Evidence map›Paper›PMID 41260339›Full record

ReviewThe Journal of biological chemistry2025

Modulation of host functions by bacterial serine/threonine protein kinase effector proteins.

Jinli Ge, Jiazhang Qiu

Abstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

2 authors.

Jinli GeState Key Laboratory for Diagnosis and Treatment of Severe Zoonotic Infectious Diseases, Key Laboratory for Zoonosis Research of the Ministry of Education, College of Veterinary Medicine, Jilin University, Changchun, China.
Jiazhang QiuState Key Laboratory for Diagnosis and Treatment of Severe Zoonotic Infectious Diseases, Key Laboratory for Zoonosis Research of the Ministry of Education, College of Veterinary Medicine, Jilin University, Changchun, China. Electronic address: qiujz@jlu.edu.cn.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein phosphorylation, one of the most ubiquitous and evolutionarily conserved posttranslational modifications, serves as a master regulator of cellular signaling networks. In host-pathogen interactions, bacterial subversion of phosphorylation-dependent signaling pathways has emerged as a pivotal mechanism of microbial pathogenesis. Notably, recent advances in eukaryotic-like serine/threonine protein kinase effector proteins have profoundly advanced our understanding of molecular pathogenesis through their ability to hijack host cell signaling. In this review, we will summarize the sophisticated strategies by which bacterial serine/threonine protein kinase effectors manipulate host phosphorylation networks to enhance virulence and promote infection.

Indexed as

BacteriaBacterial ProteinsHost-Pathogen InteractionsProtein Serine-Threonine KinasesAnimalsHumansPhosphorylationProtein Processing, Post-TranslationalSignal TransductionBacterial ProteinsProtein Serine-Threonine Kinasesbacterial pathogenshost substratephosphorylationposttranslational modificationsserine/threonine protein kinase (STPK)

Identifiers

PMID41260339
PMCPMC12756638

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.