ReviewPrion2015
Amyloids or prions? That is the question.
Review in Prion, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 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
28 citing papers in PubMed.
- Cellular Prion Protein and Amyloid-β Oligomers in Alzheimer's Disease-Are There Connections?International journal of molecular sciences · 2025Review
- Evidence Suggesting That Alzheimer's Disease May Be a Transmissible Disorder.International journal of molecular sciences · 2025Article
- Realization of Amyloid-like Aggregation as a Common Cause for Pathogenesis in Diseases.Life (Basel, Switzerland) · 2023Review
- Concentration and time-dependent amyloidogenic characteristics of intrinsically disordered N-terminal region ofFrontiers in microbiology · 2023Article
- Excessive replacement changes drive evolution of global sheep prion protein (PRNP) sequences.Heredity · 2022Article
- Exploring cryptic amyloidogenic regions in prion-like proteins from plants.Frontiers in plant science · 2022Article
- Prion-like proteins: from computational approaches to proteome-wide analysis.FEBS open bio · 2021Review
- Hydration of Simple Model Peptides in Aqueous Osmolyte Solutions.International journal of molecular sciences · 2021Article
- The Hunt for Ancient Prions: Archaeal Prion-Like Domains Form Amyloid-Based Epigenetic Elements.Molecular biology and evolution · 2021Article
- Assessment of Amyloid Forming Tendency of Peptide Sequences from Amyloid Beta and Tau Proteins Using Force-Field, Semi-Empirical, and Density Functional Theory Calculations.International journal of molecular sciences · 2021Article
- Structures of Pathological and Functional Amyloids and Prions, a Solid-State NMR Perspective.Frontiers in molecular neuroscience · 2021Review
- Review
- Prions: Roles in Development and Adaptive Evolution.Journal of molecular evolution · 2020Review
- Novel Variations in Native Ethiopian Goat breeds PRNP Gene and Their Potential Effect on Prion Protein Stability.Scientific reports · 2020Article
- Entropic Bristles Tune the Seeding Efficiency of Prion-Nucleating Fragments.Cell reports · 2020Article
- Effect of Single Amino Acid Substitutions by Asn and Gln on Aggregation Properties of Bence-Jones Protein BIF.International journal of molecular sciences · 2019Article
- Cellular stress leads to the formation of membraneless stress assemblies in eukaryotic cells.Traffic (Copenhagen, Denmark) · 2019Review
- Article
- The Disordered C-Terminus of Yeast Hsf1 Contains a Cryptic Low-Complexity Amyloidogenic Region.International journal of molecular sciences · 2018Article
- Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Despite major efforts devoted to understanding the phenomenon of prion transmissibility, it is still poorly understood how this property is encoded in the amino acid sequence. In recent years, experimental data on yeast prion domains allow to start at least partially decrypting the sequence requirements of prion formation. These experiments illustrate the need for intrinsically disordered sequence regions enriched with a particularly high proportion of glutamine and asparagine. Bioinformatic analysis suggests that these regions strike a balance between sufficient amyloid nucleation propensity on the one hand and disorder on the other, which ensures availability of the amyloid prone regions but entropically prevents unwanted nucleation and facilitates brittleness required for propagation.
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.