Evidence map›Paper›PMID 33774477›Full record

ReviewRedox biology2021

The diverse functionality of NQO1 and its roles in redox control.

David Ross, David Siegel

Open access · goldAbstract readReview
In one paragraph

Review in Redox biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 259 papers, 3 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
259citing papers in PubMed, 3 pooled it
24.3field-weighted citation impact, top 1% 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

259 citing papers in PubMed, 3 syntheses or guidelines pooled it, 433 citations in OpenAlex.

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199 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

2 authors at 1 institution in 1 country.

David RossDepartment of Pharmaceutical Sciences, Skaggs School of Pharmacy and Pharmaceutical Sciences, University of Colorado Anschutz Medical Campus, Aurora, CO, 80045, USA. Electronic address: david.ross@cuanschutz.edu.
David SiegelDepartment of Pharmaceutical Sciences, Skaggs School of Pharmacy and Pharmaceutical Sciences, University of Colorado Anschutz Medical Campus, Aurora, CO, 80045, USA.
University of Colorado Anschutz Medical Campus · US

Funding

Regulation of insulin signaling and sensitivity by the xenobiotic metabolizing enzyme NQO1R01DK109964 · NIDDK · UNIVERSITY OF COLORADO DENVER · PI DE CABO, RAFAEL, FRITZ, KRISTOFER S · 2017 to 2021
$1.9M
NIDDK NIH HHS R01 DK109964
6 · The paper itself

Abstract

In this review, we summarize the multiple functions of NQO1, its established roles in redox processes and potential roles in redox control that are currently emerging. NQO1 has attracted interest due to its roles in cell defense and marked inducibility during cellular stress. Exogenous substrates for NQO1 include many xenobiotic quinones. Since NQO1 is highly expressed in many solid tumors, including via upregulation of Nrf2, the design of compounds activated by NQO1 and NQO1-targeted drug delivery have been active areas of research. Endogenous substrates have also been proposed and of relevance to redox stress are ubiquinone and vitamin E quinone, components of the plasma membrane redox system. Established roles for NQO1 include a superoxide reductase activity, NAD

Indexed as

NAD(P)H Dehydrogenase (Quinone)NeoplasmsAntioxidantsHumansOxidation-ReductionQuinonesAntioxidantsNAD(P)H Dehydrogenase (Quinone)NQO1 protein, humanQuinonesDT-DiaphoraseNQO1Nrf2Oxidative stressQuinoneRedox switch

Identifiers

PMID33774477
PMCPMC8027776
OpenAlexW3137878085

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.