management.Nature reviews. Neurology · 2022Review
- Article
- Understanding Creutzfeldt-Jackob disease from a viewpoint of amyloidogenic evolvability.Prion · 2020Review
- Immunotherapy against Prion Disease.Pathogens (Basel, Switzerland) · 2020Review
- Prion-Like Propagation of Post-Translationally Modified Tau in Alzheimer's Disease: A Hypothesis.Journal of molecular neuroscience : MN · 2018Review
- Extending the functional characteristics of naturally occurring autoantibodies against β-Amyloid, Prion Protein and α-Synuclein.PloS one · 2018Article
- How do PrPPathogens (Basel, Switzerland) · 2017Review
- Insights from Therapeutic Studies for PrP Prion Disease.Cold Spring Harbor perspectives in medicine · 2017Review
- Recombinant Antibody Fragments for Neurodegenerative Diseases.Current neuropharmacology · 2017Review
- Combined immunotherapy with "anti-insulin resistance" therapy as a novel therapeutic strategy against neurodegenerative diseases.NPJ Parkinson's disease · 2017Article
- Prion protein-specific antibodies-development, modes of action and therapeutics application.Viruses · 2014Review
- Peripheral administration of a humanized anti-PrP antibody blocks Alzheimer's disease Aβ synaptotoxicity.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014Article
- Prion protein-specific antibodies that detect multiple TSE agents with high sensitivity.PloS one · 2014Article
- The immunobiology of prion diseases.Nature reviews. Immunology · 2013Review
- Single-chain fragment variable passive immunotherapies for neurodegenerative diseases.International journal of molecular sciences · 2013Review
- Prion peptide uptake in microglial cells--the effect of naturally occurring autoantibodies against prion protein.PloS one · 2013Article
- Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transmissible spongiform encephalopathies (TSEs), also known as prion diseases, describe a group of fatal neurodegenerative disorders affecting both humans and animals. Accumulation of misfolded prion proteins is the pathological hallmark of these disorders; such accumulation occurs in lymphoreticular tissue prior to CNS involvement in scrapie, experimental models and human variant Creutzfeldt-Jakob disease. Lymphoreticular accumulation of misfolded prion protein has not been demonstrated in human sporadic or genetic forms of TSE. Once clinical symptoms develop, all prion disorders have a rapidly progressive and lethal course, and no effective therapy exists. In the past 10 years, antibody-based immunotherapy has been considered for other neurodegenerative disorders associated with protein misfolding and, therefore, might also be an effective approach to prevention or treatment of prion disease. Self-tolerance to endogenous prion protein is, however, a major challenge to the development of effective immunotherapy, as is the risk of adverse effects from active immunization. This Review summarizes the evidence that immunization could slow disease progression or increase lifespan in animal models of prion diseases. The therapeutic potential of these strategies in treating patients with prion diseases is also discussed.
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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.