Kim, Mi Young <br/><br/>
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 
<br/><br/> Publication Type: Comparative Study; Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>0888-8809 
<br/><br/><label>Standard No.: </label>10.1210/me.2005-0531  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Acetylation<br/>Amino Acid Sequence<br/>Animals<br/>Binding Sites<br/>Cats<br/>Cell Compartmentation<br/>Cells, Cultured<br/>Conserved Sequence<br/>Cricetinae<br/>DNA--metabolism<br/>Estrogen Receptor alpha--metabolism<br/>Estrogen Receptor beta--metabolism<br/>Estrogens--metabolism<br/>Humans<br/>Hydroxamic Acids--pharmacology<br/>Lysine--metabolism<br/>Mass Spectrometry<br/>Mice<br/>Molecular Sequence Data<br/>Niacinamide--pharmacology<br/>Nuclear Receptor Coactivator 2--metabolism<br/>Point Mutation<br/>Protein Structure, Tertiary<br/>Rats<br/>Sequence Alignment<br/>Sirtuins--metabolism<br/>Transcriptional Activation<br/>p300-CBP Transcription Factors--metabolism