Evidence map›Paper›PMID 42862221›Full record

ReviewMolecular biology reports2026

Mechanisms of phosphorylation in colitis regulation: PP2Acα as an emerging therapeutic target for inflammatory bowel disease.

Guanghao Wu, Chuan Wang, Chao Fang, Jun Li

Abstract readReview
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In one paragraph

Review in Molecular biology reports, 2026. 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

4 authors.

Guanghao WuDepartment of General Surgery, The Affiliated Jiangning Hospital of Nanjing Medical University, 169 Hushan Road, Nanjing, 211100, China.
Chuan WangDepartment of Gastroenterology, The Affiliated Jiangning Hospital of Nanjing Medical University, 169 Hushan Road, Nanjing, 211100, China.
Chao FangCentral Laboratory, The Affiliated Jiangning Hospital of Nanjing Medical University, 169 Hushan Road, Nanjing, 211100, China. fangchao@njmu.edu.cn.ORCID http://orcid.org/0000-0002-9537-8262
Jun LiDepartment of General Surgery, The Affiliated Jiangning Hospital of Nanjing Medical University, 169 Hushan Road, Nanjing, 211100, China. lijun@njmu.edu.cn.

Funding

Youth Science Fund Project of the National Natural Science Foundation of China (Category C) Grant No. 81903245
6 · The paper itself

Abstract

Post-translational modification(PTM) is the terminal regulatory step of gene expression, directly regulating protein function through reversible or irreversible chemical modifications, enabling cells to rapidly respond to internal and external environmental stimuli. Among various post-translational modifications (PTMs), the dynamic balance between phosphorylation and dephosphorylation constitutes the molecular switch for inflammatory signal transduction, and disruption of this balance is an important cause of the persistent non-healing of inflammatory bowel disease (IBD). The catalytic subunit of protein phosphatase 2 A, PP2Acα(encoded by the PPP2CA gene), as the predominant serine/threonine phosphatase in the body, accounts for more than 70% of serine/threonine phosphatase activity in mammalian tissues and has been proven to play a key role in inflammatory diseases such as rheumatoid arthritis. However, the specific regulatory network, targets, and mechanisms of PPP2CA in IBD have not yet been systematically elucidated. This review aims to summarize the regulatory role of PTMs (especially phosphorylation/dephosphorylation) in IBD, deeply explore the structure and function of PPP2CA and its potential mechanisms in intestinal inflammation, and propose core scientific questions for future research, providing a new theoretical perspective for IBD therapeutic strategies targeting PPP2CA.

Indexed as

ColitisInflammatory Bowel DiseasesProtein Phosphatase 2Protein Phosphatase 2CAnimalsHumansPhosphorylationProtein Processing, Post-TranslationalSignal TransductionPPP2CA protein, humanProtein Phosphatase 2Protein Phosphatase 2CDephosphorylationInflammatory bowel diseasePhosphorylationPost-translational modificationPPP2CA

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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.