Evidence map›Paper›PMID 30518535›Full record

ReviewBioscience reports2019

NAD(P)H quinone oxidoreductase (NQO1): an enzyme which needs just enough mobility, in just the right places.

Angel L Pey, Clare F Megarity, David J Timson

Open access · goldAbstract readReview
In one paragraph

Review in Bioscience reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
4.4field-weighted citation impact, top 4% 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

39 citing papers in PubMed, 83 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. The active ingredient of Ginkgo biloba extract (quercetin) improved HIn vitro cellular & developmental biology. Animal · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. In defence of ferroptosis.Signal transduction and targeted therapy · 2025
    Review
  9. Article
  10. Article
  11. Article
  12. Regulation of and challenges in targeting NADNature reviews. Molecular cell biology · 2024
    Review
  13. Review
  14. Review
  15. Article
  16. Review
  17. Article
  18. Review
  19. Review
  20. Article
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 3 institutions in 2 countries.

Angel L PeyDepartment of Physical Chemistry, Faculty of Sciences, University of Granada, Av. Fuentenueva s/n, Granada 18071, Spain.ORCID 0000-0001-7706-3243
Clare F MegarityMedical Biology Centre, School of Biological Sciences, Queen's University Belfast, 97 Lisburn Road, Belfast BT9 7BL, U.K.ORCID 0000-0002-0331-916X
David J TimsonSchool of Pharmacy and Biomolecular Sciences, University of Brighton, Huxley Building, Lewes Road, Brighton BN2 4GJ, U.K. d.timson@brighton.ac.uk.ORCID 0000-0002-0985-8818
Queen's University Belfast · GBUniversidad de Granada · ESUniversity of Brighton · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

NAD(P)H quinone oxidoreductase 1 (NQO1) catalyses the two electron reduction of quinones and a wide range of other organic compounds. Its physiological role is believed to be partly the reduction of free radical load in cells and the detoxification of xenobiotics. It also has non-enzymatic functions stabilising a number of cellular regulators including p53. Functionally, NQO1 is a homodimer with two active sites formed from residues from both polypeptide chains. Catalysis proceeds via a substituted enzyme mechanism involving a tightly bound FAD cofactor. Dicoumarol and some structurally related compounds act as competitive inhibitors of NQO1. There is some evidence for negative cooperativity in quinine oxidoreductases which is most likely to be mediated at least in part by alterations to the mobility of the protein. Human NQO1 is implicated in cancer. It is often over-expressed in cancer cells and as such is considered as a possible drug target. Interestingly, a common polymorphic form of human NQO1, p.P187S, is associated with an increased risk of several forms of cancer. This variant has much lower activity than the wild-type, primarily due to its substantially reduced affinity for FAD which results from lower stability. This lower stability results from inappropriate mobility of key parts of the protein. Thus, NQO1 relies on correct mobility for normal function, but inappropriate mobility results in dysfunction and may cause disease.

Indexed as

Catalytic DomainDicumarolEnzyme InhibitorsEnzyme StabilityFlavin-Adenine DinucleotideGene ExpressionHumansModels, MolecularMutationNAD(P)H Dehydrogenase (Quinone)NeoplasmsProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein Interaction Domains and MotifsProtein MultimerizationDicumarolEnzyme InhibitorsFlavin-Adenine DinucleotideNAD(P)H Dehydrogenase (Quinone)NQO1 protein, humancancer-associated mutationDT-diaphorasenegative cooperativityprotein mobilityquinone oxidoreductase

Identifiers

PMID30518535
PMCPMC6328894
OpenAlexW2902288754

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.