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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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Publisher copy:
10.1021/acs.jmedchem.9b00562

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Institution:
University of Oxford
Department:
NDM
Role:
Author
More by this author
Institution:
University of Oxford
Department:
NDORMS
Role:
Author
More by this author
Institution:
University of Oxford
Department:
NDORMS
Role:
Author
More by this author
Institution:
University of Oxford
Department:
NDM
Role:
Author
More by this author
Institution:
University of Oxford
Department:
NDORMS
Role:
Author
Publisher:
American Chemical Society
Journal:
Journal of Medicinal Chemistry More from this journal
Volume:
62
Issue:
20
Pages:
9008-9025
Publication date:
2019-09-24
Acceptance date:
2019-09-24
DOI:
EISSN:
1520-4804
ISSN:
0022-2623
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

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