Evidence map›Paper›PMID 28035004›Full record

ArticleThe Journal of biological chemistry2017

Structural and Kinetic Studies of the Human Nudix Hydrolase MTH1 Reveal the Mechanism for Its Broad Substrate Specificity.

Shaimaa Waz, Teruya Nakamura, Keisuke Hirata, Yukari Koga-Ogawa, Mami Chirifu, Takao Arimori, Taro Tamada, Shinji Ikemizu, Yusaku Nakabeppu, Yuriko Yamagata

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.9field-weighted citation impact, top 13% 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

16 citing papers in PubMed, 38 citations in OpenAlex.

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  6. Review
  7. Visualizing the three-metal-ion-dependent cleavage of a mutagenic nucleotide.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  8. Visualization of mutagenic nucleotide processing byProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
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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

10 authors at 3 institutions in 1 country.

Shaimaa WazFrom the Graduate School of Pharmaceutical Sciences, Kumamoto University, Kumamoto 862-0973.
Teruya NakamuraFrom the Graduate School of Pharmaceutical Sciences, Kumamoto University, Kumamoto 862-0973.
Keisuke HirataFrom the Graduate School of Pharmaceutical Sciences, Kumamoto University, Kumamoto 862-0973.
Yukari Koga-OgawaFrom the Graduate School of Pharmaceutical Sciences, Kumamoto University, Kumamoto 862-0973.
Mami ChirifuFrom the Graduate School of Pharmaceutical Sciences, Kumamoto University, Kumamoto 862-0973.
Takao Arimorithe Quantum Beam Science Research Directorate, National Institutes for Quantum and Radiological Science and Technology, Tokai, Ibaraki 319-1106, and.
Taro Tamadathe Quantum Beam Science Research Directorate, National Institutes for Quantum and Radiological Science and Technology, Tokai, Ibaraki 319-1106, and.
Shinji IkemizuFrom the Graduate School of Pharmaceutical Sciences, Kumamoto University, Kumamoto 862-0973.
Yusaku Nakabepputhe Medical Institute of Bioregulation, Kyushu University, Fukuoka 812-8582, Japan.
Yuriko YamagataFrom the Graduate School of Pharmaceutical Sciences, Kumamoto University, Kumamoto 862-0973, yamagata@gpo.kumamoto-u.ac.jp.
Kumamoto University · JPNational Institutes for Quantum and Radiological Science and Technology · JPKyushu University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The human MutT homolog 1 (hMTH1, human NUDT1) hydrolyzes oxidatively damaged nucleoside triphosphates and is the main enzyme responsible for nucleotide sanitization. hMTH1 recently has received attention as an anticancer target because hMTH1 blockade leads to accumulation of oxidized nucleotides in the cell, resulting in mutations and death of cancer cells. Unlike

Indexed as

Crystallography, X-RayDNA Repair EnzymesHumansKineticsMutationPhosphoric Monoester HydrolasesProtein ConformationSubstrate Specificity8-oxodGTPaseDNA Repair EnzymesPhosphoric Monoester Hydrolases8-oxoguanine (8-oxoG)crystallographyenzyme catalysisenzyme kineticsenzyme mechanismenzyme mutationsubstrate specificity

Identifiers

PMID28035004
PMCPMC5314174
OpenAlexW2565494516

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.