Recent progress in histone demethylase inhibitors
There is increasing interest in targeting histone N-methyl-lysine demethylases (KDMs) with small molecules both for the generation of probes for target exploration and for therapeutic purposes. Here we update on previous reviews on the inhibition of the lysine-specific demethylases (LSDs or KDM1s) a...
| Main Authors: | , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
American Chemical Society
2016
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| _version_ | 1797112541096181760 |
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| author | McAllister, T England, KS Hopkinson, R Brennan, PE Kawamura, A Schofield, CJ |
| author_facet | McAllister, T England, KS Hopkinson, R Brennan, PE Kawamura, A Schofield, CJ |
| author_sort | McAllister, T |
| collection | OXFORD |
| description | There is increasing interest in targeting histone N-methyl-lysine demethylases (KDMs) with small molecules both for the generation of probes for target exploration and for therapeutic purposes. Here we update on previous reviews on the inhibition of the lysine-specific demethylases (LSDs or KDM1s) and JmjC families of N-methyl-lysine demethylases (JmjC KDMs, KDM2-7), focusing on the academic and patent literature from 2014 to date. We also highlight recent biochemical, biological, and structural studies which are relevant to KDM inhibitor development. |
| first_indexed | 2024-03-07T08:25:35Z |
| format | Journal article |
| id | oxford-uuid:07826c31-26ad-49b3-9d57-24e8cf161096 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T08:25:35Z |
| publishDate | 2016 |
| publisher | American Chemical Society |
| record_format | dspace |
| spelling | oxford-uuid:07826c31-26ad-49b3-9d57-24e8cf1610962024-02-21T08:42:44ZRecent progress in histone demethylase inhibitorsJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:07826c31-26ad-49b3-9d57-24e8cf161096EnglishSymplectic Elements at OxfordAmerican Chemical Society2016McAllister, TEngland, KSHopkinson, RBrennan, PEKawamura, ASchofield, CJThere is increasing interest in targeting histone N-methyl-lysine demethylases (KDMs) with small molecules both for the generation of probes for target exploration and for therapeutic purposes. Here we update on previous reviews on the inhibition of the lysine-specific demethylases (LSDs or KDM1s) and JmjC families of N-methyl-lysine demethylases (JmjC KDMs, KDM2-7), focusing on the academic and patent literature from 2014 to date. We also highlight recent biochemical, biological, and structural studies which are relevant to KDM inhibitor development. |
| spellingShingle | McAllister, T England, KS Hopkinson, R Brennan, PE Kawamura, A Schofield, CJ Recent progress in histone demethylase inhibitors |
| title | Recent progress in histone demethylase inhibitors |
| title_full | Recent progress in histone demethylase inhibitors |
| title_fullStr | Recent progress in histone demethylase inhibitors |
| title_full_unstemmed | Recent progress in histone demethylase inhibitors |
| title_short | Recent progress in histone demethylase inhibitors |
| title_sort | recent progress in histone demethylase inhibitors |
| work_keys_str_mv | AT mcallistert recentprogressinhistonedemethylaseinhibitors AT englandks recentprogressinhistonedemethylaseinhibitors AT hopkinsonr recentprogressinhistonedemethylaseinhibitors AT brennanpe recentprogressinhistonedemethylaseinhibitors AT kawamuraa recentprogressinhistonedemethylaseinhibitors AT schofieldcj recentprogressinhistonedemethylaseinhibitors |