Evidence map›Paper›PMID 40488057›Full record

ArticleACS omega2025

Characterization of the Biological Effect Mediated by Mycobacterial Kinase PknG on Protein Phosphorylation and Acetylation.

Shuyu Xie, Tianqi Liu, Luoxi Zhang, Yang Yang, Yanqing Tang, Tong Ye, Yewen Sun, Yi Li, Shiyang Shen, Minjia Tan and 1 more

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PubMed Full text at PMC Publisher
In one paragraph

Article in ACS omega, 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

11 authors.

Shuyu XieZhongshan Institute for Drug Discovery, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, Guangdong 201203, China.
Tianqi LiuZhongshan Institute for Drug Discovery, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, Guangdong 201203, China.
Luoxi ZhangSchool of Pharmaceutical Sciences, Southern Medical University, Guangzhou 510515, China.
Yang YangSchool of Pharmaceutical Sciences, Southern Medical University, Guangzhou 510515, China.
Yanqing TangZhongshan Institute for Drug Discovery, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, Guangdong 201203, China.
Tong YeState Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.
Yewen SunZhongshan Institute for Drug Discovery, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, Guangdong 201203, China.
Yi LiZhongshan Institute for Drug Discovery, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, Guangdong 201203, China.ORCID https://orcid.org/0000-0001-6024-9973
Shiyang ShenZhongshan Institute for Drug Discovery, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, Guangdong 201203, China.
Minjia TanZhongshan Institute for Drug Discovery, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, Guangdong 201203, China.ORCID https://orcid.org/0000-0002-6784-9653
Jun-Yu XuZhongshan Institute for Drug Discovery, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, Guangdong 201203, China.ORCID https://orcid.org/0000-0002-1403-9200

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tuberculosis (TB) remains a significant global public health challenge, with post-translational modifications (PTMs) in mycobacteria being integral to physiological processes, pathogenesis, and drug resistance mechanisms. Protein kinase G (PknG), the only reported secreted kinase in mycobacteria, is associated with virulence, immune evasion, and drug resistance. Nevertheless, the comprehensive range of proteins and phosphorylation modifications regulated by PknG in mycobacteria has not yet been fully elucidated. This study conducted a systematic investigation into the dynamic alterations in the proteome and phosphoproteome of mycobacteria following the overexpression of PknG. A comprehensive analysis identified 3836 proteins and 467 phosphorylation sites, revealing the regulatory role of

Identifiers

PMID40488057
PMCPMC12138698

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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.