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JMJD5 is a human arginyl C-3 hydroxylase

Abstract:

Oxygenase catalysed post-translational modifications of basic protein residues including lysyl hydroxylations and Nε-methyl lysyl demethylations have important cellular roles. Jumonji-C (JmjC) domain-containing protein 5 (JMJD5), which genetic studies reveal is essential in animal development, is reported as a histone Nε-methyl lysine demethylase (KDM). Here we report how extensive screening with peptides based on JMJD5 interacting proteins led to the finding that JMJ...

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Publication status:
Published
Peer review status:
Peer reviewed
Version:
Publisher's version

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Publisher copy:
10.1038/s41467-018-03410-w

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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 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 Division
Department:
Chemistry; Organic Chemistry
Role:
Author
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Funding agency for:
Markolovic, S
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Funding agency for:
Hopkinson, RJ
Wellcome Trust More from this funder
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Publisher:
Springer Nature Publisher's website
Journal:
Nature Communications Journal website
Volume:
9
Pages:
Article: 1180
Publication date:
2018-03-21
Acceptance date:
2018-03-05
DOI:
EISSN:
2041-1723
ISSN:
2041-1723
Pubs id:
pubs:830024
URN:
uri:4b6981ff-7976-4647-a72b-bdd6419b5a13
UUID:
uuid:4b6981ff-7976-4647-a72b-bdd6419b5a13
Local pid:
pubs:830024

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