Evidence map›Paper›PMID 34337952›Full record

ArticleJournal of medicinal chemistry2021

Xanthine Derivatives Reveal an Allosteric Binding Site in Methylenetetrahydrofolate Dehydrogenase 2 (MTHFD2).

Lung-Chun Lee, Yi-Hui Peng, Hsin-Huei Chang, Tsu Hsu, Cheng-Tai Lu, Chih-Hsiang Huang, Ching-Cheng Hsueh, Fang-Chun Kung, Ching-Chuan Kuo, Weir-Torn Jiaang and 1 more

Open access · hybridAbstract read
In one paragraph

Article in Journal of medicinal chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.1field-weighted citation impact, top 22% 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

10 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. MTHFD2: a promising metabolic checkpoint for diseases.Journal of translational medicine · 2026
    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

11 authors at 1 institution in 1 country.

Lung-Chun LeeInstitute of Biotechnology and Pharmaceutical Research, National Health Research Institutes, 35, Keyan Road, Zhunan Town, Miaoli County 350 Taiwan, ROC.
Yi-Hui PengInstitute of Biotechnology and Pharmaceutical Research, National Health Research Institutes, 35, Keyan Road, Zhunan Town, Miaoli County 350 Taiwan, ROC.
Hsin-Huei ChangInstitute of Biotechnology and Pharmaceutical Research, National Health Research Institutes, 35, Keyan Road, Zhunan Town, Miaoli County 350 Taiwan, ROC.
Tsu HsuInstitute of Biotechnology and Pharmaceutical Research, National Health Research Institutes, 35, Keyan Road, Zhunan Town, Miaoli County 350 Taiwan, ROC.
Cheng-Tai LuInstitute of Biotechnology and Pharmaceutical Research, National Health Research Institutes, 35, Keyan Road, Zhunan Town, Miaoli County 350 Taiwan, ROC.
Chih-Hsiang HuangInstitute of Biotechnology and Pharmaceutical Research, National Health Research Institutes, 35, Keyan Road, Zhunan Town, Miaoli County 350 Taiwan, ROC.
Ching-Cheng HsuehInstitute of Biotechnology and Pharmaceutical Research, National Health Research Institutes, 35, Keyan Road, Zhunan Town, Miaoli County 350 Taiwan, ROC.
Fang-Chun KungInstitute of Biotechnology and Pharmaceutical Research, National Health Research Institutes, 35, Keyan Road, Zhunan Town, Miaoli County 350 Taiwan, ROC.
Ching-Chuan KuoInstitute of Biotechnology and Pharmaceutical Research, National Health Research Institutes, 35, Keyan Road, Zhunan Town, Miaoli County 350 Taiwan, ROC.
Weir-Torn JiaangInstitute of Biotechnology and Pharmaceutical Research, National Health Research Institutes, 35, Keyan Road, Zhunan Town, Miaoli County 350 Taiwan, ROC.ORCID 0000-0001-8781-3538
Su-Ying WuInstitute of Biotechnology and Pharmaceutical Research, National Health Research Institutes, 35, Keyan Road, Zhunan Town, Miaoli County 350 Taiwan, ROC.ORCID 0000-0003-2816-6961
National Health Research Institutes · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Methylenetetrahydrofolate dehydrogenase 2 (MTHFD2) plays an important role in one-carbon metabolism. The MTHFD2 gene is upregulated in various cancers but very low or undetectable in normal proliferating cells, and therefore a potential target for cancer treatment. In this study, we present the structure of MTHFD2 in complex with xanthine derivative

Indexed as

Allosteric SiteAminohydrolasesDose-Response Relationship, DrugEnzyme InhibitorsHumansMethylenetetrahydrofolate Dehydrogenase (NADP)Models, MolecularMolecular StructureMultifunctional EnzymesStructure-Activity RelationshipXanthineAminohydrolasesEnzyme InhibitorsMethylenetetrahydrofolate Dehydrogenase (NADP)MTHFD2 protein, humanMultifunctional EnzymesXanthine

Identifiers

PMID34337952
PMCPMC8389891
OpenAlexW3189191479

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.