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Journal article

Inhibitors of both the N-methyl lysyl- and arginyl- demethylase activities of the JmjC oxygenases

Abstract:

The Jumonji C (JmjC) family of 2-oxoglutarate (2OG) dependent oxygenases have established roles in the regulation of transcription via the catalysis of demethylation of Nε-methylated lysine residues in histone tails, especially the N-terminal tail of histone H3. Most human JmjC KDMs are complex enzymes, with ‘reader domains’ in addition to their catalytic domains. Recent biochemical evidence has shown that some, but not all, JmjC KDMs also have Nω-methyl arginyl demethylase (RDM) activity. Jm...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1098/rstb.2017.0071

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Institution:
University of Oxford
Division:
MPLS Division
Department:
Chemistry; Organic Chemistry
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MPLS Division
Department:
Chemistry; Organic Chemistry
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Organic Chemistry
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MPLS Division
Department:
Chemistry; Organic Chemistry
Role:
Author
More from this funder
Funding agency for:
Schofield, C
Grant:
C8717/A18245
Wellcome Trust More from this funder
More from this funder
Funding agency for:
Kawamura, A
Grant:
Dorothy Hodgkin Fellowship
More from this funder
Funding agency for:
Kawamura, A
Grant:
Dorothy Hodgkin Fellowship
Publisher:
Royal Society Publisher's website
Journal:
Philosophical Transactions B: Biological Sciences Journal website
Volume:
373
Issue:
1748
Article number:
20170071
Publication date:
2018-04-23
Acceptance date:
2017-10-03
DOI:
EISSN:
1471-2970
ISSN:
0962-8436
Source identifiers:
734762
Keywords:
Pubs id:
pubs:734762
UUID:
uuid:6bb258ff-9002-4ea9-9153-4c6c4a55dd4b
Local pid:
pubs:734762
Deposit date:
2017-10-09

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