Evidence map›Paper›PMID 23291110›Full record

ReviewThe Journal of steroid biochemistry and molecular biology2013

The structural biology of oestrogen metabolism.

Mark P Thomas, Barry V L Potter

Abstract readReview
In one paragraph

Review in The Journal of steroid biochemistry and molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 95 papers.

0numbers the graph read from it
0cells of the map it votes in
95citing papers in PubMed
–field-weighted citation impact
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

95 citing papers in PubMed.

  1. Trial
  2. Article
  3. Article
  4. Article
  5. Article
  6. Recent Advances in Therapeutic Potential of Dual-Acting Aromatase/COX-2.Anti-cancer agents in medicinal chemistry · 2026
    Review
  7. Review
  8. Review
  9. Review
  10. The effect of transient sex hormone fluctuations on vascular endothelial function.American journal of physiology. Heart and circulatory physiology · 2025
    Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. Oestrogen Detoxification Ability of White Rot FungusJournal of fungi (Basel, Switzerland) · 2024
    Article
  20. Article

35 more citing papers are in PubMed but not listed here.

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

2 authors.

Mark P ThomasDepartment of Pharmacy & Pharmacology, University of Bath, Claverton Down, Bath, BA2 7AY, UK. Electronic address: m.thomas@bath.ac.uk.
Barry V L Potter

Funding

Wellcome Trust 082837
6 · The paper itself

Abstract

Many enzymes catalyse reactions that have an oestrogen as a substrate and/or a product. The reactions catalysed include aromatisation, oxidation, reduction, sulfonation, desulfonation, hydroxylation and methoxylation. The enzymes that catalyse these reactions must all recognise and bind oestrogen but, despite this, they have diverse structures. This review looks at each of these enzymes in turn, describing the structure and discussing the mechanism of the catalysed reaction. Since oestrogen has a role in many disease states inhibition of the enzymes of oestrogen metabolism may have an impact on the state or progression of the disease and inhibitors of these enzymes are briefly discussed. This article is part of a Special Issue entitled 'CSR 2013'.

Indexed as

17-Hydroxysteroid DehydrogenasesAmino Acid SequenceAnimalsAromataseBiocatalysisCatechol O-MethyltransferaseEstrogensHumansHydroxylationModels, MolecularMolecular Sequence DataMolecular StructureSequence Homology, Amino AcidSteryl-SulfataseSulfotransferases17-Hydroxysteroid DehydrogenasesAromataseCatechol O-MethyltransferaseEstrogensestrone sulfotransferaseSteryl-SulfataseSulfotransferases17β-HSD17β-hydroxysteroid dehydrogenase17β-Hydroxysteroid dehydrogenase3,5-dinitrocatechol3-(((8R,9S,13S,14S,16R,17S)-3,17-dihydroxy-13-methyl-7,8,9,11,12,13,14,15,16,17-decahydro-6H-cyclopenta[a]phenanthren-16-yl)methyl)benzamide3′-phosphoadenosine-5′-phosphate3′-phosphoadenosine-5′-phosphosulfateAromatasecatechol-O-methyl transferaseCOMTdehydroepiandrosterone (sulfate)DHEA(S)DHETNADNCE1(S)E2BE2(S)E3E4ERestetrolestradiol (sulfate)estriolestrogen receptorestrone (sulfate)FAD/FMNFGflavin adenine dinucleotide/flavin mononucleotideformylglycineHFG(S)hydroxyformylglycine (sulfate)mb-COMTmembrane-bound COMTNADP(+)NADPHnicotinamide adenine dinucleotide phosphate (oxidised)nicotinamide adenine dinucleotide phosphate (reduced)O5′-[9-(3,17β-dihydroxy-1,3,5(10)-estratrien-16β-yl)-nonanoyl]adenosineOestrogenPAPPAPSProtein structureReaction mechanismS-adenosyl methionineSAMs-COMTSDRshort-chain dehydrogenase/reductasesoluble COMTSulfataseSulfotransferase

Identifiers

PMID23291110
PMCPMC3866684

What OpenQuestion holds

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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.