ArticleCommunicative & integrative biology2011
Pulling rabbits to reveal the secrets of the prion protein.
Article in Communicative & integrative biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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
10 citing papers in PubMed, 25 citations in OpenAlex.
- Prion Protein Codon Implicated in Resistance in Dogs Detected in Non-Domesticated Members of Mammalia.Animals : an open access journal from MDPI · 2026Article
- Different folding mechanisms in prion proteins from mammals with different disease susceptibility observed at the single-molecule level.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Rabbit PrP Is Partially Resistant toFrontiers in neuroscience · 2021Article
- Identification of a homology-independent linchpin domain controlling mouse and bank vole prion protein conversion.PLoS pathogens · 2020Article
- D159 and S167 are protective residues in the prion protein from dog and horse, two prion-resistant animals.Neurobiology of disease · 2018Article
- Article
- Drosophila models of prionopathies: insight into prion protein function, transmission, and neurotoxicity.Current opinion in genetics & development · 2017Review
- Progress on low susceptibility mechanisms of transmissible spongiform encephalopathies.Dong wu xue yan jiu = Zoological research · 2014Review
- Drosophila models of proteinopathies: the little fly that could.Current pharmaceutical design · 2012Review
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
The Prion protein (PrP) is a membrane-tethered glycoprotein that plays a central role in a unique class of neurodegenerative diseases that affect humans and other mammals. Prion diseases have genetic and sporadic origins, but their infectious nature sets them apart from other neurodegenerative disorders. According to the "protein-only" hypothesis, misfolded PrP conformers (prions) are responsible for both spongiform degeneration of the brain and disease transmissibility. Thus, understanding PrP conformational dynamics is key to developing effective therapies. Classic studies showing the different susceptibility to prion disease in mammals have recently found support in structural and transgenic studies with PrP from susceptible (mouse, hamster) and resistant (rabbit, horse, dog) animals. These studies identify key residues in PrP that determine both PrP structure and its propensity to acquire a β-structure conformation proposed to be neurotoxic.
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.