Search: onr:"swepub:oai:DiVA.org:su-168366" >
Potent inhibitors o...
-
Lindström, HelenaStockholms universitet,Institutionen för biokemi och biofysik
(author)
Potent inhibitors of equine steroid isomerase EcaGST A3-3
- Article/chapterEnglish2019
Publisher, publication year, extent ...
-
2019-03-21
-
Public Library of Science (PLoS),2019
-
printrdacarrier
Numbers
-
LIBRIS-ID:oai:DiVA.org:su-168366
-
https://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-168366URI
-
https://doi.org/10.1371/journal.pone.0214160DOI
Supplementary language notes
-
Language:English
-
Summary in:English
Part of subdatabase
Classification
-
Subject category:ref swepub-contenttype
-
Subject category:art swepub-publicationtype
Notes
-
Equine glutathione transferase A3-3 (EcaGST A3-3) belongs to the superfamily of detoxication enzymes found in all higher organisms. However, it is also the most efficient steroid double-bond isomerase known in mammals. Equus ferus caballus shares the steroidogenic pathway with Homo sapiens, which makes the horse a suitable animal model for investigations of human steroidogenesis. Inhibition of the enzyme has potential for treatment of steroid-hormone-dependent disorders. Screening of a library of FDA-approved drugs identified 16 out of 1040 compounds, which at 10 mu M concentration afforded at least 50% inhibition of EcaGST A3-3. The most potent inhibitors, anthralin, sennoside A, tannic acid, and ethacrynic acid, were characterized by IC50 values in the submicromolar range when assayed with the natural substrate Delta(5)-androstene-3,17-dione.
Subject headings and genre
Added entries (persons, corporate bodies, meetings, titles ...)
-
Mazari, Aslam M. A.Stockholms universitet,Institutionen för biokemi och biofysik
(author)
-
Musdal, YamanStockholms universitet,Institutionen för biokemi och biofysik
(author)
-
Mannervik, BengtStockholms universitet,Institutionen för biokemi och biofysik(Swepub:su)bmann
(author)
-
Stockholms universitetInstitutionen för biokemi och biofysik
(creator_code:org_t)
Related titles
-
In:PLOS ONE: Public Library of Science (PLoS)14:31932-6203
Internet link
Find in a library
-
PLOS ONE
(Search for host publication in LIBRIS)
To the university's database