Linking of 2-oxoglutarate and substrate binding sites enables potent and highly selective inhibition of JmjC histone demethylases.
Select an isoform: Linking of cosubstrate and substrate binding sites enables highly selective inhibiton of isoforms of human histone lysine demethylases. The results should provide a basis for the development of potent and selective JmjC inhibitors, possibly suitable for clinical use. Copyright © 2...
| Main Authors: | , , , , , , , , , , , , , , |
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| Formato: | Journal article |
| Idioma: | English |
| Publicado em: |
2012
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| _version_ | 1826291906484633600 |
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| author | Woon, E Tumber, A Kawamura, A Hillringhaus, L Ge, W Rose, N Ma, J Chan, M Walport, L Che, K Ng, S Marsden, B Oppermann, U McDonough, M Schofield, C |
| author_facet | Woon, E Tumber, A Kawamura, A Hillringhaus, L Ge, W Rose, N Ma, J Chan, M Walport, L Che, K Ng, S Marsden, B Oppermann, U McDonough, M Schofield, C |
| author_sort | Woon, E |
| collection | OXFORD |
| description | Select an isoform: Linking of cosubstrate and substrate binding sites enables highly selective inhibiton of isoforms of human histone lysine demethylases. The results should provide a basis for the development of potent and selective JmjC inhibitors, possibly suitable for clinical use. Copyright © 2012 WILEY-VCH Verlag GmbH and Co. KGaA, Weinheim. |
| first_indexed | 2024-03-07T03:06:32Z |
| format | Journal article |
| id | oxford-uuid:b2bad656-596e-4a6d-a151-c3aeeb4ad749 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T03:06:32Z |
| publishDate | 2012 |
| record_format | dspace |
| spelling | oxford-uuid:b2bad656-596e-4a6d-a151-c3aeeb4ad7492022-03-27T04:13:46ZLinking of 2-oxoglutarate and substrate binding sites enables potent and highly selective inhibition of JmjC histone demethylases.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:b2bad656-596e-4a6d-a151-c3aeeb4ad749EnglishSymplectic Elements at Oxford2012Woon, ETumber, AKawamura, AHillringhaus, LGe, WRose, NMa, JChan, MWalport, LChe, KNg, SMarsden, BOppermann, UMcDonough, MSchofield, CSelect an isoform: Linking of cosubstrate and substrate binding sites enables highly selective inhibiton of isoforms of human histone lysine demethylases. The results should provide a basis for the development of potent and selective JmjC inhibitors, possibly suitable for clinical use. Copyright © 2012 WILEY-VCH Verlag GmbH and Co. KGaA, Weinheim. |
| spellingShingle | Woon, E Tumber, A Kawamura, A Hillringhaus, L Ge, W Rose, N Ma, J Chan, M Walport, L Che, K Ng, S Marsden, B Oppermann, U McDonough, M Schofield, C Linking of 2-oxoglutarate and substrate binding sites enables potent and highly selective inhibition of JmjC histone demethylases. |
| title | Linking of 2-oxoglutarate and substrate binding sites enables potent and highly selective inhibition of JmjC histone demethylases. |
| title_full | Linking of 2-oxoglutarate and substrate binding sites enables potent and highly selective inhibition of JmjC histone demethylases. |
| title_fullStr | Linking of 2-oxoglutarate and substrate binding sites enables potent and highly selective inhibition of JmjC histone demethylases. |
| title_full_unstemmed | Linking of 2-oxoglutarate and substrate binding sites enables potent and highly selective inhibition of JmjC histone demethylases. |
| title_short | Linking of 2-oxoglutarate and substrate binding sites enables potent and highly selective inhibition of JmjC histone demethylases. |
| title_sort | linking of 2 oxoglutarate and substrate binding sites enables potent and highly selective inhibition of jmjc histone demethylases |
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