Journal article
Serine is a new target residue for endogenous ADP-ribosylation on histones
- Abstract:
- ADP-ribosylation (ADPr) is a biologically and clinically important post-translational modification, but little is known about the amino acids it targets on cellular proteins. Here we present a proteomic approach for direct in vivo identification and quantification of ADPr sites on histones. We have identified 12 unique ADPr sites in human osteosarcoma cells and report serine ADPr as a new type of histone mark that responds to DNA damage.
- Publication status:
- Published
- Peer review status:
- Peer reviewed
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- Files:
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(Preview, Accepted manuscript, pdf, 1013.8KB, Terms of use)
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(Preview, Accepted manuscript, pdf, 16.5MB, Terms of use)
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(Accepted manuscript, xlsx, 69.8KB, Terms of use)
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- Publisher copy:
- 10.1038/nchembio.2180
Authors
Bibliographic Details
- Publisher:
- Nature Publishing Group
- Journal:
- Nature Chemical Biology More from this journal
- Volume:
- 12
- Issue:
- 12
- Pages:
- 998-1000
- Publication date:
- 2016-10-10
- Acceptance date:
- 2016-07-21
- DOI:
- EISSN:
-
1552-4469
- ISSN:
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1552-4450
- Pmid:
-
27723750
Item Description
- Language:
-
English
- Keywords:
- Pubs id:
-
pubs:653384
- UUID:
-
uuid:0ef5b9a5-51fe-47d4-84a2-26801e838c39
- Local pid:
-
pubs:653384
- Source identifiers:
-
653384
- Deposit date:
-
2017-09-08
Terms of use
- Copyright holder:
- Leidecker et al
- Copyright date:
- 2016
- Notes:
- This is the accepted manuscript version of the article. The final version is available online from Nature Publishing Group at: https://doi.org/10.1038/nchembio.2180
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