ArticleACS chemical biology2020
Reactivity-Based Screening for Citrulline-Containing Natural Products Reveals a Family of Bacterial Peptidyl Arginine Deiminases.
Article in ACS chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 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
22 citing papers in PubMed, 32 citations in OpenAlex.
- Bis-hydroxylation of Homocitrulline Catalyzed by a Multinuclear Nonheme Iron Oxidative Enzyme during RiPP Biosynthesis.Journal of the American Chemical Society · 2026Article
- Tangled Tail of Mechanically Interlocked Peptides.Journal of the American Chemical Society · 2026Review
- Bis-hydroxylation of Homocitrulline Catalyzed by a Multinuclear Nonheme Iron-Dependent Oxidative Enzyme during RiPP Biosynthesis.bioRxiv : the preprint server for biology · 2026Article
- Dual-probe genome mining identifies citrulassin N, a novel citrulline modified lasso peptide fromFrontiers in microbiology · 2026Article
- Evolution-Guided Discovery of Antimycobacterial Triculamin-Like Lasso Peptides.Angewandte Chemie (International ed. in English) · 2025Article
- Iterative glycosylation on a single residue of a mature lasso peptide.Chemical science · 2025Article
- Integrating Metabolomics and Genomics to Uncover Antimicrobial Compounds inAntibiotics (Basel, Switzerland) · 2025Article
- Article
- A Diels-Alder probe for discovery of natural products containing furan moieties.Beilstein journal of organic chemistry · 2024Article
- Bioinformatics-guided discovery of biaryl-linked lasso peptides.Chemical science · 2023Article
- Bioinformatics-Guided Discovery of Biaryl-Tailored Lasso Peptides.bioRxiv : the preprint server for biology · 2023Article
- Bioinformatic prediction and experimental validation of RiPP recognition elements.Methods in enzymology · 2023Article
- Catch-enrich-release approach for amine-containing natural products.Chemical communications (Cambridge, England) · 2022Article
- Identification, characterization, and genome sequencing of3 Biotech · 2022Article
- Unusual Post-Translational Modifications in the Biosynthesis of Lasso Peptides.International journal of molecular sciences · 2022Review
- Comprehensive Mutational Analysis of the Lasso Peptide Klebsidin.ACS chemical biology · 2022Article
- Reactivity-based screening for natural product discovery.Methods in enzymology · 2022Article
- New azodyrecins identified by a genome mining-directed reactivity-based screening.Beilstein journal of organic chemistry · 2022Article
- Cellulonodin-2 and Lihuanodin: Lasso Peptides with an Aspartimide Post-Translational Modification.Journal of the American Chemical Society · 2021Article
- Sterol Sponge Mechanism Is Conserved for Glycosylated Polyene Macrolides.ACS central science · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Ribosomally synthesized and post-translationally modified peptides (RiPPs) are a family of natural products defined by a genetically encoded precursor peptide that is processed by associated biosynthetic enzymes to form the mature product. Lasso peptides are a class of RiPP defined by an isopeptide linkage between the N-terminal amine and an internal Asp/Glu residue with the C-terminal sequence threaded through the macrocycle. This unique lariat topology, which typically provides considerable stability toward heat and proteases, has stimulated interest in lasso peptides as potential therapeutics. Post-translational modifications beyond the class-defining, threaded macrolactam have been reported, including one example of Arg deimination to yield citrulline (Cit). Although a Cit-containing lasso peptide (i.e., citrulassin) was serendipitously discovered during a genome-guided campaign, the gene(s) responsible for Arg deimination has remained unknown. Herein, we describe the use of reactivity-based screening to discriminate bacterial strains that produce Arg- versus Cit-bearing citrulassins, yielding 13 new lasso peptide variants. Partial phylogenetic profiling identified a distally encoded peptidyl arginine deiminase (PAD) gene ubiquitous to the Cit-containing variants. Absence of this gene correlated strongly with lasso peptide variants only containing Arg (i.e.,
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.