ReviewViruses2019
Transmissibility versus Pathogenicity of Self-Propagating Protein Aggregates.
Review in Viruses, 2019. 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
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
18 citing papers in PubMed, 31 citations in OpenAlex.
- Prions and protein aggregates as pathogens, self-propagating structures, biomarkers, and therapeutic targets.Microbiology and molecular biology reviews : MMBR · 2025Review
- Cryo-EM structure of a natural prion: chronic wasting disease fibrils from deer.Acta neuropathologica · 2024Article
- Sensitive detection of pathological seeds of α-synuclein, tau and prion protein on solid surfaces.PLoS pathogens · 2024Article
- Tau seeds occur before earliest Alzheimer's changes and are prevalent across neurodegenerative diseases.Acta neuropathologica · 2023Article
- A structural basis for prion strain diversity.Nature chemical biology · 2023Article
- Cryo-EM structure of disease-related prion fibrils provides insights into seeding barriers.Nature structural & molecular biology · 2022Article
- Review
- Disease-associated mutations within the yeast DNAJB6 homolog Sis1 slow conformer-specific substrate processing and can be corrected by the modulation of nucleotide exchange factors.Nature communications · 2022Article
- Structural biology of ex vivo mammalian prions.The Journal of biological chemistry · 2022Review
- Pathogenic prion structures at high resolution.PLoS pathogens · 2022Article
- Proteostasis unbalance in prion diseases: Mechanisms of neurodegeneration and therapeutic targets.Frontiers in neuroscience · 2022Review
- Neuropathology and molecular diagnosis of Synucleinopathies.Molecular neurodegeneration · 2021Review
- Is Multiple System Atrophy a Prion-like Disorder?International journal of molecular sciences · 2021Review
- Transmissible α-synuclein seeding activity in brain and stomach of patients with Parkinson's disease.Acta neuropathologica · 2021Article
- Risk of Transmissibility From Neurodegenerative Disease-Associated Proteins: Experimental Knowns and Unknowns.Journal of neuropathology and experimental neurology · 2020Review
- Defining the Protein Seeds of Neurodegeneration using Real-Time Quaking-Induced Conversion Assays.Biomolecules · 2020Review
- microRNA-Based Biomarkers in Alzheimer's Disease (AD).Frontiers in neuroscience · 2020Review
- Soluble endogenous oligomeric α-synuclein species in neurodegenerative diseases: Expression, spreading, and cross-talk.Journal of Parkinson's disease · 2020Review
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 2 institutions in 1 country.
Funding
Abstract
The prion-like spreading and accumulation of specific protein aggregates appear to be central to the pathogenesis of many human diseases, including Alzheimer's and Parkinson's. Accumulating evidence indicates that inoculation of tissue extracts from diseased individuals into suitable experimental animals can in many cases induce the aggregation of the disease-associated protein, as well as related pathological lesions. These findings, together with the history of the prion field, have raised the questions about whether such disease-associated protein aggregates are transmissible between humans by casual or iatrogenic routes, and, if so, do they propagate enough in the new host to cause disease? These practical considerations are important because real, and perhaps even only imagined, risks of human-to-human transmission of diseases such as Alzheimer's and Parkinson's may force costly changes in clinical practice that, in turn, are likely to have unintended consequences. The prion field has taught us that a single protein, PrP, can aggregate into forms that can propagate exponentially in vitro, but range from being innocuous to deadly when injected into experimental animals in ways that depend strongly on factors such as conformational subtleties, routes of inoculation, and host responses. In assessing the hazards posed by various disease-associated, self-propagating protein aggregates, it is imperative to consider both their actual transmissibilities and the pathological consequences of their propagation, if any, in recipient hosts.
Indexed as
Identifiers
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.