From splicing to disease: the crucial role of serine/arginine protein kinases in cellular regulation.

Rilang Sa, Xuemin Zhang, Mandi Wu, Lan Yu

Abstract readReview

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.

Rilang Sa *Graduate School, Inner Mongolia Medical University, Hohhot, 010059, Inner Mongolia, China.ORCID http://orcid.org/0000-0003-0531-3383

Xuemin Zhang *Inner Mongolia Academy of Medical Sciences, Inner Mongolia People's Hospital, Hohhot, 010010, Inner Mongolia, China.

Mandi WuInner Mongolia Academy of Medical Sciences, Inner Mongolia People's Hospital, Hohhot, 010010, Inner Mongolia, China.

Lan YuAffiliated Inner Mongolia Clinical College of Inner Mongolia Medical University, Hohhot, 010059, Inner Mongolia, China. yulan@imph.ac.cn.

Funding

National Natural Science Foundation of China 82160299

6 · The paper itself

Abstract

The Serine/Arginine Protein Kinase (SRPK) family plays a critical role in regulating RNA splicing and associated phosphorylation events, thereby governing essential cellular processes such as splicing regulation, proteome diversification, and signaling pathway activation. Growing evidence implicates SRPKs in the pathogenesis of various diseases, underscoring their potential as promising therapeutic targets. In this review, we systematically summarize current knowledge on the structural characteristics of SRPKs, their mechanistic involvement in disease pathogenesis, and emerging therapeutic strategies, based on comprehensive searches of databases including PubMed, Google Scholar, and X-mol. We further provide mechanistic insights into SRPK-mediated disease regulation, assess recent advances in the development of SRPK-targeted inhibitors, and discuss key challenges and future research directions in the field. This review aims to offer guidance for subsequent studies and to facilitate the translation of SRPK-related mechanisms into precision medicine applications.

Indexed as

Protein Serine-Threonine KinasesRNA SplicingAnimalsHumansPhosphorylationProtein Kinase InhibitorsSignal TransductionProtein Kinase InhibitorsProtein Serine-Threonine KinasesPhosphorylationSignaling pathwaysSplicing regulationTargeted inhibitorsTherapeutic potentialThe SRPK family

Identifiers

PMID42213263

DOI10.1371/journal.pone.0315569

What OpenQuestion holds

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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.