ArticleProceedings of the National Academy of Sciences of the United States of America2012
Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 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
74 citing papers in PubMed, 138 citations in OpenAlex.
- Pushing the limits of single-cell proteomics to investigate bacterial heterogeneity using bacSCP.Nature communications · 2026Article
- Roles of PknB and CslA in Cell Wall Morphogenesis of Streptomyces.Molecular microbiology · 2026Article
- Let the peptides shine: SOX (Sulfonamido-OXine)-labelled peptides for direct kinase and phosphatase monitoring.RSC chemical biology · 2026Review
- Mass Spectrometry-Based Identification of Post-Translational Modifications (PTMs) of Proteins.Advances in experimental medicine and biology · 2026Article
- Recent progress in proteins regulating the germination ofJournal of bacteriology · 2025Review
- Rok from B. subtilis: Bridging genome structure and transcription regulation.Molecular microbiology · 2025Review
- The regulatory impact of serine/threonine-specific protein phosphorylation among cyanobacteria.Frontiers in plant science · 2025Review
- The Transcriptomic Response of Cells of the Thermophilic BacteriumInternational journal of molecular sciences · 2024Article
- Structural insights into the regulation of protein-arginine kinase McsB by McsA.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Processing of stalled replication forks in Bacillus subtilis.FEMS microbiology reviews · 2024Review
- Giving a signal: how protein phosphorylation helps Bacillus navigate through different life stages.FEMS microbiology reviews · 2023Review
- Molecular Characterization of the ClpC AAA+ ATPase in the Biology of Chlamydia trachomatis.mBio · 2023Article
- A Review of the Bacterial Phosphoproteomes of Beneficial Microbes.Microorganisms · 2023Review
- Identification of Arginine Phosphorylation in Mycolicibacterium smegmatis.Microbiology spectrum · 2022Article
- Toward the Complete Functional Characterization of a Minimal Bacterial Proteome.The journal of physical chemistry. B · 2022Article
- Widespread Arginine Phosphorylation in Staphylococcus aureus.Molecular & cellular proteomics : MCP · 2022Article
- Reviving the view: evidence that macromolecule synthesis fuels bacterial spore germination.microLife · 2022Review
- Update on the Protein Homeostasis Network inFrontiers in microbiology · 2022Review
- Cultivation of Spore-Forming Gut Microbes Using a Combination of Bile Acids and Amino Acids.Microorganisms · 2021Article
- Article
14 more citing papers are in PubMed but not listed here.
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 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Reversible protein phosphorylation is an important and ubiquitous protein modification in all living cells. Here we report that protein phosphorylation on arginine residues plays a physiologically significant role. We detected 121 arginine phosphorylation sites in 87 proteins in the gram-positive model organism Bacillus subtilis in vivo. Moreover, we provide evidence that protein arginine phosphorylation has a functional role and is involved in the regulation of many critical cellular processes, such as protein degradation, motility, competence, and stringent and stress responses. Our results suggest that in B. subtilis the combined activity of a protein arginine kinase and phosphatase allows a rapid and reversible regulation of protein activity and that protein arginine phosphorylation can play a physiologically important and regulatory role in bacteria.
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.