Inhibition of histone demethylases by 4-carboxy-2,2'-bipyridyl compounds.
Exploiting epigenetics: 2-Oxoglutarate (2OG)-dependent histone lysine demethylases, such as JMJD2E, are potential therapeutic targets in a range of diseases. Through structure-activity relationship studies and analyses, we identified a potent 4-carboxy-2,2'-bipyridyl compound, which inhibits JM...
| Main Authors: | , , , , , , , |
|---|---|
| Format: | Journal article |
| Language: | English |
| Published: |
2011
|
| _version_ | 1797072079974039552 |
|---|---|
| author | Chang, K King, O Tumber, A Woon, E Heightman, T McDonough, M Schofield, C Rose, N |
| author_facet | Chang, K King, O Tumber, A Woon, E Heightman, T McDonough, M Schofield, C Rose, N |
| author_sort | Chang, K |
| collection | OXFORD |
| description | Exploiting epigenetics: 2-Oxoglutarate (2OG)-dependent histone lysine demethylases, such as JMJD2E, are potential therapeutic targets in a range of diseases. Through structure-activity relationship studies and analyses, we identified a potent 4-carboxy-2,2'-bipyridyl compound, which inhibits JMJD2E with an IC50 value of 110nM, representing a 66-fold improvement over the lead compound. These bipyridyl derivatives bind in the 2-oxoglutarate binding site. © 2011 WILEY-VCH Verlag GmbH and Co. KGaA, Weinheim. |
| first_indexed | 2024-03-06T23:02:28Z |
| format | Journal article |
| id | oxford-uuid:629ee095-6c6b-43fb-982f-1bb59851edb4 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T23:02:28Z |
| publishDate | 2011 |
| record_format | dspace |
| spelling | oxford-uuid:629ee095-6c6b-43fb-982f-1bb59851edb42022-03-26T18:07:26ZInhibition of histone demethylases by 4-carboxy-2,2'-bipyridyl compounds.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:629ee095-6c6b-43fb-982f-1bb59851edb4EnglishSymplectic Elements at Oxford2011Chang, KKing, OTumber, AWoon, EHeightman, TMcDonough, MSchofield, CRose, NExploiting epigenetics: 2-Oxoglutarate (2OG)-dependent histone lysine demethylases, such as JMJD2E, are potential therapeutic targets in a range of diseases. Through structure-activity relationship studies and analyses, we identified a potent 4-carboxy-2,2'-bipyridyl compound, which inhibits JMJD2E with an IC50 value of 110nM, representing a 66-fold improvement over the lead compound. These bipyridyl derivatives bind in the 2-oxoglutarate binding site. © 2011 WILEY-VCH Verlag GmbH and Co. KGaA, Weinheim. |
| spellingShingle | Chang, K King, O Tumber, A Woon, E Heightman, T McDonough, M Schofield, C Rose, N Inhibition of histone demethylases by 4-carboxy-2,2'-bipyridyl compounds. |
| title | Inhibition of histone demethylases by 4-carboxy-2,2'-bipyridyl compounds. |
| title_full | Inhibition of histone demethylases by 4-carboxy-2,2'-bipyridyl compounds. |
| title_fullStr | Inhibition of histone demethylases by 4-carboxy-2,2'-bipyridyl compounds. |
| title_full_unstemmed | Inhibition of histone demethylases by 4-carboxy-2,2'-bipyridyl compounds. |
| title_short | Inhibition of histone demethylases by 4-carboxy-2,2'-bipyridyl compounds. |
| title_sort | inhibition of histone demethylases by 4 carboxy 2 2 bipyridyl compounds |
| work_keys_str_mv | AT changk inhibitionofhistonedemethylasesby4carboxy22bipyridylcompounds AT kingo inhibitionofhistonedemethylasesby4carboxy22bipyridylcompounds AT tumbera inhibitionofhistonedemethylasesby4carboxy22bipyridylcompounds AT woone inhibitionofhistonedemethylasesby4carboxy22bipyridylcompounds AT heightmant inhibitionofhistonedemethylasesby4carboxy22bipyridylcompounds AT mcdonoughm inhibitionofhistonedemethylasesby4carboxy22bipyridylcompounds AT schofieldc inhibitionofhistonedemethylasesby4carboxy22bipyridylcompounds AT rosen inhibitionofhistonedemethylasesby4carboxy22bipyridylcompounds |