Evidence map›Paper›PMID 28236663›Full record

ArticleThe FEBS journal2017

Catalytic competence, structure and stability of the cancer-associated R139W variant of the human NAD(P)H:quinone oxidoreductase 1 (NQO1).

Wolf-Dieter Lienhart, Emilia Strandback, Venugopal Gudipati, Karin Koch, Alexandra Binter, Michael K Uhl, David M Rantasa, Benjamin Bourgeois, Tobias Madl, Klaus Zangger and 2 more

Open access · hybridAbstract read
In one paragraph

Article in The FEBS journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
3.2field-weighted citation impact, top 9% 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

17 citing papers in PubMed, 33 citations in OpenAlex.

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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

12 authors at 3 institutions in 1 country.

Wolf-Dieter LienhartInstitute of Biochemistry, Graz University of Technology, Austria.
Emilia StrandbackInstitute of Biochemistry, Graz University of Technology, Austria.
Venugopal GudipatiInstitute of Biochemistry, Graz University of Technology, Austria.
Karin KochInstitute of Biochemistry, Graz University of Technology, Austria.
Alexandra BinterInstitute of Biochemistry, Graz University of Technology, Austria.
Michael K UhlInstitute of Molecular Biosciences, University of Graz, Austria.
David M RantasaInstitute of Biochemistry, Graz University of Technology, Austria.
Benjamin BourgeoisInstitute of Molecular Biology and Biochemistry, Medical University of Graz, Austria.
Tobias MadlInstitute of Molecular Biology and Biochemistry, Medical University of Graz, Austria.
Klaus ZanggerInstitute of Chemistry, University of Graz, Austria.
Karl GruberInstitute of Molecular Biosciences, University of Graz, Austria.
Peter MacherouxInstitute of Biochemistry, Graz University of Technology, Austria.
Graz University of Technology · ATUniversity of Graz · ATMedical University of Graz · AT

Funding

Austrian Science Fund FWF P 28854
6 · The paper itself

Abstract

The human NAD(P)H:quinone oxidoreductase 1 (NQO1; EC1.6.99.2) is an essential enzyme in the antioxidant defence system. Furthermore, NQO1 protects tumour suppressors like p53, p33

Indexed as

CalorimetryCatalysisHumansKineticsNAD(P)H Dehydrogenase (Quinone)NeoplasmsScattering, Small AngleX-Ray DiffractionNAD(P)H Dehydrogenase (Quinone)NQO1 protein, humancancercrystal structureenzyme kineticsmicrocalorimetryNMR-spectroscopysingle nucleotide polymorphism

Identifiers

PMID28236663
PMCPMC6250432
OpenAlexW2590434670

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.