ArticleFrontiers in microbiology2018
Discovering Putative Prion-Like Proteins in
Article in Frontiers in microbiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
What it found
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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
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Who cites it
34 citing papers in PubMed, 55 citations in OpenAlex.
- A New Soaking Protocol to Live StainbioRxiv : the preprint server for biology · 2026Article
- Targeting protein-protein interactions in Plasmodium: from asexual replication to sexual development.Parasites & vectors · 2026Review
- Exogenous prion-like proteins and their potential to trigger cognitive dysfunction.Molecular systems biology · 2025Article
- Biochemistry of Heat Shock Proteins From Human Intracellular Protozoan Parasites as Diagnostic and Therapeutic Biomarkers.Biochemistry · 2025Review
- Extracellular Vesicle Abundance, but Not a High Aggregation-Prone Peptide Cargo, Is Associated with Dihydroartemisinin Exposure inInternational journal of molecular sciences · 2025Article
- YAT2150 is irresistible in Plasmodium falciparum and active against Plasmodium vivax and Leishmania clinical isolates.Scientific reports · 2025Article
- Overexpression inFrontiers in cellular and infection microbiology · 2025Article
- Leveraging the Aggregated Protein Dye YAT2150 for Malaria Chemotherapy.Pharmaceutics · 2024Article
- Swapping the linkers of canonical Hsp70 and Hsp110 chaperones compromises both self-association and client selection.Heliyon · 2024Article
- Effect of the aggregated protein dye YAT2150 onAntimicrobial agents and chemotherapy · 2024Article
- Molecular Descriptors Property Prediction Using Transformer-Based Approach.International journal of molecular sciences · 2023Article
- The protein aggregation inhibitor YAT2150 has potent antimalarial activity in Plasmodium falciparum in vitro cultures.BMC biology · 2022Article
- Inhibition ofFrontiers in molecular biosciences · 2022Article
- Review
- Exploring cryptic amyloidogenic regions in prion-like proteins from plants.Frontiers in plant science · 2022Article
- Inhibitors of theCells · 2021Review
- Prion-like proteins: from computational approaches to proteome-wide analysis.FEBS open bio · 2021Review
- Mutation of GGMP Repeat Segments ofInternational journal of molecular sciences · 2021Article
- Heat Shock Proteins as Targets for Novel Antimalarial Drug Discovery.Advances in experimental medicine and biology · 2021Article
- Bioprospecting for Novel Heat Shock Protein Modulators: The New Frontier for Antimalarial Drug Discovery?Advances in experimental medicine and biology · 2021Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Prions are a singular subset of proteins able to switch between a soluble conformation and a self-perpetuating amyloid state. Traditionally associated with neurodegenerative diseases, increasing evidence indicates that organisms exploit prion-like mechanisms for beneficial purposes. The ability to transit between conformations is encoded in the so-called prion domains, long disordered regions usually enriched in glutamine/asparagine residues. Interestingly,
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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.