Journal article
Potent and selective KDM5 inhibitor stops cellular demethylation of H3K4me3 at transcription start sites and proliferation of MM1S myeloma cells
- Abstract:
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Methylation of lysine residues on histone tail is a dynamic epigenetic modification that plays a key role in chromatin structure and gene regulation. Members of the KDM5 (also known as JARID1) sub-family are 2-oxoglutarate (2-OG) and Fe2+-dependent oxygenases acting as histone 3 lysine 4 trimethyl (H3K4me3) demethylases, regulating proliferation, stem cell self-renewal, and differentiation. Here we present the characterization of KDOAM-25, an inhibitor of KDM5 enzymes. KDOAM-25 shows bioch...
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- Publication status:
- Published
- Peer review status:
- Peer reviewed
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(Preview, Version of record, pdf, 2.6MB, Terms of use)
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(Preview, Version of record, pdf, 820.7KB, Terms of use)
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- Publisher copy:
- 10.1016/j.chembiol.2017.02.006
Authors
Funding
+ Royal Society
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Funding agency for:
Kawamura, A
Grant:
Dorothy Hodgkin Research Fellow
Bibliographic Details
- Publisher:
- Elsevier
- Journal:
- Cell Chemical Biology More from this journal
- Publication date:
- 2017-03-02
- Acceptance date:
- 2017-02-01
- DOI:
- ISSN:
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2451-9456
Item Description
- Language:
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English
- Keywords:
- Pubs id:
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pubs:684148
- UUID:
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uuid:ed7f02af-e1f0-49ca-b094-477e2a4b81fb
- Local pid:
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pubs:684148
- Deposit date:
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2017-03-07
Terms of use
- Copyright holder:
- Schofield et al
- Copyright date:
- 2017
- Notes:
- © 2017 The Authors. Published by Elsevier Ltd. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
- Licence:
- CC Attribution (CC BY)
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