ArticleScientific reports2014
Lysine pyrrolation is a naturally-occurring covalent modification involved in the production of DNA mimic proteins.
Article in Scientific reports, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 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
18 citing papers in PubMed, 27 citations in OpenAlex.
- Design, synthesis, antibacterial activity evaluation, and mechanism of action study of novel pyrrolidine derivatives containing sulfonamide structures.Molecular diversity · 2026Article
- Covalent Protein Inhibitors via Tyrosine and Tryptophan Conjugation with Cyclic Imine Mannich Electrophiles.Angewandte Chemie (International ed. in English) · 2026Article
- Microvascular endothelial dysfunction in vascular senescence and disease.Frontiers in cardiovascular medicine · 2025Review
- Immunoproteasomal Processing of IsoLG-Adducted Proteins Is Essential for Hypertension.Circulation research · 2024Article
- Molecular and structural basis of anti-DNA antibody specificity for pyrrolated proteins.Communications biology · 2024Article
- Cellular and epigenetic perspective of protein stability and its implications in the biological system.Epigenomics · 2024Review
- Isolevuglandins disrupt PU.1-mediated C1q expression and promote autoimmunity and hypertension in systemic lupus erythematosus.JCI insight · 2022Article
- Unique B-1 cells specific for both N-pyrrolated proteins and DNA evolve with apolipoprotein E deficiency.The Journal of biological chemistry · 2022Article
- Glycolaldehyde is an endogenous source of lysineThe Journal of biological chemistry · 2020Article
- Isolevuglandins as mediators of disease and the development of dicarbonyl scavengers as pharmaceutical interventions.Pharmacology & therapeutics · 2020Review
- A Dual Perspective of the Action of Lysine on Soybean Oil Oxidation Process Obtained by CombiningAntioxidants (Basel, Switzerland) · 2019Article
- Apolipoprotein E binds to and reduces serum levels of DNA-mimicking, pyrrolated proteins.The Journal of biological chemistry · 2019Article
- Hypertension as an autoimmune and inflammatory disease.Hypertension research : official journal of the Japanese Society of Hypertension · 2016Review
- Accumulation of isolevuglandin-modified protein in normal and fibrotic lung.Scientific reports · 2016Article
- Immune activation caused by vascular oxidation promotes fibrosis and hypertension.The Journal of clinical investigation · 2016Article
- Observed surface lysine acetylation of human carbonic anhydrase II expressed in Escherichia coli.Protein science : a publication of the Protein Society · 2015Article
- Site-specific, intramolecular cross-linking of Pin1 active site residues by the lipid electrophile 4-oxo-2-nonenal.Chemical research in toxicology · 2015Article
- Inflammation, immunity, and hypertensive end-organ damage.Circulation research · 2015Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
11 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Covalent modification of proteins exerts significant effects on their chemical properties and has important functional and regulatory consequences. We now report the identification and verification of an electrically-active form of modified proteins recognized by a group of small molecules commonly used to interact with DNA. This previously unreported property of proteins was initially discovered when the γ-ketoaldehydes were identified as a source of the proteins stained by the DNA intercalators. Using 1,4-butanedial, the simplest γ-ketoaldehyde, we characterized the structural and chemical criteria governing the recognition of the modified proteins by the DNA intercalators and identified N(ε)-pyrrolelysine as a key adduct. Unexpectedly, the pyrrolation conferred an electronegativity and electronic properties on the proteins that potentially constitute an electrical mimic to the DNA. In addition, we found that the pyrrolated proteins indeed triggered an autoimmune response and that the production of specific antibodies against the pyrrolated proteins was accelerated in human systemic lupus erythematosus. These findings and the apparent high abundance of N(ε)-pyrrolelysine in vivo suggest that protein pyrrolation could be an endogenous source of DNA mimic proteins, providing a possible link connecting protein turnover and immune disorders.
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.