Evidence map›Paper›PMID 37198350›Full record

ReviewCellular and molecular life sciences : CMLS2023

Serine-arginine protein kinases and their targets in viral infection and their inhibition.

Kai Zheng, Zhe Ren, Yifei Wang

Open access · bronzeAbstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.2field-weighted citation impact, top 13% of its field
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

14 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Review
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  6. Article
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  9. Review
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  11. Article
  12. Review
  13. Review
  14. Protein arginine methylation in viral infection and antiviral immunity.International journal of biological sciences · 2023
    Review
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

3 authors at 2 institutions in 1 country.

Kai ZhengSchool of Pharmacy, Shenzhen University Medical School, Shenzhen, 518055, China. zhengk@szu.edu.cn.ORCID http://orcid.org/0000-0001-9275-1239
Zhe RenInstitute of Biomedicine, College of Life Science and Technology, Guangdong Province Key Laboratory of Bioengineering Medicine, Key Laboratory of Innovative Technology Research On Natural Products and Cosmetics Raw Materials, Jinan University, Guangzhou, 510632, China.
Yifei WangInstitute of Biomedicine, College of Life Science and Technology, Guangdong Province Key Laboratory of Bioengineering Medicine, Key Laboratory of Innovative Technology Research On Natural Products and Cosmetics Raw Materials, Jinan University, Guangzhou, 510632, China.
Jinan University · CNShenzhen University · CN

Funding

National Natural Science Foundation of China 82072274the Basic and Applied Basic Research Foundation of Guangdong Province 2021B1515120088
6 · The paper itself

Abstract

Accumulating evidence has consolidated the interaction between viral infection and host alternative splicing. Serine-arginine (SR) proteins are a class of highly conserved splicing factors critical for the spliceosome maturation, alternative splicing and RNA metabolism. Serine-arginine protein kinases (SRPKs) are important kinases that specifically phosphorylate SR proteins to regulate their distribution and activities in the central pre-mRNA splicing and other cellular processes. In addition to the predominant SR proteins, other cytoplasmic proteins containing a serine-arginine repeat domain, including viral proteins, have been identified as substrates of SRPKs. Viral infection triggers a myriad of cellular events in the host and it is therefore not surprising that viruses explore SRPKs-mediated phosphorylation as an important regulatory node in virus-host interactions. In this review, we briefly summarize the regulation and biological function of SRPKs, highlighting their involvement in the infection process of several viruses, such as viral replication, transcription and capsid assembly. In addition, we review the structure-function relationships of currently available inhibitors of SRPKs and discuss their putative use as antivirals against well-characterized viruses or newly emerging viruses. We also highlight the viral proteins and cellular substrates targeted by SRPKs as potential antiviral therapeutic candidates.

Indexed as

Protein KinasesVirus DiseasesAlternative SplicingArginineHumansPhosphorylationProtein Serine-Threonine KinasesRNA SplicingSerineSerine-Arginine Splicing FactorsViral ProteinsArginineProtein KinasesProtein Serine-Threonine KinasesSerineSerine-Arginine Splicing FactorsViral ProteinsAlternative splicingAntiviralSerine-arginine protein kinasesSR proteinsVirus–host interaction

Identifiers

PMID37198350
PMCPMC10191411
OpenAlexW4376868269

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.