DNA Double-stranded Breaks Induce Histone H2AX Phosphorylation on Serine 139

This publication has 36 references indexed in Scilit:

• Crystal structure of the nucleosome core particle at 2.8 Å resolution
  Nature, 1997
• Tetrahymena Histone Acetyltransferase A: A Homolog to Yeast Gcn5p Linking Histone Acetylation to Gene Activation
  Cell, 1996
• Histone Sequence Database: a compilation of highly-conserved nucleoprotein sequences
  Nucleic Acids Research, 1996
• Nucleosomal anatomy – where are the histones?
  BioEssays, 1995
• Phylogenetic analysis of the core histones H2A, H2B, H3, and H4
  Nucleic Acids Research, 1994
• The regulation of histone gene expression during the cell cycle
  Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression, 1991
• H2A.X. a histone isoprotein with a conserved C-terminal sequence, is encoded by a novel mRNA with both DNA replication type and polyA 3′ processing signals
  Nucleic Acids Research, 1989
• Histone 2A, a heteromorphous family of eight protein species
  Biochemistry, 1980
• Histone Phosphorylation and Chromatin Structure during Mitosis in Chinese Hamster Cells
  European Journal of Biochemistry, 1978
• Control of Cell Division by Very Lysine Rich Histone (F1) Phosphorylation
  Nature, 1974