Acetylation of estrogen receptor alpha by p300 at lysines 266 and 268 enhances the deoxyribonucleic acid binding and transactivation activities of the receptor.

Kim, Mi Young

Acetylation of estrogen receptor alpha by p300 at lysines 266 and 268 enhances the deoxyribonucleic acid binding and transactivation activities of the receptor. [electronic resource] - Molecular endocrinology (Baltimore, Md.) Jul 2006 - 1479-93 p. digital

Publication Type: Comparative Study; Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't

0888-8809

10.1210/me.2005-0531 doi


Acetylation
Amino Acid Sequence
Animals
Binding Sites
Cats
Cell Compartmentation
Cells, Cultured
Conserved Sequence
Cricetinae
DNA--metabolism
Estrogen Receptor alpha--metabolism
Estrogen Receptor beta--metabolism
Estrogens--metabolism
Humans
Hydroxamic Acids--pharmacology
Lysine--metabolism
Mass Spectrometry
Mice
Molecular Sequence Data
Niacinamide--pharmacology
Nuclear Receptor Coactivator 2--metabolism
Point Mutation
Protein Structure, Tertiary
Rats
Sequence Alignment
Sirtuins--metabolism
Transcriptional Activation
p300-CBP Transcription Factors--metabolism