ReviewCurrent aging science2019
Oxidative and Inflammatory Events in Prion Diseases: Can They Be Therapeutic Targets?
Review in Current aging science, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
16 citing papers in PubMed, 33 citations in OpenAlex.
- Anti-Inflammatory Mechanisms of Selenium Nanosheets in Ulcerative Colitis: Protein Corona, GP130 Interaction, and Transcriptomic Profile.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Mesenchymal Stem Cell Secretome Attenuates PrPCells · 2025Article
- Adipose-Derived Mesenchymal Stem Cell Secretome Attenuates Prion Protein Peptide (106-126)-Induced Oxidative Stress via Nrf2 Activation.Stem cell reviews and reports · 2025Article
- Global, regional, and national disease burden of tobacco-related Alzheimer's disease among individuals over the age of 55: a global burden of disease study.Frontiers in public health · 2025Article
- Prion protein fragment (106-126) activates NLRP3 inflammasome and promotes platelet-monocyte/neutrophil interactions, potentially contributing to an inflammatory state.Frontiers in cell and developmental biology · 2025Article
- New Light on Prions: Putative Role of PrPInternational journal of molecular sciences · 2024Review
- Phosphorus-carrying cascade molecules: inner architecture to biomedical applications.Turkish journal of chemistry · 2023Article
- SARS-CoV-2 Invasion and Pathological Links to Prion Disease.Biomolecules · 2022Article
- PrPMolecular neurobiology · 2022Article
- Naturally Occurring Antioxidant Therapy in Alzheimer's Disease.Antioxidants (Basel, Switzerland) · 2022Review
- Melatonin: Regulation of Prion Protein Phase Separation in Cancer Multidrug Resistance.Molecules (Basel, Switzerland) · 2022Review
- The Role of Vitamins in Neurodegenerative Disease: An Update.Biomedicines · 2021Review
- microRNA-146a-5p, Neurotropic Viral Infection and Prion Disease (PrD).International journal of molecular sciences · 2021Review
- ω-3 Polyunsaturated Fatty Acids on Colonic Inflammation and Colon Cancer: Roles of Lipid-Metabolizing Enzymes Involved.Nutrients · 2020Review
- Role of Nuclear Factor Kappa B (NF-κB) Signalling in Neurodegenerative Diseases: An Mechanistic Approach.Current neuropharmacology · 2020Review
- Yeast Models for Amyloids and Prions: Environmental Modulation and Drug Discovery.Molecules (Basel, Switzerland) · 2019Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Prion diseases are a group of incurable infectious terminal neurodegenerative diseases caused by the aggregated misfolded PrPsc in selected mammals including humans. The complex physical interaction between normal prion protein PrPc and infectious PrPsc causes conformational change from the α- helix structure of PrPc to the β-sheet structure of PrPsc, and this process is repeated. Increased oxidative stress is one of the factors that facilitate the conversion of PrPc to PrPsc. This overview presents evidence to show that increased oxidative stress and inflammation are involved in the progression of this disease. Evidence is given for the participation of redoxsensitive metals Cu and Fe with PrPsc inducing oxidative stress by disturbing the homeostasis of these metals. The fact that some antioxidants block the toxicity of misfolded PrPc peptide supports the role of oxidative stress in prion disease. After exogenous infection in mice, PrPsc enters the follicular dendritic cells where PrPsc replicates before neuroinvasion where they continue to replicate and cause inflammation leading to neurodegeneration. Therefore, reducing levels of oxidative stress and inflammation may decrease the rate of the progression of this disease. It may be an important order to reduce oxidative stress and inflammation at the same time. This may be achieved by increasing the levels of antioxidant enzymes by activating the Nrf2 pathway together with simultaneous administration of dietary and endogenous antioxidants. It is proposed that a mixture of micronutrients could enable these concurrent events thereby reducing the progression of human 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.