Evidence map›Paper›PMID 31605637›Full record

ArticleFEBS letters2020

A small molecule chaperone rescues the stability and activity of a cancer-associated variant of NAD(P)H:quinone oxidoreductase 1 in vitro.

Emilia Strandback, Wolf-Dieter Lienhart, Altijana Hromic-Jahjefendic, Benjamin Bourgeois, Anja Högler, Daniel Waltenstorfer, Andreas Winkler, Klaus Zangger, Tobias Madl, Karl Gruber and 1 more

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in FEBS letters, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.7field-weighted citation impact, top 35% 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

6 citing papers in PubMed, 12 citations in OpenAlex.

  1. Review
  2. iScience · 2025
    Article
  3. Article
  4. Impact of NQO1 dysregulation in CNS disorders.Journal of translational medicine · 2024
    Review
  5. Galactosemia: Towards Pharmacological Chaperones.Journal of personalized medicine · 2021
    Review
  6. 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

11 authors at 3 institutions in 2 countries.

Emilia StrandbackInstitute of Biochemistry, Graz University of Technology, Austria.
Wolf-Dieter LienhartInstitute of Biochemistry, Graz University of Technology, Austria.
Altijana Hromic-JahjefendicInstitute of Molecular Biosciences, University of Graz, Austria.
Benjamin BourgeoisGottfried Schatz Research Center for Cell Signaling, Metabolism and Aging, Molecular Biology and Biochemistry, Medical University of Graz, Austria.
Anja HöglerInstitute of Biochemistry, Graz University of Technology, Austria.
Daniel WaltenstorferInstitute of Biochemistry, Graz University of Technology, Austria.
Andreas WinklerInstitute of Biochemistry, Graz University of Technology, Austria.
Klaus ZanggerInstitute of Chemistry, University of Graz, Austria.
Tobias MadlGottfried Schatz Research Center for Cell Signaling, Metabolism and Aging, Molecular Biology and Biochemistry, Medical University of Graz, Austria.ORCID 0000-0002-9725-5231
Karl GruberInstitute of Molecular Biosciences, University of Graz, Austria.
Peter MacherouxInstitute of Biochemistry, Graz University of Technology, Austria.ORCID 0000-0002-0242-454X
Graz University of Technology · ATUniversity of Graz · ATMedical University of Graz · AT

Funding

Austrian Science Fund FWF I 3792Austrian Science Fund FWF P 22361Austrian Science Fund FWF P 28854
6 · The paper itself

Abstract

NAD(P)H:quinone oxidoreductase 1 (NQO1) is a human FAD-dependent enzyme that plays a crucial role in the antioxidant defense system. A naturally occurring single-nucleotide polymorphism (NQO1*2) in the NQO1 gene leads to an amino acid substitution (P187S), which severely compromises the activity and stability of the enzyme. The NQO1*2 genotype has been linked to a higher risk for several types of cancer and poor survival rate after anthracycline-based chemotherapy. In this study, we show that a small molecular chaperone (N-(2-bromophenyl)pyrrolidine-1-sulfonamide) repopulates the native wild-type conformation. As a consequence of the stabilizing effect, the enzymatic activity of the P187S variant protein is strongly improved in the presence of the molecular chaperone in vitro.

Indexed as

MutationAmino Acid SequenceDrug Evaluation, PreclinicalEnzyme ActivationEnzyme StabilityLigandsMolecular Docking SimulationMutant ProteinsNAD(P)H Dehydrogenase (Quinone)NeoplasmsProtein ConformationLigandsMutant ProteinsNAD(P)H Dehydrogenase (Quinone)cancerchemical chaperonechemotherapeuticsquinonesingle-nucleotide polymorphism

Identifiers

PMID31605637
PMCPMC7027498
OpenAlexW2979711166

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.