Evidence map›Paper›PMID 37145304›Full record

ReviewPlanta2023

Plant serine/arginine-rich proteins: versatile players in RNA processing.

Zi-Chang Jia, Debatosh Das, Youjun Zhang, Alisdair R Fernie, Ying-Gao Liu, Moxian Chen, Jianhua Zhang

Abstract readReview
PubMed Publisher
In one paragraph

Review in Planta, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

9 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Identification of the Splicing FactorInternational journal of molecular sciences · 2025
    Article
  5. Review
  6. Genome-Wide Isoform Switching Reveals SR45-Mediated Splicing Control ofInternational journal of molecular sciences · 2025
    Article
  7. Article
  8. Article
  9. 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

7 authors at 5 institutions in 6 countries.

Zi-Chang Jia *National Key Laboratory of Green Pesticide, Key Laboratory of Green Pesticide and Agricultural Bioengineering, Ministry of Education, Center for R&D of Fine Chemicals of Guizhou University, Guiyang, 550025, China.
Debatosh Das *College of Agriculture, Food and Natural Resources (CAFNR), Division of Plant Sciences and Technology, 52 Agricultural Building, University of Missouri, Columbia, MO, 65201, USA.
Youjun ZhangCenter of Plant System Biology and Biotechnology, 4000, Plovdiv, Bulgaria.
Alisdair R FernieCenter of Plant System Biology and Biotechnology, 4000, Plovdiv, Bulgaria.
Ying-Gao LiuState Key Laboratory of Crop Biology, College of Life Science, Shandong Agricultural University, Taian, Shandong, China.
Moxian ChenNational Key Laboratory of Green Pesticide, Key Laboratory of Green Pesticide and Agricultural Bioengineering, Ministry of Education, Center for R&D of Fine Chemicals of Guizhou University, Guiyang, 550025, China. cmx2009920734@gmail.com.ORCID http://orcid.org/0000-0003-4538-5533
Jianhua ZhangDepartment of Biology, Hong Kong Baptist University, and State Key Laboratory of Agrobiotechnology, The Chinese University of Hong Kong, Shatin, Hong Kong. jzhang@hkbu.edu.hk.
Center of Plant Systems Biology and Biotechnology · BGHong Kong Baptist University · HKGuizhou University · CNShandong Agricultural University · CNShenzhen Institutes of Advanced Technology · CN

Funding

National Natural Science Foundation of China 91535109Natural Science Foundation of Jiangsu Province SBK2020042924
6 · The paper itself

Abstract

MAIN

conclusionSerine/arginine-rich (SR) proteins participate in RNA processing by interacting with precursor mRNAs or other splicing factors to maintain plant growth and stress responses. Alternative splicing is an important mechanism involved in mRNA processing and regulation of gene expression at the posttranscriptional level, which is the main reason for the diversity of genes and proteins. The process of alternative splicing requires the participation of many specific splicing factors. The SR protein family is a splicing factor in eukaryotes. The vast majority of SR proteins' existence is an essential survival factor. Through its RS domain and other unique domains, SR proteins can interact with specific sequences of precursor mRNA or other splicing factors and cooperate to complete the correct selection of splicing sites or promote the formation of spliceosomes. They play essential roles in the composition and alternative splicing of precursor mRNAs, providing pivotal functions to maintain growth and stress responses in animals and plants. Although SR proteins have been identified in plants for three decades, their evolutionary trajectory, molecular function, and regulatory network remain largely unknown compared to their animal counterparts. This article reviews the current understanding of this gene family in eukaryotes and proposes potential key research priorities for future functional studies.

Indexed as

RNA-Binding ProteinsSerineAlternative SplicingAnimalsArginineNuclear ProteinsPlant ProteinsRNA, MessengerRNA PrecursorsRNA SplicingRNA Splicing FactorsArginineNuclear ProteinsPlant ProteinsRNA-Binding ProteinsRNA, MessengerRNA PrecursorsRNA Splicing FactorsSerineMolecular mechanismPre-mRNA splicingRNA bindingSerine arginine-rich (SR) proteinsSplicing factor

Identifiers

PMID37145304
OpenAlexW4372292204

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.