Evidence map›Paper›PMID 39543097›Full record

ArticleNature communications2024

DHX36 binding induces RNA structurome remodeling and regulates RNA abundance via m

Yuwei Zhang, Jieyu Zhao, Xiaona Chen, Yulong Qiao, Jinjin Kang, Xiaofan Guo, Feng Yang, Kaixin Lyu, Yiliang Ding, Yu Zhao and 3 more

Abstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

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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

13 authors.

Yuwei Zhang *Department of Chemical Pathology, Li Ka Shing Institute of Health Sciences, Chinese University of Hong Kong, Hong Kong, SAR, China.
Jieyu Zhao *Department of Chemistry and State Key Laboratory of Marine Pollution, City University of Hong Kong, Hong Kong, SAR, China.
Xiaona ChenDepartment of Orthopaedics and Traumatology, Li Ka Shing Institute of Health Sciences, Chinese University of Hong Kong, Hong Kong, SAR, China.
Yulong QiaoDepartment of Orthopaedics and Traumatology, Li Ka Shing Institute of Health Sciences, Chinese University of Hong Kong, Hong Kong, SAR, China.
Jinjin KangMolecular Cancer Research Center, School of Medicine, Shenzhen Campus of Sun Yat-sen University, Sun Yat-sen University, Shenzhen, China.
Xiaofan GuoDepartment of Orthopaedics and Traumatology, Li Ka Shing Institute of Health Sciences, Chinese University of Hong Kong, Hong Kong, SAR, China.
Feng YangDepartment of Chemical Pathology, Li Ka Shing Institute of Health Sciences, Chinese University of Hong Kong, Hong Kong, SAR, China.
Kaixin LyuDepartment of Chemistry and State Key Laboratory of Marine Pollution, City University of Hong Kong, Hong Kong, SAR, China.ORCID 0000-0002-9330-1296
Yiliang DingDepartment of Cell and Developmental Biology, John Innes Centre, Norwich Research Park, Norwich, NR4 7UH, United Kingdom.ORCID 0000-0003-4161-6365
Yu ZhaoMolecular Cancer Research Center, School of Medicine, Shenzhen Campus of Sun Yat-sen University, Sun Yat-sen University, Shenzhen, China.
Hao SunWarshel Institute for Computational Biology, The Chinese University of Hong Kong, Shenzhen, China. sunhao100@cuhk.edu.cn.ORCID 0000-0002-5547-9501
Chun-Kit KwokDepartment of Chemistry and State Key Laboratory of Marine Pollution, City University of Hong Kong, Hong Kong, SAR, China. ckkwok42@cityu.edu.hk.ORCID 0000-0001-9175-8543
Huating WangDepartment of Orthopaedics and Traumatology, Li Ka Shing Institute of Health Sciences, Chinese University of Hong Kong, Hong Kong, SAR, China. huating.wang@cuhk.edu.hk.ORCID 0000-0001-5474-2905

Funding

National Natural Science Foundation of China (National Science Foundation of China) 32270587National Natural Science Foundation of China (National Science Foundation of China) 32300703National Natural Science Foundation of China (National Science Foundation of China) 82172436
6 · The paper itself

Abstract

RNA structure constitutes a new layer of gene regulatory mechanisms. RNA binding proteins can modulate RNA secondary structures, thus participating in post-transcriptional regulation. The DEAH-box helicase 36 (DHX36) is known to bind and unwind RNA G-quadruplex (rG4) structure but the transcriptome-wide RNA structure remodeling induced by DHX36 binding and the impact on RNA fate remain poorly understood. Here, we investigate the RNA structurome alteration induced by DHX36 depletion. Our findings reveal that DHX36 binding induces structural remodeling not only at the localized binding sites but also on the entire mRNA transcript most pronounced in 3'UTR regions. DHX36 binding increases structural accessibility at 3'UTRs which is correlated with decreased post-transcriptional mRNA abundance. Further analyses and experiments uncover that DHX36 binding sites are enriched for N6-methyladenosine (m

Indexed as

3' Untranslated RegionsAdenosineDEAD-box RNA HelicasesProtein BindingRNA-Binding ProteinsRNA, MessengerBinding SitesGene Expression RegulationG-QuadruplexesHEK293 CellsHeLa CellsHumansNucleic Acid ConformationRNARNA Stability3' Untranslated RegionsAdenosineDEAD-box RNA HelicasesDHX36 protein, humanN-methyladenosineRNARNA-Binding ProteinsRNA, MessengerYTHDF1 protein, human

Identifiers

PMID39543097
PMCPMC11564809

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.