Evidence map›Paper›PMID 22889913›Full record

ReviewPhilosophical transactions of the Royal Society of London. Series B, Biological sciences2012

Bacterial tyrosine kinases: evolution, biological function and structural insights.

Christophe Grangeasse, Sylvie Nessler, Ivan Mijakovic

Abstract readReview
In one paragraph

Review in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.

0numbers the graph read from it
0cells of the map it votes in
78citing papers in PubMed
5.4field-weighted citation impact, top 3% 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

78 citing papers in PubMed, 141 citations in OpenAlex.

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  17. 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 · 2022
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18 more citing papers are in PubMed but not listed here.

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

3 authors at 3 institutions in 1 country.

Christophe GrangeasseBases Moléculaires et Structurales des Systèmes Infectieux, IBCP, CNRS, Université de Lyon, UMR 5086, 7 passage du Vercors, 69367 Lyon, France. c.grangeasse@ibcp.fr
Sylvie Nessler
Ivan Mijakovic
AgroParisTech · FRLaboratoire d'Enzymologie et Biochimie Structurales · FRStructural and Molecular Basis of Infectious Systems · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Reversible protein phosphorylation is a major mechanism in the regulation of fundamental signalling events in all living organisms. Bacteria have been shown to possess a versatile repertoire of protein kinases, including histidine and aspartic acid kinases, serine/threonine kinases, and more recently tyrosine and arginine kinases. Tyrosine phosphorylation is today recognized as a key regulatory device of bacterial physiology, linked to exopolysaccharide production, virulence, stress response and DNA metabolism. However, bacteria have evolved tyrosine kinases that share no resemblance with their eukaryotic counterparts and are unique in exploiting the ATP/GTP-binding Walker motif to catalyse autophosphorylation and substrate phosphorylation on tyrosine. These enzymes, named BY-kinases (for Bacterial tYrosine kinases), have been identified in a majority of sequenced bacterial genomes, and to date no orthologues have been found in Eukarya. The aim of this review was to present the most recent knowledge about BY-kinases by focusing primarily on their evolutionary origin, structural and functional aspects, and emerging regulatory potential based on recent bacterial phosphoproteomic studies.

Indexed as

Evolution, MolecularPhosphorylationAdenosine TriphosphateBacteriaBacterial ProteinsCatalytic DomainCell MembraneEnzyme ActivationMembrane ProteinsPolysaccharides, BacterialProtein-Tyrosine KinasesSpecies SpecificityStructure-Activity RelationshipAdenosine TriphosphateBacterial ProteinsMembrane ProteinsPolysaccharides, BacterialProtein-Tyrosine Kinases

Identifiers

PMID22889913
PMCPMC3415835
OpenAlexW2128077684

What OpenQuestion 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 OpenQuestion graph.