Investigating D-lysine stereochemistry for epigenetic methylation, demethylation and recognition
Histone lysine methylation is regulated by Nε-methyltransferases, demethylases, and Nε-methyl lysine binding proteins. Thermodynamic, catalytic and computational studies were carried out to investigate the interaction of three epigenetic protein classes with synthetic histone substrates containing l...
| Prif Awduron: | , , , , , , , , , , , , , |
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| Fformat: | Journal article |
| Iaith: | English |
| Cyhoeddwyd: |
Royal Society of Chemistry
2017
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| _version_ | 1826264934933069824 |
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| author | Belle, R Al Temimi, A Kumar, K Pieters, B Tumber, A Dunford, J Johansson, C Oppermann, U Brown, T Schofield, C Hopkinson, R Paton, R Kawamura, A Mecinović, J |
| author_facet | Belle, R Al Temimi, A Kumar, K Pieters, B Tumber, A Dunford, J Johansson, C Oppermann, U Brown, T Schofield, C Hopkinson, R Paton, R Kawamura, A Mecinović, J |
| author_sort | Belle, R |
| collection | OXFORD |
| description | Histone lysine methylation is regulated by Nε-methyltransferases, demethylases, and Nε-methyl lysine binding proteins. Thermodynamic, catalytic and computational studies were carried out to investigate the interaction of three epigenetic protein classes with synthetic histone substrates containing l- and d-lysine residues. The results reveal that out of the three classes, Nε-methyl lysine binding proteins are superior in accepting lysines with the d-configuration. |
| first_indexed | 2024-03-06T20:15:46Z |
| format | Journal article |
| id | oxford-uuid:2c17b09b-ec29-44cd-91a6-ea1241e7b638 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T20:15:46Z |
| publishDate | 2017 |
| publisher | Royal Society of Chemistry |
| record_format | dspace |
| spelling | oxford-uuid:2c17b09b-ec29-44cd-91a6-ea1241e7b6382022-03-26T12:35:00ZInvestigating D-lysine stereochemistry for epigenetic methylation, demethylation and recognitionJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:2c17b09b-ec29-44cd-91a6-ea1241e7b638EnglishSymplectic Elements at OxfordRoyal Society of Chemistry2017Belle, RAl Temimi, AKumar, KPieters, BTumber, ADunford, JJohansson, COppermann, UBrown, TSchofield, CHopkinson, RPaton, RKawamura, AMecinović, JHistone lysine methylation is regulated by Nε-methyltransferases, demethylases, and Nε-methyl lysine binding proteins. Thermodynamic, catalytic and computational studies were carried out to investigate the interaction of three epigenetic protein classes with synthetic histone substrates containing l- and d-lysine residues. The results reveal that out of the three classes, Nε-methyl lysine binding proteins are superior in accepting lysines with the d-configuration. |
| spellingShingle | Belle, R Al Temimi, A Kumar, K Pieters, B Tumber, A Dunford, J Johansson, C Oppermann, U Brown, T Schofield, C Hopkinson, R Paton, R Kawamura, A Mecinović, J Investigating D-lysine stereochemistry for epigenetic methylation, demethylation and recognition |
| title | Investigating D-lysine stereochemistry for epigenetic methylation, demethylation and recognition |
| title_full | Investigating D-lysine stereochemistry for epigenetic methylation, demethylation and recognition |
| title_fullStr | Investigating D-lysine stereochemistry for epigenetic methylation, demethylation and recognition |
| title_full_unstemmed | Investigating D-lysine stereochemistry for epigenetic methylation, demethylation and recognition |
| title_short | Investigating D-lysine stereochemistry for epigenetic methylation, demethylation and recognition |
| title_sort | investigating d lysine stereochemistry for epigenetic methylation demethylation and recognition |
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