4.8 Article

Serine is a new target residue for endogenous ADP-ribosylation on histones

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NATURE CHEMICAL BIOLOGY
卷 12, 期 12, 页码 998-+

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NATURE PUBLISHING GROUP
DOI: 10.1038/nchembio.2180

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资金

  1. Deutsche Forschungsgemeinschaft (Cellular Stress Responses in Aging-Associated Diseases) [EXC 229]
  2. European Union [657501]
  3. Wellcome Trust [101794]
  4. European Research Council [281739]
  5. Marie Curie Actions (MSCA) [657501] Funding Source: Marie Curie Actions (MSCA)
  6. European Research Council (ERC) [281739] Funding Source: European Research Council (ERC)

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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.

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