Evidence map›Paper›PMID 31262836›Full record

ReviewJournal of bacteriology2019

Tyrosine Phosphorylation as a Widespread Regulatory Mechanism in Prokaryotes.

Landon J Getz, Cameron S Runte, Jan K Rainey, Nikhil A Thomas

Open access · bronzeAbstract readReview
In one paragraph

Review in Journal of bacteriology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.5field-weighted citation impact, top 18% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

14 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. A Tale aboutMicroorganisms · 2023
    Review
  9. Review
  10. D-Peptide and D-Protein Technology: Recent Advances, Challenges, and Opportunities.Chembiochem : a European journal of chemical biology · 2023
    Review
  11. Article
  12. Article
  13. Article
  14. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Landon J GetzDepartment of Microbiology and Immunology, Dalhousie University, Halifax, Nova Scotia, Canada.ORCID 0000-0002-3841-1062
Cameron S RunteDepartment of Microbiology and Immunology, Dalhousie University, Halifax, Nova Scotia, Canada.
Jan K RaineyDepartment of Biochemistry & Molecular Biology, Dalhousie University, Halifax, Nova Scotia, Canada.
Nikhil A ThomasDepartment of Microbiology and Immunology, Dalhousie University, Halifax, Nova Scotia, Canada n.thomas@dal.ca.ORCID 0000-0003-3037-425X
Dalhousie University · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phosphorylation events modify bacterial and archaeal proteomes, imparting cells with rapid and reversible responses to specific environmental stimuli or niches. Phosphorylated proteins are generally modified at one or more serine, threonine, or tyrosine residues. Within the last ten years, increasing numbers of global phosphoproteomic surveys of prokaryote species have revealed an abundance of tyrosine-phosphorylated proteins. In some cases, novel phosphorylation-dependent regulatory paradigms for cell division, gene transcription, and protein translation have been identified, suggesting that a wide scope of prokaryotic physiology remains to be characterized. Recent observations of bacterial proteins with putative phosphotyrosine binding pockets or Src homology 2 (SH2)-like domains suggest the presence of phosphotyrosine-dependent protein interaction networks. Here in this minireview, we focus on protein tyrosine phosphorylation, a posttranslational modification once thought to be rare in prokaryotes but which has emerged as an important regulatory facet in microbial biology.

Indexed as

ArchaeaBacteriaCell DivisionPhosphorylationProtein Interaction MapsProtein Processing, Post-TranslationalTranscription, GeneticTyrosineTyrosinecell biologypathogenesisphosphorylationprotein chaperoneprotein tyrosine binding domainproteomicsSH2 domaintranscriptional regulationtyrosine kinase

Identifiers

PMID31262836
PMCPMC6755747
OpenAlexW2954003973

What Socratic holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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 Socratic graph.