ReviewPrion
Prion propagation: the role of protein dynamics.
Review in Prion. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 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
12 citing papers in PubMed.
- Modelling human proteostasis and organelle homeostasis disorders in yeast and its application in drug discovery.FEMS yeast research · 2026Review
- Clearance of variant Creutzfeldt-Jakob disease prions in vivo by the Hsp70 disaggregase system.Brain : a journal of neurology · 2022Article
- The HSP110/HSP70 disaggregation system generates spreading-competent toxic α-synuclein species.The EMBO journal · 2020Article
- Initiation and Transmission of α-Synuclein Pathology in Parkinson's Disease.Neurochemical research · 2019Review
- [PIN+]ing down the mechanism of prion appearance.FEMS yeast research · 2018Review
- Overexpression of the essential Sis1 chaperone reduces TDP-43 effects on toxicity and proteolysis.PLoS genetics · 2017Article
- Prion diseases as transmissible zoonotic diseases.Osong public health and research perspectives · 2013Review
- Hsp70 targets Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation.The Journal of cell biology · 2012Article
- A size threshold limits prion transmission and establishes phenotypic diversity.Science (New York, N.Y.) · 2010Article
- Prion dynamics and the quest for the genetic determinant in protein-only inheritance.Current opinion in microbiology · 2009Review
- The NatA acetyltransferase couples Sup35 prion complexes to the [PSI+] phenotype.Molecular biology of the cell · 2009Article
- Insights into prion biology: integrating a protein misfolding pathway with its cellular environment.PrionArticle
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.
Funding
Abstract
The transfer of phenotypes from one individual to another is a fundamental aspect of biology. In addition to traditional nucleic acid-based genetic determinants, unique proteins known as prions can also act as elements of inheritance, infectivity, and disease. Nucleic acids and proteins encode genetic information in distinct ways, either in the sequence of bases in DNA or RNA or in the three dimensional structure of the polypeptide chain. Given these differences in the nature of the genetic repository, the mechanisms underlying the transmission of nucleic acid-based and protein-based phenotypes are necessarily distinct. While the appearance, persistence and transfer of nucleic acid determinants require the synthesis of new polymers, recent studies indicate that prions are propagated through dynamic transitions in the structure of existing protein.
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.