Linking covalent histone modifications to epigenetics: the rigidity and plasticity of the marks.
Wang
Y
Y
Department of Genetic Medicine, Weill Medical College of Cornell University, New York, New York 10021, USA.
Wysocka
J
J
Perlin
J R
JR
Leonelli
L
L
Allis
C D
CD
Coonrod
S A
SA
D000581:Amidohydrolases / Q000235:genetics; D000595:Amino Acid Sequence; D000818:Animals; D002454:Cell Differentiation / Q000235:genetics; D002843:Chromatin / Q000235:genetics / Q000378:metabolism; D019976:Cloning, Organism; D047108:Embryonic Development / Q000235:genetics; D044127:Epigenesis, Genetic; D005260:Female; D005854:Germ Cells / Q000378:metabolism; D000076983:Histone Methyltransferases; D011495:Histone-Lysine N-Methyltransferase / Q000235:genetics / Q000378:metabolism; D006657:Histones / Q000235:genetics* / Q000378:metabolism*; D006801:Humans; D006867:Hydrolases / Q000235:genetics; D008745:Methylation; D051379:Mice; D008957:Models, Genetic; D008969:Molecular Sequence Data; D009369:Neoplasms / Q000209:etiology / Q000235:genetics / Q000378:metabolism; D011247:Pregnancy; D011496:Protein Methyltransferases; D000076342:Protein-Arginine Deiminases
D002843:Chromatin; D006657:Histones; D000076983:Histone Methyltransferases; D011496:Protein Methyltransferases; D011495:Histone-Lysine N-Methyltransferase; D006867:Hydrolases; D000581:Amidohydrolases; D000076342:Protein-Arginine Deiminases; C059999:dimethylargininase