ArticleBMC bioinformatics2019
AMYCO: evaluation of mutational impact on prion-like proteins aggregation propensity.
Article in BMC bioinformatics, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 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
24 citing papers in PubMed, 35 citations in OpenAlex.
- Assessment of Aggregation- and Condensation-Prone Regions of Proteins Involved in Neurodegenerative, Neurological and Mental-State Diseases.Biomolecules · 2026Article
- First report of novel single nucleotide polymorphisms (SNPs) and genetic characteristics of the prion-like protein gene (Frontiers in veterinary science · 2026Article
- Novel polymorphisms and functional characterization of the prion protein gene in sparrows (Frontiers in veterinary science · 2026Article
- Clinical phenotype associated with A118V mutation of PRPN gene.Journal of neurology · 2025Article
- Mapping PRNP Polymorphisms in Portuguese Serra da Estrela Ovine Populations: Insights into Scrapie Susceptibility and Farm Animal Improvement.Animals : an open access journal from MDPI · 2025Article
- Identification of the Highly Polymorphic Prion Protein Gene (Animals : an open access journal from MDPI · 2025Article
- Novel Single-Nucleotide Polymorphisms (SNPs) and Genetic Studies of the Shadow of Prion Protein (Animals : an open access journal from MDPI · 2024Article
- Novel polymorphisms and genetic studies of the shadow of prion protein gene (Frontiers in veterinary science · 2024Article
- Article
- Novel polymorphisms in the prion protein gene (PRNP) and stability of the resultant prion protein in different horse breeds.Veterinary research · 2023Article
- First report of a novel polymorphism and genetic characteristics of the leporine prion protein (Frontiers in veterinary science · 2023Article
- In-Silico Analysis of pH-Dependent Liquid-Liquid Phase Separation in Intrinsically Disordered Proteins.Biomolecules · 2022Article
- Novel Single Nucleotide Polymorphisms (SNPs) and Genetic Features of the Prion Protein Gene (Frontiers in veterinary science · 2022Article
- Novel Polymorphisms and Genetic Characteristics of the Prion Protein Gene in Pheasants.Frontiers in veterinary science · 2022Article
- Prion-like proteins: from computational approaches to proteome-wide analysis.FEBS open bio · 2021Review
- SGnn: A Web Server for the Prediction of Prion-Like Domains Recruitment to Stress Granules Upon Heat Stress.Frontiers in molecular biosciences · 2021Article
- Article
- Novel Polymorphisms and Genetic Characteristics of the Prion Protein Gene (International journal of molecular sciences · 2020Article
- Composition-based prediction and rational manipulation of prion-like domain recruitment to stress granules.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Using protein engineering to understand and modulate aggregation.Current opinion in structural biology · 2020Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
backgroundAround 1% of human proteins are predicted to contain a disordered and low complexity prion-like domain (PrLD). Mutations in PrLDs have been shown promote a transition towards an aggregation-prone state in several diseases.
resultsRecently, we have shown that an algorithm that considers the effects of mutations on PrLDs composition, as well as on localized amyloid propensity can predict the impact of these amino acid changes on protein intracellular aggregation. In this application note, we implement this concept into the AMYCO web server, a refined algorithm that forecasts the influence of amino acid changes in prion-like proteins aggregation propensity better than state-of-the-art predictors.
conclusionsThe AMYCO web server allows for a fast and automated evaluation of the effect of mutations on the aggregation properties of prion-like proteins. This might uncover novel disease-linked amino acid changes in the sequences of human prion-like proteins. Additionally, it can find application in the in silico design of synthetic prion-like proteins with tuned aggregation propensities for different purposes. AMYCO does not require previous registration and is freely available to all users at: http://bioinf.uab.cat/amyco/ .
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.