Evidence map›Paper›PMID 17067289›Full record

ArticleThe Biochemical journal2007

Structural and biochemical characterization of human orphan DHRS10 reveals a novel cytosolic enzyme with steroid dehydrogenase activity.

Petra Lukacik, Brigitte Keller, Gabor Bunkoczi, Kathryn L Kavanagh, Kathryn Kavanagh, Wen Hwa Lee, Wen Hwa Lee, Jerzy Adamski, Udo Oppermann

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
4.8field-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

36 citing papers in PubMed, 104 citations in OpenAlex.

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  10. Glial expression of a steroidogenic enzyme underlies natural variation in hitchhiking behavior.Proceedings of the National Academy of Sciences of the United States of America · 2024
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  16. Association of Coding Variants in Hydroxysteroid 17-beta Dehydrogenase 14 (Journal of the American Society of Nephrology : JASN · 2021
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4 · The record

Corrections and comments

  • Erratum issued
    Kavanagh, Kathryn [Kavanagh, Kathryn L]; Hwa, Lee Wen [corrected to Lee, Wen Hwa]
5 · Who and what money

Authors and funding

9 authors at 1 institution in 1 country.

Petra LukacikStructural Genomics Consortium, University of Oxford, Oxford OX3 7LD, UK. lukacikp@niddk.nih.gov
Brigitte Keller
Gabor Bunkoczi
Kathryn L Kavanagh
Kathryn Kavanagh
Wen Hwa Lee
Wen Hwa Lee
Jerzy Adamski
Udo Oppermann
Institute of Groundwater Ecology · DE

Funding

Wellcome Trust
6 · The paper itself

Abstract

To this day, a significant proportion of the human genome remains devoid of functional characterization. In this study, we present evidence that the previously functionally uncharacterized product of the human DHRS10 gene is endowed with 17beta-HSD (17beta-hydroxysteroid dehydrogenase) activity. 17beta-HSD enzymes are primarily involved in the metabolism of steroids at the C-17 position and also of other substrates such as fatty acids, prostaglandins and xenobiotics. In vitro, DHRS10 converts NAD+ into NADH in the presence of oestradiol, testosterone and 5-androstene-3beta,17beta-diol. Furthermore, the product of oestradiol oxidation, oestrone, was identified in intact cells transfected with a construct plasmid encoding the DHRS10 protein. In situ fluorescence hybridization studies have revealed the cytoplasmic localization of DHRS10. Along with tissue expression data, this suggests a role for DHRS10 in the local inactivation of steroids in the central nervous system and placenta. The crystal structure of the DHRS10 apoenzyme exhibits secondary structure of the SDR (short-chain dehydrogenase/reductase) family: a Rossmann-fold with variable loops surrounding the active site. It also reveals a broad and deep active site cleft into which NAD+ and oestradiol can be docked in a catalytically competent orientation.

Indexed as

17-Hydroxysteroid DehydrogenasesAmino Acid SequenceBinding SitesCell LineCrystallography, X-RayCytosolGene ExpressionHumansKineticsLigandsModels, MolecularMolecular Sequence DataNADOrgan SpecificityOxidation-ReductionProtein Structure, Secondary17-Hydroxysteroid DehydrogenasesHSD17B14 protein, humanLigandsNAD

Identifiers

PMID17067289
PMCPMC1863559
OpenAlexW2065619933

What OpenQuestion holds

Textmetadata
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.