ReviewThe Journal of biological chemistry2016
The "Jekyll and Hyde" Actions of Nucleic Acids on the Prion-like Aggregation of Proteins.
Review in The Journal of biological chemistry, 2016. 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
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
34 citing papers in PubMed, 72 citations in OpenAlex.
- Molecular recognition and structural plasticity in amyloid-nucleic acid complexes.Journal of structural biology · 2025Review
- Intermolecular energy migration via homoFRET captures the modulation in the material property of phase-separated biomolecular condensates.Nature communications · 2024Article
- Oncogenic p53 triggers amyloid aggregation of p63 and p73 liquid droplets.Communications chemistry · 2024Article
- In silico analysis of fungal prion-like proteins for elucidating their role in plant-fungi interactions.Archives of microbiology · 2024Article
- Roles of Nucleic Acids in Protein Folding, Aggregation, and Disease.ACS chemical biology · 2024Review
- The ALS/FTD-related C9orf72 hexanucleotide repeat expansion forms RNA condensates through multimolecular G-quadruplexes.Nature communications · 2023Article
- Differential interactome mapping of aggregation prone/prion-like proteins under stress: novel links to stress granule biology.Cell & bioscience · 2023Article
- (Dys)functional insights into nucleic acids and RNA-binding proteins modulation of the prion protein and α-synuclein phase separation.Biophysical reviews · 2023Review
- Biophysics of biomolecular condensates.Biophysical journal · 2023Article
- Heterotypic electrostatic interactions control complex phase separation of tau and prion into multiphasic condensates and co-aggregates.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Enterovirus infection and its relationship with neurodegenerative diseases.Memorias do Instituto Oswaldo Cruz · 2023Article
- Single-droplet surface-enhanced Raman scattering decodes the molecular determinants of liquid-liquid phase separation.Nature communications · 2022Article
- Supersaturation-Dependent Formation of Amyloid Fibrils.Molecules (Basel, Switzerland) · 2022Review
- Spatiotemporal modulations in heterotypic condensates of prion and α-synuclein control phase transitions and amyloid conversion.Nature communications · 2022Article
- Protein of a thousand faces: The tumor-suppressive and oncogenic responses of p53.Frontiers in molecular biosciences · 2022Review
- Phase separation of p53 precedes aggregation and is affected by oncogenic mutations and ligands.Chemical science · 2021Article
- Complex Networks of Prion-Like Proteins Reveal Cross Talk Between Stress and Memory Pathways in Plants.Frontiers in plant science · 2021Article
- Rabbit PrP Is Partially Resistant toFrontiers in neuroscience · 2021Article
- Tau and DNA Damage in Neurodegeneration.Brain sciences · 2020Review
- RNA as the stone guest of protein aggregation.Nucleic acids research · 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
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein misfolding results in devastating degenerative diseases and cancer. Among the culprits involved in these illnesses are prions and prion-like proteins, which can propagate by converting normal proteins to the wrong conformation. For spongiform encephalopathies, a real prion can be transmitted among individuals. In other disorders, the bona fide prion characteristics are still under investigation. Besides inducing misfolding of native proteins, prions bind nucleic acids and other polyanions. Here, we discuss how nucleic acid binding might influence protein misfolding for both disease-related and benign, functional prions and why the line between bad and good amyloids might be more subtle than previously thought.
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.