ArticleBiophysical journal2020
DNA Facilitates Oligomerization and Prevents Aggregation via DNA Networks.
Article in Biophysical journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 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.
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Who cites it
12 citing papers in PubMed.
- Cis-Acting Chaperoning by Macromolecular Tethering: A Built-In Layer of Cellular Chaperoning.International journal of molecular sciences · 2026Review
- NMR-based conformational analysis of DNA G-quadruplex guides mapping essential structure-function relationship in protein chaperoning.Physical chemistry chemical physics : PCCP · 2026Article
- Catalyzing Protein Folding by Chaperones.Biology · 2025Review
- DNA binding and mitotic phosphorylation protect polyglutamine proteins from assembly formation.Cell · 2025Article
- Beyond Misfolding: A New Paradigm for the Relationship Between Protein Folding and Aggregation.International journal of molecular sciences · 2024Review
- Roles of Nucleic Acids in Protein Folding, Aggregation, and Disease.ACS chemical biology · 2024Review
- G-quadruplexes rescuing protein folding.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Why are G-quadruplexes good at preventing protein aggregation?RNA biology · 2023Article
- Modulation of α-Synuclein Aggregation In Vitro by a DNA Aptamer.Biochemistry · 2022Article
- A Conceptual Framework for Integrating Cellular Protein Folding, Misfolding and Aggregation.Life (Basel, Switzerland) · 2021Review
- Chaperna: linking the ancient RNA and protein worlds.RNA biology · 2021Review
- G-Quadruplexes act as sequence-dependent protein chaperones.EMBO reports · 2020Article
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
Abstract
Previous studies have shown that nucleic acids can nucleate protein aggregation in disease-related proteins, but in other cases, they can act as molecular chaperones that prevent protein aggregation, even under extreme conditions. In this study, we describe the link between these two behaviors through a combination of electron microscopy and aggregation kinetics. We find that two different proteins become soluble under harsh conditions through oligomerization with DNA. These DNA/protein oligomers form "networks," which increase the speed of oligomerization. The cases of DNA both increasing and preventing protein aggregation are observed to stem from this enhanced oligomerization. This observation raises interesting questions about the role of nucleic acids in aggregate formation in disease states.
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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.