Evidence map›Paper›PMID 32713350›Full record

ArticleBMC plant biology2020

Genome-wide identification and expression analysis of YTH domain-containing RNA-binding protein family in common wheat.

Jing Sun, Xiao Min Bie, Ning Wang, Xian Sheng Zhang, Xin-Qi Gao

Open access · goldAbstract read
In one paragraph

Article in BMC plant biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
2.2field-weighted citation impact, top 12% of its field
1 · What the graph read from it

What it found

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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

38 citing papers in PubMed, 54 citations in OpenAlex.

  1. Article
  2. Genome-Wide Analysis of YTH Domain Proteins inPlants (Basel, Switzerland) · 2026
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  5. The role of NTAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2025
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  9. Article
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  12. Identification of mBiochemistry and biophysics reports · 2024
    Article
  13. Article
  14. Genome-Wide Identification and Expression Analysis ofInternational journal of molecular sciences · 2024
    Article
  15. Genome-wide identification of the NBMC plant biology · 2024
    Article
  16. Article
  17. Article
  18. The plant cytosolic mPlant communications · 2023
    Article
  19. Review
  20. Article
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

5 authors at 1 institution in 1 country.

Jing SunNational Key Laboratory of Crop Biology, College of Life Sciences, Shandong Agricultural University, Tai'an, 271018, China.
Xiao Min BieNational Key Laboratory of Crop Biology, College of Life Sciences, Shandong Agricultural University, Tai'an, 271018, China.
Ning WangNational Key Laboratory of Crop Biology, College of Life Sciences, Shandong Agricultural University, Tai'an, 271018, China.
Xian Sheng ZhangNational Key Laboratory of Crop Biology, College of Life Sciences, Shandong Agricultural University, Tai'an, 271018, China.
Xin-Qi GaoNational Key Laboratory of Crop Biology, College of Life Sciences, Shandong Agricultural University, Tai'an, 271018, China. gaoxq@sdau.edu.cn.ORCID http://orcid.org/0000-0002-2530-7776
Shandong Agricultural University · CN

Funding

National Natural Science Foundation of China 91935302National Transgenic Science and Technology Program 2019ZX08010-003
6 · The paper itself

Abstract

backgroundN6-Methyladenosine (m6A) is the most widespread RNA modification that plays roles in the regulation of genes and genome stability. YT521-B homology (YTH) domain-containing RNA-binding proteins are important RNA binding proteins that affect the fate of m6A-containing RNA by binding m6A. Little is known about the YTH genes in common wheat (Triticum aestivum L.), one of the most important crops for humans.

resultsA total of 39 TaYTH genes were identified in common wheat, which are comprised of 13 homologous triads, and could be mapped in 18 out of the 21 chromosomes. A phylogenetic analysis revealed that the TaYTHs could be divided into two groups: YTHDF (TaDF) and YTHDC (TaDC). The TaYTHs in the same group share similar motif distributions and domain organizations, which indicates functional similarity between the closely related TaYTHs. The TaDF proteins share only one domain, which is the YTH domain. In contrast, the TaDCs possess three C3H1-type zinc finger repeats at their N-termini in addition to their central YTH domain. In TaDFs, the predicated aromatic cage pocket that binds the methylysine residue of m6A is composed of tryptophan, tryptophan, and tryptophan (WWW). In contrast, the aromatic cage pocket in the TaDCs is composed of tryptophan, tryptophan, and tyrosine (WWY). In addition to the general aspartic acid or asparagine residue used to form a hydrogen bond with N

conclusionsIn this study, we identified 39 TaYTH genes from common wheat. The phylogenetic structure, chromosome distribution, and patterns of expression of these genes and their protein structures were analyzed. Our results provide a foundation for the functional analysis of TaYTHs in the future.

Indexed as

Gene Expression Regulation, PlantGenome-Wide Association StudyMultigene FamilyPhylogenyPlant ProteinsProtein DomainsRNA-Binding ProteinsRNA Recognition Motif ProteinsStress, PhysiologicalSyntenyTriticumPlant ProteinsRNA-Binding ProteinsRNA Recognition Motif ProteinsAbiotic stressDevelopmentExpression profilingWheatYTH domain-containing RNA-binding protein

Identifiers

PMID32713350
PMCPMC7384225
OpenAlexW3045194704

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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.