ReviewInternational journal of molecular sciences2019
Goals and Challenges in Bacterial Phosphoproteomics.
Review in International journal of molecular sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 18 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.
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, 34 citations in OpenAlex.
- H-NOX and NosP Regulate Flagellar Protein and Virulence Factor Production in Vibrio Cholerae.Molecular & cellular proteomics : MCP · 2026Article
- Phosphoproteomics reveals essential regulatory roles of phosphorylation in marine oligotrophic bacteria.Marine life science & technology · 2026Article
- Evaluation of Data-Independent Acquisition-Based Phosphoproteomics Analysis in Mammalian and Bacterial Systems.Journal of proteome research · 2026Article
- Ser/Thr protein kinase Stk1 phosphorylates the key transcriptional regulator AlgR to modulate virulence and resistance inVirulence · 2024Article
- Dynamic Protein Phosphorylation inMicroorganisms · 2024Article
- A Review of the Bacterial Phosphoproteomes of Beneficial Microbes.Microorganisms · 2023Review
- FtsZ phosphorylation pleiotropically affects Z-ladder formation, antibiotic production, and morphogenesis in Streptomyces coelicolor.Antonie van Leeuwenhoek · 2023Article
- Impact of c-di-GMP on the Extracellular Proteome ofBiology · 2022Article
- Phosphoproteome Dynamics of Streptomyces rimosus during Submerged Growth and Antibiotic Production.mSystems · 2022Article
- pHisPred: a tool for the identification of histidine phosphorylation sites by integrating amino acid patterns and properties.BMC bioinformatics · 2022Article
- The Anti-Fungal Activity of Nitropropenyl Benzodioxole (NPBD), a Redox-Thiol Oxidant and Tyrosine Phosphatase Inhibitor.Antibiotics (Basel, Switzerland) · 2022Article
- Clostridioides difficile Phosphoproteomics Shows an Expansion of Phosphorylated Proteins in Stationary Growth Phase.mSphere · 2022Article
- Antibacterial Profile of a Microbicidal Agent Targeting Tyrosine Phosphatases and Redox Thiols, Novel Drug Targets.Antibiotics (Basel, Switzerland) · 2021Article
- Automated Phosphopeptide Enrichment for Gram-Positive Bacteria.Journal of proteome research · 2021Article
- Protein Tyrosine and Serine/Threonine Phosphorylation in Oral Bacterial Dysbiosis and Bacteria-Host Interaction.Frontiers in cellular and infection microbiology · 2021Review
- Addressing the Possibility of a Histone-Like Code in Bacteria.Journal of proteome research · 2021Review
- Phosphorylation of Extracellular Proteins inFrontiers in microbiology · 2021Article
- Correction: Yagüe, P., et al. Goals and Challenges in Bacterial Phosphoproteomics.International journal of molecular sciences · 2020Article
Corrections and comments
- Erratum issued
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Reversible protein phosphorylation at serine, threonine and tyrosine is a well-known dynamic post-translational modification with stunning regulatory and signalling functions in eukaryotes. Shotgun phosphoproteomic analyses revealed that this post-translational modification is dramatically lower in bacteria than in eukaryotes. However, Ser/Thr/Tyr phosphorylation is present in all analysed bacteria (24 eubacteria and 1 archaea). It affects central processes, such as primary and secondary metabolism development, sporulation, pathogenicity, virulence or antibiotic resistance. Twenty-nine phosphoprotein orthologues were systematically identified in bacteria: ribosomal proteins, enzymes from glycolysis and gluconeogenesis, elongation factors, cell division proteins, RNA polymerases, ATP synthases and enzymes from the citrate cycle. While Ser/Thr/Tyr phosphorylation exists in bacteria, there is a consensus that histidine phosphorylation is the most abundant protein phosphorylation in prokaryotes. Unfortunately, histidine shotgun phosphorproteomics is not possible due to the reduced phosphohistidine half-life under the acidic pH conditions used in standard LC-MS/MS analysis. However, considering the fast and continuous advances in LC-MS/MS-based phosphoproteomic methodologies, it is expected that further innovations will allow for the study of His phosphoproteomes and a better coverage of bacterial phosphoproteomes. The characterisation of the biological role of bacterial Ser/Thr/Tyr and His phosphorylations might revolutionise our understanding of prokaryotic physiology.
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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.