ReviewNature neuroscience2018
Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases.
Review in Nature neuroscience, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 577 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
577 citing papers in PubMed, 1,111 citations in OpenAlex.
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- Oxidative stress and inflammation in neurodegenerative disorders.Archives of toxicology · 2026Review
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- Somatic mosaicism in the brain: linking development, ageing and neurodegeneration.Nature reviews. Neurology · 2026Review
- Metal-organic macrocycles as molecular modulators of amyloid-β aggregation and cytotoxicity.Chemical science · 2026Article
- Lipid-conjugated Ru(iii) complexes as inhibitors of pathological peptide aggregation in neurodegenerative disorders.RSC medicinal chemistry · 2026Article
- Clinical innovations and future directions of nanoparticles in the treatment of psychiatric and neurological disorders.Molecular psychiatry · 2026Review
- Combating ageing beyond the cell: Emerging roles of extracellular proteostasis.The FEBS journal · 2026Review
- Neuroproteasomes regulate endogenous tau paired helical filament formation in an APOE genotype- and age-dependent manner.Nature neuroscience · 2026Article
- Article
- PROTAC-Based Strategies in Neurodegenerative Diseases: Challenges and Perspectives.Pharmaceuticals (Basel, Switzerland) · 2026Review
- JP1 peptide modulates oxidative stress and autophagy via Keap1-Nrf2-ARE in ALS model mice.BMC medicine · 2026Article
- Liquid-liquid phase-separated tau colocalizes with and stabilizes Aβ oligomers.Communications chemistry · 2026Article
- Fluoride exposure induces oxidative damage in primary astrocytes of SD rats and changes in the expression of α-synuclein and its effect on Nrf2-NQO1/HO-1 signaling pathway.Journal of bioenergetics and biomembranes · 2026Article
- Amelioration of behavioral and neural deficits in animal models of neurodegenerative disease by nanoformulations of curcumin and quercetin.Neural regeneration research · 2026Article
- Metallothionein and neurodegenerative diseases.Neural regeneration research · 2026Article
- Active Vaccination Strategies for Alzheimer's Disease: An Expanded Review.European journal of immunology · 2026Review
- Review
517 more citing papers are in PubMed but not listed here.
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
Abstract
A hallmark event in neurodegenerative diseases (NDs) is the misfolding, aggregation, and accumulation of proteins, leading to cellular dysfunction, loss of synaptic connections, and brain damage. Despite the involvement of distinct proteins in different NDs, the process of protein misfolding and aggregation is remarkably similar. A recent breakthrough in the field was the discovery that misfolded protein aggregates can self-propagate through seeding and spread the pathological abnormalities between cells and tissues in a manner akin to the behavior of infectious prions in prion diseases. This discovery has vast implications for understanding the mechanisms involved in the initiation and progression of NDs, as well as for the design of novel strategies for treatment and diagnosis. In this Review, we provide a critical discussion of the role of protein misfolding and aggregation in NDs. Commonalities and differences between distinct protein aggregates will be highlighted, in addition to evidence supporting the hypothesis that misfolded aggregates can be transmissible by the prion principle. We will also describe the molecular basis and implications for prion-like conformational strains, cross-interaction between different misfolded proteins in the brain, and how these concepts can be applied to the development of novel strategies for therapy and diagnosis.
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What 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.