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Journal article

Conversion of cysteine into dehydroalanine enables access to synthetic histones bearing diverse post-translational modifications.

Abstract:
Six for the price of one: From a single precursor, dehydroalanine, six distinct post-translational modifications can be site-selectively installed on histone proteins (see figure), including the first site-selective phosphorylation and glycosylation of histones. Direct observation of histone deacetylase activity on a full-length modified histone as well as its interactions with both chromatin reader and writer/eraser proteins are reported. © 2012 WILEY-VCH Verlag GmbH and Co. KGaA, Weinheim.
Publication status:
Published

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Publisher copy:
10.1002/anie.201106432

Authors


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
Department:
Chemistry
Sub department:
Organic Chemistry
Role:
Author


Journal:
Angewandte Chemie (International ed. in English) More from this journal
Volume:
51
Issue:
8
Pages:
1835-1839
Publication date:
2012-02-01
DOI:
EISSN:
1521-3773
ISSN:
1433-7851


Language:
English
Keywords:
Pubs id:
pubs:237395
UUID:
uuid:5403a6a2-0fa9-4f61-8d8a-dec6b9b9b638
Local pid:
pubs:237395
Source identifiers:
237395
Deposit date:
2012-12-19

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