Evidence map›Paper›PMID 23604305›Full record

ArticleAge1997

Xanthine dehydrogenase/xanthine oxidase and oxidative stress.

H Y Chung, B S Baek, S H Song, M S Kim, J I Huh, K H Shim, K W Kim, K H Lee

Open access · bronzeAbstract read
In one paragraph

Article in Age, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed, 2 pooled it
0.8field-weighted citation impact, top 33% 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

76 citing papers in PubMed, 2 syntheses or guidelines pooled it, 190 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
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16 more citing papers are in PubMed but not listed here.

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

8 authors at 1 institution in 1 country.

H Y Chung
B S Baek
S H Song
M S Kim
J I Huh
K H Shim
K W Kim
K H Lee
Pusan National University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Xanthine dehydrogenase (XDH) and xanthine oxidase (XOD) are single-gene products that exist in separate but interconvertible forms. XOD utilizes hypoxanthine or xanthine as a substrate and O2 as a cofactor to produce superoxide (·O2 (-)) and uric acid. XDH acts on these same substrates but utilizes NAD as a cofactor to produce NADH instead of ·O2 (-) and uric acid. XOD has been proposed as a source of oxygen radicals in polymorphonuclear, endothelial, epithelial, and connective tissue cells. However, several questions remain about the physiological significance and functions of XOD on aging and oxidative stress. XOD is reported to play an important role in cellular oxidative status, detoxification of aldehydes, oxidative injury in ischemia-reperfusion, and neutrophil mediation. For example, XOD may serve as a messenger or mediator in the activation of neutrophil, T cell, cytokines, or transcription in defense mechanisms rather than as a free radical generator of tissue damage. Emerging evidence on the synergistic interactions of ·O2 (-), a toxic product of XOD and nitric oxide, may be another illustration of XOD involvement in tissue injury and cytotoxicity in an emergent condition such as ischemia or inflammation.

Indexed as

AgingOxidative stressXanthine dehydrogenaseXanthine oxidase

Identifiers

PMID23604305
PMCPMC3455892
OpenAlexW1977223820

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.