Nature Communications (Mar 2019)

Reversible histone glycation is associated with disease-related changes in chromatin architecture

  • Qingfei Zheng,
  • Nathaniel D. Omans,
  • Rachel Leicher,
  • Adewola Osunsade,
  • Albert S. Agustinus,
  • Efrat Finkin-Groner,
  • Hannah D’Ambrosio,
  • Bo Liu,
  • Sarat Chandarlapaty,
  • Shixin Liu,
  • Yael David

DOI
https://doi.org/10.1038/s41467-019-09192-z
Journal volume & issue
Vol. 10, no. 1
pp. 1 – 12

Abstract

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Proteins continuously undergo non-enzymatic modifications such as glycation, which accumulate under physiological conditions but can be enhanced in disease. Here the authors characterise histone glycation, provide evidence that it affects chromatin, particularly in breast cancer, and identify DJ-1 as a deglycase.