ArticleEMBO reports2020
Enzymatic degradation of RNA causes widespread protein aggregation in cell and tissue lysates.
Article in EMBO reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 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
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
29 citing papers in PubMed, 38 citations in OpenAlex.
- Preformulated, Shelf-Stable, Dendritic Cell-Targeting Nanogel mRNA Vaccine Delivery Platform.Bioconjugate chemistry · 2026Article
- Aβ Aggregates Bind the U1 Spliceosomal Ribonucleoprotein in Alzheimer Disease Brain.bioRxiv : the preprint server for biology · 2026Article
- Condensatopathies as a mechanistic framework for disease and integrated theranostic intervention.Theranostics · 2026Review
- Catalyzing Protein Folding by Chaperones.Biology · 2025Review
- DNA binding and mitotic phosphorylation protect polyglutamine proteins from assembly formation.Cell · 2025Article
- The role of RNA structural motifs in RNA-lipid raft interaction.Scientific reports · 2025Article
- SUMO2/3 conjugation of TDP-43 protects against aggregation.Science advances · 2025Article
- Single-molecule diffusivity quantification inProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Synchronized motion of interface residues for evaluating protein-RNA complex binding affinity: Application to aptamer-mediated inhibition of TDP-43 aggregates.Protein science : a publication of the Protein Society · 2024Article
- Article
- RNA-driven phase transitions in biomolecular condensates.Molecular cell · 2024Review
- 1-L Transcription in Prion Diseases.International journal of molecular sciences · 2024Article
- Roles of Nucleic Acids in Protein Folding, Aggregation, and Disease.ACS chemical biology · 2024Review
- RNA-dependent proteome solubility maintenance inRNA biology · 2024Article
- Let's make it clear: systematic exploration of mitochondrial DNA- and RNA-protein complexes by complexome profiling.Nucleic acids research · 2023Article
- Nondomain biopolymers: Flexible molecular strategies to acquire biological functions.Genes to cells : devoted to molecular & cellular mechanisms · 2023Review
- Protein nanocondensates: the next frontier.Biophysical reviews · 2023Review
- Disrupting pathologic phase transitions in neurodegeneration.The Journal of clinical investigation · 2023Review
- G-quadruplexes rescuing protein folding.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Addressing Critical Issues Related to Storage and Stability of the Vault Nanoparticle Expressed and Purified fromInternational journal of molecular sciences · 2023Article
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
Most proteins in cell and tissue lysates are soluble. We show here that in lysate from human neurons, more than 1,300 proteins are maintained in a soluble and functional state by association with endogenous RNA, as degradation of RNA invariably leads to protein aggregation. The majority of these proteins lack conventional RNA-binding domains. Using synthetic oligonucleotides, we identify the importance of nucleic acid structure, with single-stranded pyrimidine-rich bulges or loops surrounded by double-stranded regions being particularly efficient in the maintenance of protein solubility. These experiments also identify an apparent one-to-one protein-nucleic acid stoichiometry. Furthermore, we show that protein aggregates isolated from brain tissue from Amyotrophic Lateral Sclerosis patients can be rendered soluble after refolding by both RNA and synthetic oligonucleotides. Together, these findings open new avenues for understanding the mechanism behind protein aggregation and shed light on how certain proteins remain soluble.
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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.