ReviewBiochemistry2009
Prion diseases and their biochemical mechanisms.
Review in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 92 papers, 1 of them a synthesis that pooled it.
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
92 citing papers in PubMed, 1 synthesis or guideline pooled it, 209 citations in OpenAlex.
- The first meta-analysis of the G96S single nucleotide polymorphism (SNP) of the prion protein gene (Frontiers in veterinary science · 2024Pooled it
- Bovine Spongiform Encephalopathy: An Integrated Review of Prion Mechanisms, Neuroanatomy, and Control.Veterinary sciences · 2026Review
- First report of novel single nucleotide polymorphisms (SNPs) and genetic characteristics of the prion-like protein gene (Frontiers in veterinary science · 2026Article
- Protein misfolding: understanding biology to classify and treat synucleinopathies.Journal of neural transmission (Vienna, Austria : 1996) · 2025Review
- The structure of complexes between zinc(ii) cations and histidine-rich repeats from the unstructured N-terminal domain of human prion protein.RSC advances · 2025Review
- 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
- Beyond Misfolding: A New Paradigm for the Relationship Between Protein Folding and Aggregation.International journal of molecular sciences · 2024Review
- A microfluidic biosensor for the diagnosis of chronic wasting disease.Microsystems & nanoengineering · 2023Article
- Probing the origin of prion protein misfolding via reconstruction of ancestral proteins.Protein science : a publication of the Protein Society · 2022Article
- Cryo-EM structure of disease-related prion fibrils provides insights into seeding barriers.Nature structural & molecular biology · 2022Article
- Populations of Tau Conformers Drive Prion-like Strain Effects in Alzheimer's Disease and Related Dementias.Cells · 2022Review
- Chiral carbon dots: synthesis, optical properties, and emerging applications.Light, science & applications · 2022Review
- Phenotypic Heterogeneity of Variably Protease-Sensitive Prionopathy: A Report of Three Cases Carrying Different Genotypes atViruses · 2022Article
- Distinct populations of highly potent TAU seed conformers in rapidly progressing Alzheimer's disease.Science translational medicine · 2022Article
- Tissue Engineering and Photodynamic Therapy: A New Frontier of Science for Clinical Application -An Up-To-Date Review.Frontiers in bioengineering and biotechnology · 2022Review
- The prion-like transmission of tau oligomersFrontiers in aging neuroscience · 2022Review
- Nanopore Technology for the Application of Protein Detection.Nanomaterials (Basel, Switzerland) · 2021Review
- Structurally distinct external solvent-exposed domains drive replication of major human prions.PLoS pathogens · 2021Article
- Non-Oncologic Applications of Nanomedicine-Based Phototherapy.Biomedicines · 2021Review
- Understanding and exploiting interactions between cellular proteostasis pathways and infectious prion proteins for therapeutic benefit.Open biology · 2020Article
32 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
Prion diseases, also known as the transmissible spongiform encephalopathies (TSEs), are a group of fatal neurodegenerative disorders that affect humans and animals. These diseases are intimately associated with conformational conversion of the cellular prion protein, PrP(C), into an oligomeric beta-sheet-rich form, PrP(Sc). A growing number of observations support the once heretical hypothesis that transmission of TSE diseases does not require nucleic acids and that PrP(Sc) alone can act as an infectious agent. The view that misfolded proteins can be infectious is also supported by recent findings regarding prion phenomena in yeast and other fungi. One of the most intriguing facets of prions is their ability to form different strains, leading to distinct phenotypes of TSE diseases. Within the context of the "protein-only" model, prion strains are believed to be encoded in distinct conformations of misfolded prion protein aggregates. In this review, we describe recent advances in biochemical aspects of prion research, with a special focus on the mechanism of conversion of prion protein to the pathogenic form(s), the emerging structural knowledge of fungal and mammalian prions, and our rapidly growing understanding of the molecular basis of prion strains and their relation to barriers of interspecies transmissibility.
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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.