ArticleThe Journal of biological chemistry2012
Binding with nucleic acids or glycosaminoglycans converts soluble protein oligomers to amyloid.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers, 1 of them a synthesis that pooled it.
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
38 citing papers in PubMed, 1 synthesis or guideline pooled it, 59 citations in OpenAlex.
- Microbial dysbiosis in systemic lupus erythematosus: a scientometric study.Frontiers in microbiology · 2024Pooled it
- Molecular recognition and structural plasticity in amyloid-nucleic acid complexes.Journal of structural biology · 2025Review
- The mouse epididymal amyloid matrix is a mammalian counterpart of a bacterial biofilm.iScience · 2024Article
- RNA tailing machinery drives amyloidogenic phase transition.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Amyloid-containing biofilms and autoimmunity.Current opinion in structural biology · 2022Review
- Modulation of assembly of TDP-43 low-complexity domain by heparin: From droplets to amyloid fibrils.Biophysical journal · 2022Article
- Polymorphism in alpha-synuclein oligomers and its implications in toxicity under disease conditions.Frontiers in molecular biosciences · 2022Review
- A genetic link between risk for Alzheimer's disease and severe COVID-19 outcomes via the OAS1 gene.Brain : a journal of neurology · 2021Article
- Type I interferon response drives neuroinflammation and synapse loss in Alzheimer disease.The Journal of clinical investigation · 2020Article
- Intrinsic antiviral immunity drives neurodegeneration in Alzheimer disease.The Journal of clinical investigation · 2020Article
- Antiviral Immune Response in Alzheimer's Disease: Connecting the Dots.Frontiers in neuroscience · 2020Article
- Functional Reciprocity of Amyloids and Antimicrobial Peptides: Rethinking the Role of Supramolecular Assembly in Host Defense, Immune Activation, and Inflammation.Frontiers in immunology · 2020Review
- Triggers of Autoimmunity: The Role of Bacterial Infections in the Extracellular Exposure of Lupus Nuclear Autoantigens.Frontiers in immunology · 2019Review
- Loss of GPNMB Causes Autosomal-Recessive Amyloidosis Cutis Dyschromica in Humans.American journal of human genetics · 2018Article
- Why are Functional Amyloids Non-Toxic in Humans?Biomolecules · 2017Review
- A TLR9-dependent checkpoint governs B cell responses to DNA-containing antigens.The Journal of clinical investigation · 2017Article
- Bacterial amyloid curli acts as a carrier for DNA to elicit an autoimmune response via TLR2 and TLR9.PLoS pathogens · 2017Article
- Amyloids assemble as part of recognizable structures during oogenesis in Xenopus.Biology open · 2016Article
- Do nucleic acids moonlight as molecular chaperones?Nucleic acids research · 2016Article
- Extracellular DNA facilitates the formation of functional amyloids in Staphylococcus aureus biofilms.Molecular microbiology · 2016Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Ample evidence suggests that almost all polypeptides can either adopt a native structure (folded or intrinsically disordered) or form misfolded amyloid fibrils. Soluble protein oligomers exist as an intermediate between these two states, and their cytotoxicity has been implicated in the pathology of multiple human diseases. However, the mechanism by which soluble protein oligomers develop into insoluble amyloid fibrils is not clear, and investigation of this important issue is hindered by the unavailability of stable protein oligomers. Here, we have obtained stabilized protein oligomers generated from common native proteins. These oligomers exert strong cytotoxicity and display a common conformational structure shared with known protein oligomers. They are soluble and remain stable in solution. Intriguingly, the stabilized protein oligomers interact preferentially with both nucleic acids and glycosaminoglycans (GAG), which facilitates their rapid conversion into insoluble amyloid. Concomitantly, binding with nucleic acids or GAG strongly diminished the cytotoxicity of the protein oligomers. EGCG, a small molecule that was previously shown to directly bind to protein oligomers, effectively inhibits the conversion to amyloid. These results indicate that stabilized oligomers of common proteins display characteristics similar to those of disease-associated protein oligomers and represent immediate precursors of less toxic amyloid fibrils. Amyloid conversion is potently expedited by certain physiological factors, such as nucleic acids and GAGs. These findings concur with reports of cofactor involvement with disease-associated amyloid and shed light on potential means to interfere with the pathogenic properties of misfolded proteins.
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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.