Evidence map›Paper›PMID 27537049›Full record

ArticleBioengineered2016

Xanthine dehydrogenase: An old enzyme with new knowledge and prospects.

Cheng-Hua Wang, Chong Zhang, Xin-Hui Xing

Open access · goldAbstract read
In one paragraph

Article in Bioengineered, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

32 citing papers in PubMed, 81 citations in OpenAlex.

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  20. Metabolism and Hepatotoxicity of Pyrazinamide, an Antituberculosis Drug.Drug metabolism and disposition: the biological fate of chemicals · 2021
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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

3 authors at 1 institution in 1 country.

Cheng-Hua Wanga Key Laboratory for Industrial Biocatalysis, Ministry of Education of China, Institute of Biochemical Engineering , Department of Chemical Engineering , Tsinghua University , Beijing , People's Republic of China.
Chong Zhanga Key Laboratory for Industrial Biocatalysis, Ministry of Education of China, Institute of Biochemical Engineering , Department of Chemical Engineering , Tsinghua University , Beijing , People's Republic of China.
Xin-Hui Xinga Key Laboratory for Industrial Biocatalysis, Ministry of Education of China, Institute of Biochemical Engineering , Department of Chemical Engineering , Tsinghua University , Beijing , People's Republic of China.
Tsinghua University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Xanthine dehydrogenase (EC 1.17.1.4, XDH) is a typical and complex molybdenum-containing flavoprotein which has been extensively studied for over 110 years. This enzyme catalyzes the oxidation of purines, pterin and aldehydes with NAD

Indexed as

5'-NucleotidaseAdenosine DeaminaseAldehydesAnimalsBiodegradation, EnvironmentalHumansNitric OxideOxidation-ReductionPhosphorusPterinsPurinesReactive Oxygen SpeciesRibavirinXanthine DehydrogenaseXanthine Oxidase5'-NucleotidaseAdenosine DeaminaseAldehydesNitric OxidePhosphorusPterinspurinePurinesReactive Oxygen SpeciesRibavirinXanthine DehydrogenaseXanthine Oxidaseflavoproteingenetic engineeringnucleosideoxidoreductasepurine catabolismxanthine dehydrogenasexanthine oxidase

Identifiers

PMID27537049
PMCPMC5094624
OpenAlexW2513762283

What OpenQuestion holds

Textmetadata
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.