Evidence map›Paper›PMID 22989153›Full record

ArticleBiochemistry2012

Human NAD(P)H:quinone oxidoreductase type I (hNQO1) activation of quinone propionic acid trigger groups.

Maria F Mendoza, Nicole M Hollabaugh, Suraj U Hettiarachchi, Robin L McCarley

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.6field-weighted citation impact, top 12% 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

19 citing papers in PubMed, 72 citations in OpenAlex.

  1. Article
  2. Switching on Supramolecular DNA Junction Binding Using a Human Enzyme.Angewandte Chemie (International ed. in English) · 2025
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  4. Roles of Ferredoxin-NADPAntioxidants (Basel, Switzerland) · 2022
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  7. Review
  8. Aerobic Cytotoxicity of AromaticInternational journal of molecular sciences · 2020
    Article
  9. Article
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  11. Article
  12. Hypoxia-activated prodrugs and redox-responsive nanocarriers.International journal of nanomedicine · 2018
    Review
  13. Stimuli-responsive liposomes for drug delivery.Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnology · 2017
    Review
  14. Article
  15. Article
  16. Article
  17. Siderophore-fluoroquinolone conjugates containing potential reduction-triggered linkers for drug release: synthesis and antibacterial activity.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2015
    Article
  18. Article
  19. 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

4 authors at 1 institution in 1 country.

Maria F MendozaDepartment of Chemistry, Louisiana State University, 232 Choppin Hall, Baton Rouge, Louisiana 70803-1804, USA.
Nicole M Hollabaugh
Suraj U Hettiarachchi
Robin L McCarley
Louisiana State University · US

Funding

ZERNIKE PHASE PLATE CRYOEM IN OKAZAKIP41RR002250 · NCRR · UNIVERSITY OF ARIZONA · PI CHIU, WAH · 1985 to 2011
$22.1M
Reductase Enzyme-responsive, Self-immolative NanovehiclesR21CA135585 · NCI · LOUISIANA STATE UNIV A&M COL BATON ROUGE · PI MCCARLEY, ROBIN LINDSEY · 2009 to 2010
$326k
NCI NIH HHS 5R21CA135585NCI NIH HHS R21 CA135585NCRR NIH HHS P41 RR002250
6 · The paper itself

Abstract

NAD(P)H:quinone oxidoreductase type I (NQO1) is a target enzyme for triggered delivery of drugs at inflamed tissue and tumor sites, particularly those that challenge traditional therapies. Prodrugs, macromolecules, and molecular assemblies possessing trigger groups that can be cleaved by environmental stimuli are vehicles with the potential to yield active drug only at prescribed sites. Furthermore, quinone propionic acids (QPAs) covalently attached to prodrugs or liposome surfaces can be removed by application of a reductive trigger stimulus, such as that from NQO1; their rates of reductive activation should be tunable via QPA structure. We explored in detail the recombinant human NAD(P)H:quinone oxidoreductase type I (rhNQO1)-catalyzed NADH reduction of a family of substituted QPAs and obtained high precision kinetic parameters. It is found that small changes in QPA structure-in particular, single atom and function group substitutions on the quinone ring at R(1)-lead to significant impacts on the Michaelis constant (K(m)), maximum velocity (V(max)), catalytic constant (k(cat)), and catalytic efficiency (k(cat)/K(m)). Molecular docking simulations demonstrate that alterations in QPA structure result in large changes in QPA alignment and placement with respect to the flavin isoalloxazine ring in the active site of rhNQO1; a qualitative relationship exists between the kinetic parameters and the depth of QPA penetration into the rhNQO1 active site. From a quantitative perspective, a very good correlation is observed between log(k(cat)/K(m)) and the molecular-docking-derived distance between the flavin hydride donor site and quinone hydride acceptor site in the QPAs, an observation that is in agreement with developing theories. The comprehensive kinetic and molecular modeling knowledge obtained for the interaction of recombinant human NQO1 with the quinone propionic acid analogues provides insight into the design and implementation of the QPA trigger groups for drug delivery applications.

Indexed as

Catalytic DomainKineticsModels, MolecularMolecular StructureNAD(P)H Dehydrogenase (Quinone)PropionatesProtein BindingQuinonesRecombinant ProteinsSubstrate SpecificityNAD(P)H Dehydrogenase (Quinone)NQO1 protein, humanPropionatespropionic acidQuinonesRecombinant Proteins

Identifiers

PMID22989153
PMCPMC3525107
OpenAlexW2013225650

What OpenQuestion holds

Textmetadata
LicenceTDM
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.