Evidence map›Paper›PMID 33428944›Full record

ArticleThe Journal of biological chemistry

Enzymatic characterization of three human RNA adenosine methyltransferases reveals diverse substrate affinities and reaction optima.

Dan Yu, Gundeep Kaur, Robert M Blumenthal, Xing Zhang, Xiaodong Cheng

Open access · goldAbstract read
In one paragraph

Article in The Journal of biological chemistry. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.1field-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

24 citing papers in PubMed, 35 citations in OpenAlex.

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  11. Ghost authors revealed: The structure and function of human NWiley interdisciplinary reviews. RNA · 2023
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  18. Systematic Design of Adenosine Analogs as Inhibitors of aJournal of medicinal chemistry · 2023
    Article
  19. Review
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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

5 authors at 2 institutions in 1 country.

Dan YuDepartment of Epigenetics and Molecular Carcinogenesis, University of Texas MD Anderson Cancer Center, Houston, Texas, USA.
Gundeep KaurDepartment of Epigenetics and Molecular Carcinogenesis, University of Texas MD Anderson Cancer Center, Houston, Texas, USA.
Robert M BlumenthalDepartment of Medical Microbiology and Immunology, and Program in Bioinformatics, The University of Toledo College of Medicine and Life Sciences, Toledo, Ohio, USA.
Xing ZhangDepartment of Epigenetics and Molecular Carcinogenesis, University of Texas MD Anderson Cancer Center, Houston, Texas, USA. Electronic address: XZhang21@mdanderson.org.
Xiaodong ChengDepartment of Epigenetics and Molecular Carcinogenesis, University of Texas MD Anderson Cancer Center, Houston, Texas, USA. Electronic address: XCheng5@mdanderson.org.
The University of Texas MD Anderson Cancer Center · USUniversity of Toledo · US

Funding

User Training and OutreachP30GM124169 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI PAUL David ADAMS, Gregory L Hura · 2017 to 2026
$28.6M
Epigenetic regulations of DNA and histone methylation and deMethylation: Structures and MechanismsR35GM134744 · NIGMS · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI Xiaodong Cheng · 2020 to 2026
$4.5M
NIGMS NIH HHS P30 GM124169NIGMS NIH HHS R35 GM134744
6 · The paper itself

Abstract

RNA methylations of varied RNA species (mRNA, tRNA, rRNA, non-coding RNA) generate a range of modified nucleotides, including N6-methyladenosine. Here we study the enzymology of three human RNA methyltransferases that methylate the adenosine amino group in diverse contexts, when it is: the first transcribed nucleotide after the mRNA cap (PCIF1), at position 1832 of 18S rRNA (MettL5-Trm112 complex), and within a hairpin in the 3' UTR of the S-adenosyl-l-methionine synthetase (MettL16). Among these three enzymes, the catalytic efficiency ranges from PCIF1, with the fastest turnover rate of >230 h

Indexed as

Adaptor Proteins, Signal TransducingAdenosineHumansMethionine AdenosyltransferaseMethylationMethyltransferasesMultiprotein ComplexesNuclear ProteinsRNA, Ribosomal, 18SS-AdenosylmethionineSubstrate SpecificityAdaptor Proteins, Signal TransducingAdenosineMethionine AdenosyltransferaseMethyltransferasesMETTL16 protein, humanMETTL5 protein, humanMultiprotein ComplexesNuclear ProteinsPCIF1 protein, humanRNA, Ribosomal, 18SS-AdenosylmethionineMettL16MettL5-Trm112PCIF1RNA adenine methylation

Identifiers

PMID33428944
PMCPMC7948815
OpenAlexW3118759818

What OpenQuestion 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 OpenQuestion graph.