Linking covalent histone modifications to epigenetics: the rigidity and plasticity of the marks

Cold Spring Harb Symp Quant Biol. 2004;69:161-9. doi: 10.1101/sqb.2004.69.161.
No abstract available

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Amidohydrolases / genetics
  • Amino Acid Sequence
  • Animals
  • Cell Differentiation / genetics
  • Chromatin / genetics
  • Chromatin / metabolism
  • Cloning, Organism
  • Embryonic Development / genetics
  • Epigenesis, Genetic*
  • Female
  • Germ Cells / metabolism
  • Histone Methyltransferases
  • Histone-Lysine N-Methyltransferase / genetics
  • Histone-Lysine N-Methyltransferase / metabolism
  • Histones / genetics*
  • Histones / metabolism*
  • Humans
  • Hydrolases / genetics
  • Methylation
  • Mice
  • Models, Genetic
  • Molecular Sequence Data
  • Neoplasms / etiology
  • Neoplasms / genetics
  • Neoplasms / metabolism
  • Pregnancy
  • Protein Methyltransferases
  • Protein-Arginine Deiminases

Substances

  • Chromatin
  • Histones
  • Histone Methyltransferases
  • Protein Methyltransferases
  • Histone-Lysine N-Methyltransferase
  • Hydrolases
  • Amidohydrolases
  • Protein-Arginine Deiminases
  • dimethylargininase