Journal article
A chemical probe for Tudor domain protein spindlin1 to investigate chromatin function
- Abstract:
-
Modifications of histone tails, including lysine/arginine methylation, provide the basis of a “chromatin or histone code”. Proteins that contain “reader” domains can bind to these modifications and form specific effector complexes, which ultimately mediate chromatin function. The spindlin1 (SPIN1) protein contains three Tudor methyllysine/arginine reader domains and was identified as a putative oncogene and transcriptional coactivator. Here we report a SPIN1 chemical probe inhibitor with low ...
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- Publication status:
- Published
- Peer review status:
- Peer reviewed
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Authors
Bibliographic Details
- Publisher:
- American Chemical Society Publisher's website
- Journal:
- Journal of Medicinal Chemistry Journal website
- Volume:
- 62
- Issue:
- 20
- Pages:
- 9008-9025
- Publication date:
- 2019-09-24
- Acceptance date:
- 2019-09-24
- DOI:
- EISSN:
-
1520-4804
- ISSN:
-
0022-2623
Item Description
- Language:
- English
- Keywords:
- Pubs id:
-
pubs:1055773
- UUID:
-
uuid:6a9d4c56-2bde-4124-a7d5-02e47ec9621a
- Local pid:
- pubs:1055773
- Source identifiers:
-
1055773
- Deposit date:
- 2019-09-26
Terms of use
- Copyright holder:
- American Chemical Society
- Copyright date:
- 2019
- Rights statement:
- Copyright © 2019 American Chemical Society
- Notes:
- This is the accepted manuscript version of the article. The final version is available online from the American Chemical Society at: https://doi.org/10.1021/acs.jmedchem.9b00562
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