Journal article
Arginine demethylation is catalysed by a subset of JmjC histone lysine demethylases.
- Abstract:
-
While the oxygen-dependent reversal of lysine N(ɛ)-methylation is well established, the existence of bona fide N(ω)-methylarginine demethylases (RDMs) is controversial. Lysine demethylation, as catalysed by two families of lysine demethylases (the flavin-dependent KDM1 enzymes and the 2-oxoglutarate- and oxygen-dependent JmjC KDMs, respectively), proceeds via oxidation of the N-methyl group, resulting in the release of formaldehyde. Here we report detailed biochemical studies clearly demonstr...
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- Publication status:
- Published
- Peer review status:
- Peer reviewed
Actions
Authors
Funding
+ Biotechnology and Biological Sciences Research Council
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Funding agency for:
Walport, L
Grant:
studentships
+ Biotechnology and Biological Sciences Research Council
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Funding agency for:
Hopkinson, R
Grant:
studentships
+ William R. Miller Junior Research Fellowship
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Funding agency for:
Hopkinson, R
Grant:
studentships
+ Royal Society
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Funding agency for:
Kawamura, A
Grant:
Centre of Research Excellence Oxford (RE/13/1/30181
+ British Heart Foundation
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Funding agency for:
Kawamura, A
Grant:
Centre of Research Excellence Oxford (RE/13/1/30181
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Bibliographic Details
- Publisher:
- Nature Publishing Group Publisher's website
- Journal:
- Nature Communications Journal website
- Volume:
- 7
- Pages:
- 11974
- Publication date:
- 2016-06-23
- Acceptance date:
- 2016-05-17
- DOI:
- EISSN:
-
2041-1723
- Source identifiers:
-
629752
Item Description
- Language:
- English
- Pubs id:
-
pubs:629752
- UUID:
-
uuid:6baa5164-8b08-419a-a342-c8152ad20645
- Local pid:
- pubs:629752
- Deposit date:
- 2016-07-16
Terms of use
- Copyright holder:
- Walport et al
- Copyright date:
- 2016
- Notes:
- © 2016 the Author(s). This work is licensed under a Creative Commons Attribution 4.0 International License. The final version is available online from Nature Publishing Group at: [10.1038/ncomms11974].
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