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In vitro enzyme assays for JmjC-domain-containing lysine histone demethylases (JmjC-KDMs)

Abstract:

Histone modifications, including lysine methylation marks on histone tails, modulate the accessibility of genes for transcription. Changes in histone tail methylation patterns can cause transcriptional activation or repression. The dynamic regulation of lysine methylation patterns is enabled by two distinct groups of enzymes: histone methyltransferases (KMTs) and demethylases (KDMs). The Jumonji C (JmjC) domain–containing lysine histone demethylases (JmjC‐KDMs) alter the methylation levels of...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1002/cpph.34

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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
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
Publisher:
Wiley Publisher's website
Journal:
Current Protocols in Pharmacology Journal website
Volume:
80
Issue:
1
Pages:
3.15.1-3.15.12
Publication date:
2018-04-02
Acceptance date:
2017-10-06
DOI:
EISSN:
1934-8290
Source identifiers:
734756
Keywords:
Pubs id:
pubs:734756
UUID:
uuid:48c026db-3bac-4adb-9ac5-7fed28048226
Local pid:
pubs:734756
Deposit date:
2017-10-09

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