Evidence map›Paper›PMID 21272640›Full record

ReviewThe Journal of steroid biochemistry and molecular biology2011

Human hydroxysteroid dehydrogenases and pre-receptor regulation: insights into inhibitor design and evaluation.

Trevor M Penning

Open access · greenAbstract readReview
In one paragraph

Review in The Journal of steroid biochemistry and molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

24 citing papers in PubMed, 50 citations in OpenAlex.

  1. Review
  2. Chronic alcohol intake elicits distinct multi-omic profiles in the liverbioRxiv : the preprint server for biology · 2025
    Article
  3. Review
  4. Article
  5. Review
  6. Gut feelings about bacterial steroid-17,20-desmolase.Molecular and cellular endocrinology · 2021
    Review
  7. The Biosynthesis of Enzymatically Oxidized Lipids.Frontiers in endocrinology · 2020
    Review
  8. Article
  9. Article
  10. Article
  11. Virtual screening applications in short-chain dehydrogenase/reductase research.The Journal of steroid biochemistry and molecular biology · 2017
    Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Review
  20. 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

1 author at 1 institution in 1 country.

Trevor M PenningCenter of Excellence in Environmental Toxicology, Department of Pharmacology, University of Pennsylvania School of Medicine, Philadelphia, PA 19104-6084, USA. penning@upenn.edu
University of Pennsylvania · US

Funding

Translational Research Support CoreP30ES013508 · NIEHS · UNIVERSITY OF PENNSYLVANIA · PI Trevor M Penning · 2006 to 2026
$35.3M
Structure/Function of Steroid Transforming AKR'sR01DK047015 · NIDDK · UNIVERSITY OF PENNSYLVANIA · PI PENNING, TREVOR M · 1994 to 2011
$3.2M
Human Aldo Keto Reductases and Steroid Hormone ActionR01CA090744 · NCI · UNIVERSITY OF PENNSYLVANIA · PI PENNING, TREVOR M · 2001 to 2011
$3.1M
NCI NIH HHS R01 CA090744NCI NIH HHS R01CA90744NIDDK NIH HHS R01 DK047015NIDDK NIH HHS R01-DK47015NIEHS NIH HHS P30 ES013508NIEHS NIH HHS P30-ES013508-05
6 · The paper itself

Abstract

Hydroxysteroid dehydrogenases (HSDs) represent a major class of NAD(P)(H) dependent steroid hormone oxidoreductases involved in the pre-receptor regulation of hormone action. This is achieved by HSDs working in pairs so that they can interconvert ketosteroids with hydroxysteroids resulting in a change in ligand potency for nuclear receptors. HSDs belong to two protein superfamilies the aldo-keto reductases and the short-chain dehydrogenase/reductases. In humans, many of the important enzymes have been thoroughly characterized including the elucidation of their three-dimensional structures. Because these enzymes play fundamental roles in steroid hormone action they can be considered to be drug targets for a variety of steroid driven diseases, e.g. metabolic syndrome and obesity, inflammation, and hormone dependent malignancies of the endometrium, prostate and breast. This article will review how fundamental knowledge of these enzymes can be exploited in the development of isoform specific HSD inhibitors from both protein superfamilies. Article from the Special issue on Targeted Inhibitors.

Indexed as

Drug DesignHumansHydroxysteroid DehydrogenasesModels, MolecularMolecular StructureProtein ConformationReceptors, SteroidSteroidsThermodynamicsHydroxysteroid DehydrogenasesReceptors, SteroidSteroids

Identifiers

PMID21272640
PMCPMC3104102
OpenAlexW2051741107

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.