Evidence map›Paper›PMID 40944356›Full record

ReviewBiochemical Society transactions2025

Structural and evolutionary insights into understudied bacterial serine-threonine pseudokinase families.

Brady O'Boyle, Debarshi Ryan Bhowmik, Patrick A Eyers, Dominic P Byrne, Natarajan Kannan

Abstract readReview
In one paragraph

Review in Biochemical Society transactions, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Review
  2. 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

5 authors.

Brady O'BoyleDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, GA, 30602, U.S.A.
Debarshi Ryan BhowmikInstitute of Bioinformatics University of Georgia, Athens, GA, 30602, U.S.A.ORCID 0000-0001-6979-5460
Patrick A EyersDepartment of Biochemistry, Cell and Systems Biology, Institute of Systems, Molecular and Integrative Biology, University of Liverpool, Liverpool, L69 7ZB, U.K.ORCID 0000-0002-9220-2966
Dominic P ByrneDepartment of Biochemistry, Cell and Systems Biology, Institute of Systems, Molecular and Integrative Biology, University of Liverpool, Liverpool, L69 7ZB, U.K.ORCID 0000-0001-5197-345X
Natarajan KannanDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, GA, 30602, U.S.A.ORCID 0000-0002-2833-8375

Funding

Unlocking sequence-structure-function-disease relationships in large protein super-familiesR35GM139656 · NIGMS · UNIVERSITY OF GEORGIA · PI KANNAN, NATARAJAN · 2021 to 2025
$2.2M
NIGMS NIH HHS R35 GM139656
6 · The paper itself

Abstract

Pseudokinases, once considered catalytically inactive remnants of evolution, have emerged as key regulators of numerous fundamental biological processes. While eukaryotic pseudokinases have attracted significant attention, bacterial pseudokinases remain largely unexplored experimentally. Recent advances in sequence analysis and structural modeling have identified and characterized multiple conserved bacterial pseudokinase families, each with distinct predicted catalytic impairments but unknown functions. This review delves into their classification, structural features, and evolutionary adaptation. We also highlight the significance of bacterial pseudokinases in host-microbe interactions and their emerging potential as therapeutic targets. By integrating bioinformatics with experimental approaches, future research is poised to uncover the biological functions of bacterial pseudokinases, providing new insights into microbial signaling mechanisms and revealing new strategies to interrogate bacterial cell signaling, including pseudokinase drivers of infection and antimicrobial drug resistance.

Indexed as

BacteriaBacterial ProteinsEvolution, MolecularProtein Serine-Threonine KinasesHumansSignal TransductionBacterial ProteinsProtein Serine-Threonine Kinasesbacterial kinasesevolutionary biologyprotein–serine–threonine kinasesprotein structurepseudokinases

Identifiers

PMID40944356
PMCPMC12599244

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Registered trials

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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.