Phosphorylation of Histone H2A.X by DNA-dependent Protein Kinase Is Not Affected by Core Histone Acetylation, but It Alters Nucleosome Stability and Histone H1 Binding

DNA-PKcs plays a dominant role in the regulation of H2AX phosphorylation in response to DNA damage and cell cycle progression

(2010) Jing An et al.   BMC MOLECULAR BIOLOGY

Repair of ionizing radiation-induced DNA double-strand breaks by non-homologous end-joining

(2009) Brandi L. Mahaney et al.   BIOCHEMICAL JOURNAL

Acetylation of Vertebrate H2A.Z and Its Effect on the Structure of the Nucleosome

(2009) Toyotaka Ishibashi et al.   BIOCHEMISTRY

γ-radiation-induced γH2AX formation occurs preferentially in actively transcribing euchromatic loci

(2009) Raja S. Vasireddy et al.   CELLULAR AND MOLECULAR LIFE SCIENCES

A distinct H2A.X isoform is enriched in Xenopus laevis eggs and early embryos and is phosphorylated in the absence of a checkpoint

(2009) David Shechter et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Genome-wide profiling of salt fractions maps physical properties of chromatin

(2008) S. Henikoff et al.   GENOME RESEARCH

FACT-Mediated Exchange of Histone Variant H2AX Regulated by Phosphorylation of H2AX and ADP-Ribosylation of Spt16

(2008) Kyu Heo et al.   MOLECULAR CELL

WSTF regulates the H2A.X DNA damage response via a novel tyrosine kinase activity

(2008) Andrew Xiao et al.   NATURE

The γ-H2A.X: Is it just a surrogate marker of double-strand breaks or much more?

(2007) Ismail Hassan Ismail et al.   ENVIRONMENTAL AND MOLECULAR MUTAGENESIS