ReviewThe Journal of biological chemistry2014
Microbial protein-tyrosine kinases.
Review in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 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
36 citing papers in PubMed, 69 citations in OpenAlex.
- Construction and phenotypic analysis of a low molecular weight tyrosine phosphatase mutant in Streptococcus suis serotype 2.BMC veterinary research · 2026Article
- Structural and mechanistic basis of ubiquitous bacterial kinase signaling identifies PorX as a noncanonical substrate in Porphyromonas gingivalis.The Journal of biological chemistry · 2026Article
- Molecular basis for the phosphorylation of bacterial tyrosine kinase Wzc.Nature communications · 2025Article
- An exopolysaccharide pathway from a freshwaterJournal of bacteriology · 2024Article
- Review
- A novel exopolysaccharide pathway from a freshwaterbioRxiv : the preprint server for biology · 2023Article
- Giving a signal: how protein phosphorylation helps Bacillus navigate through different life stages.FEMS microbiology reviews · 2023Review
- A Review of the Bacterial Phosphoproteomes of Beneficial Microbes.Microorganisms · 2023Review
- Phosphorylation and sulfation share a common biosynthetic pathway, but extend biochemical and evolutionary diversity of biological macromolecules in distinct ways.Journal of the Royal Society, Interface · 2022Article
- Structural basis for the recognition of the bacterial tyrosine kinase Wzc by its cognate tyrosine phosphatase Wzb.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Tyrosine Kinases and Phosphatases: Enablers of theFrontiers in oral health · 2022Review
- Identification and characterization of a UbK family kinase in Porphyromonas gingivalis that phosphorylates the RprY response regulator.Molecular oral microbiology · 2021Article
- An ATPase with a twist: A unique mechanism underlies the activity of the bacterial tyrosine kinase, Wzc.Science advances · 2021Article
- Structural and Functional Insights into the Biofilm-Associated BceF Tyrosine Kinase Domain fromBiomolecules · 2021Article
- Review
- Novel Tyrosine Kinase-Mediated Phosphorylation With Dual Specificity Plays a Key Role in the Modulation ofFrontiers in microbiology · 2021Article
- Potential ProbioticFrontiers in microbiology · 2021Article
- A tyrosine phosphoregulatory system controls exopolysaccharide biosynthesis and biofilm formation in Vibrio cholerae.PLoS pathogens · 2020Article
- Recent Development of Machine Learning Methods in Microbial Phosphorylation Sites.Current genomics · 2020Review
- Tyrosine Phosphorylation as a Widespread Regulatory Mechanism in Prokaryotes.Journal of bacteriology · 2019Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Microbial ester kinases identified in the past 3 decades came as a surprise, as protein phosphorylation on Ser, Thr, and Tyr amino acids was thought to be unique to eukaryotes. Current analysis of available microbial genomes reveals that "eukaryote-like" protein kinases are prevalent in prokaryotes and can converge in the same signaling pathway with the classical microbial "two-component" systems. Most microbial tyrosine kinases lack the "eukaryotic" Hanks domain signature and are designated tyrosine kinases based upon their biochemical activity. These include the tyrosine kinases termed bacterial tyrosine kinases (BY-kinases), which are responsible for the majority of known bacterial tyrosine phosphorylation events. Although termed generally as bacterial tyrosine kinases, BY-kinases can be considered as one family belonging to the superfamily of prokaryotic protein-tyrosine kinases in bacteria. Other members of this superfamily include atypical "odd" tyrosine kinases with diverse mechanisms of protein phosphorylation and the "eukaryote-like" Hanks-type tyrosine kinases. Here, we discuss the distribution, phylogeny, and function of the various prokaryotic protein-tyrosine kinases, focusing on the recently discovered Mycobacterium tuberculosis PtkA and its relationship with other members of this diverse family of 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.