ReviewPrion
Tracking protein aggregate interactions.
Review in Prion. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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
4 citing papers in PubMed, 4 citations in OpenAlex.
- The applications of nanozymes in neurological diseases: From mechanism to design.Theranostics · 2023Review
- Molecular Factors Mediating Neural Cell Plasticity Changes in Dementia Brain Diseases.Neural plasticity · 2021Review
- Foundations for a Realism-Based Ontology of Protein Aggregates.CEUR workshop proceedings · 2020Article
- Effect of charged residues in the N-domain of Sup35 protein on prion [PSI+] stability and propagation.The Journal of biological chemistry · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 3 institutions in 2 countries.
Funding
Abstract
Amyloid fibrils share a structural motif consisting of highly ordered β-sheets aligned perpendicular to the fibril axis ( 1, 2) . At each fibril end, β-sheets provide a template for recruiting and converting monomers ( 3) . Various amyloid fibrils often occur in the same individual, yet whether distinct protein aggregates aid or inhibit the assembly of heterologous proteins is unclear. In prion disease, different amyloid-like prion aggregate structures, or strains, are thought to be the basis of disparate disease phenotypes in the same species expressing identical prion protein sequences ( 4-7) . Here we focus on the interactions reported to occur when two pre-existing amyloids or two distinct prion strains occur together in the central nervous system.
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.