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Journal article : Letter

The catalytic domains of all human KDM5 JmjC demethylases catalyse N-methyl arginine demethylation.

Abstract:

The demethylation of Nε -methyllysine residues on histones by Jumonji-C lysine demethylases (JmjC-KDMs) has been established. A subset of JmjC-KDMs has also been reported to have Nω -methylarginine residue demethylase (RDM) activity. Here, we describe biochemical screening studies, showing that the catalytic domains of all human KDM5s (KDM5A-KDM5D), KDM4E and, to a lesser extent, KDM4A/D, have both KDM and RDM activities with histone peptides. Ras GTPase-activating prote...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1002/1873-3468.14586

Authors


More by this author
Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Role:
Author
ORCID:
0000-0002-2723-6895
More by this author
Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Chemistry Research Laboratory
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Chemistry Research Laboratory
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Chemistry Research Laboratory
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MPLS
Department:
Chemistry
Sub department:
Organic Chemistry
Role:
Author
ORCID:
0000-0002-0290-6565
Publisher:
Wiley
Journal:
FEBS Letters More from this journal
Volume:
597
Issue:
7
Pages:
933-946
Publication date:
2023-02-07
Acceptance date:
2022-12-28
DOI:
EISSN:
1873-3468
ISSN:
0014-5793
Pmid:
36700827
Language:
English
Keywords:
Subtype:
Letter
Pubs id:
1326806
Local pid:
pubs:1326806
Deposit date:
2023-05-19

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