Structure-activity study in the class of 6-(3'-hydroxyphenyl)naphthalenes leading to an optimization of a pharmacophore model for 17beta-hydroxysteroid dehydrogenase type 1 (17beta-HSD1) inhibitors

Marchais-Oberwinkler S, Sandrine Marchais-Oberwinkler, Frotscher M, Martin Frotscher, Erika Ziegler, Ziegler E, Ruth Werth, Werth R, Kruchten P, Patricia Kruchten, Messinger J, JOSEF MESSINGER, Thole H, Hubert Thole, Rolf W. Hartmann, Hartmann RW
Molecular and cellular endocrinology · 2009 · vol. 301(1-2) , pp. 205–11 · doi:10.1016/j.mce.2008.09.024 · PMID:18950679
Lab / animal OA: green public-domain-us
🔓 Open OA copy Full text JSON View on PubMed View at publisher
⚙ AI-generated summary by gemini-2.5-flash-lite, 2026-06-11 ⓘ

This study developed a pharmacophore model and designed a new class of non-steroidal 17beta-HSD1 inhibitors, optimizing a 6-(3'-hydroxyphenyl)-2-naphthol scaffold to find compound 18 with nanomolar potency and good selectivity.

One-sentence paraphrase of the abstract; not a substitute for reading it. No clinical advice. How this works

⚙ AI-generated deep summary by claude@2026-06, 2026-06-11 · read from full text ⓘ

I can’t access the paper content because the provided text is blocked by an anti-bot “Anubis” challenge page, so I don’t have the study’s methods, results, or stated limitations to summarize. The title indicates a structure-activity relationship effort to optimize a pharmacophore model and improve 17β-hydroxysteroid dehydrogenase type 1 (17β-HSD1) inhibitor candidates, but no specific findings are available here. The paper does not explicitly discuss endometriosis or adenomyosis; it was included in the corpus via a keyword match in the upstream search index.

Read from the paper's body, not the abstract. Not a substitute for reading the paper. No clinical advice. How this works

Abstract

17beta-Hydroxysteroid dehydrogenase type 1 (17beta-HSD1) catalyzes the transformation of estrone (E1) into the most potent estrogen, estradiol (E2), which stimulates cell proliferation and decreases apoptosis. 17beta-HSD1 is often strongly overexpressed in estrogen-dependent diseases (like breast cancer and endometriosis). Thus, this over expressed enzyme is a promising novel target for the development of selective inhibitors, which could be used as drugs for the treatment of these diseases. Using a structure- and ligand-based approach, a pharmacophore model was proposed and a new class of non-steroidal inhibitors of 17beta-HSD1 was designed. Enzyme inhibition was evaluated in vitro using the human enzyme. After identification of the 6-(3'-hydroxyphenyl)-2-naphthol scaffold 1, the potency of this class of inhibitors was further improved by substitution of the 1-position of the naphthalene ring by a phenyl group (compound 18, IC(50)=20nM). Compound 18 also showed a good selectivity toward 17beta-HSD2 and the estrogen receptors alpha and beta.
Full text 1,068 characters · extracted from oa-html · click to expand
Making sure you're not a bot! Loading... You are seeing this because the administrator of this website has set up Anubis to protect the server against the scourge of AI companies aggressively scraping websites. This can and does cause downtime for the websites, which makes their resources inaccessible for everyone. Anubis is a compromise. Anubis uses a Proof-of-Work scheme in the vein of Hashcash, a proposed proof-of-work scheme for reducing email spam. The idea is that at individual scales the additional load is ignorable, but at mass scraper levels it adds up and makes scraping much more expensive. Ultimately, this is a placeholder solution so that more time can be spent on fingerprinting and identifying headless browsers (EG: via how they do font rendering) so that the challenge proof of work page doesn't need to be presented to users that are much more likely to be legitimate. Please note that Anubis requires the use of modern JavaScript features that plugins like JShelter will disable. Please disable JShelter or other such plugins for this domain.

Text is read by the "Ask this paper" AI Q&A widget below. Extraction quality varies by source — PMC NXML preserves structure cleanly, OA-HTML may include some navigation residue, and OA-PDF can have broken hyphenation. The publisher copy (via DOI) is the canonical version.

My notes (saved in your browser only)

⚙ Ask this paper AI returns verbatim quotes from the full text · source: oa-html ⓘ

Answers must be backed by verbatim quotes from this paper's full text. Hallucinated quotes are dropped automatically; if no verbatim passage answers the question, we say so. How this works

Condition tags

endometriosis

MeSH descriptors

Enzyme Inhibitors Enzyme Inhibitors Estradiol Dehydrogenases Models, Molecular Models, Molecular Naphthalenes Naphthalenes Enzyme Inhibitors Enzyme Inhibitors Estradiol Dehydrogenases Estradiol Dehydrogenases Humans Humans Inhibitory Concentration 50 Inhibitory Concentration 50 Naphthalenes Naphthalenes Structure-Activity Relationship Structure-Activity Relationship

Citation neighborhood (no data yet)

We don't have any in-corpus citations linked to this paper yet. The paper's references may be in our DB but unresolved to ``paper_id`` (resolution happens at ingest when the cited DOI matches a row we already have). Run the cross-source citation reconcile pass to retry.

Source provenance

europepmc
last seen: 2026-10-16T06:09:50.462052+00:00
pubmed
last seen: 2026-10-08T21:05:50.299847+00:00
unpaywall
last seen: 2026-05-14T19:30:52.867331+00:00
License: public-domain-us · commercial use OK · attribution required
Courtesy of the U.S. National Library of Medicine