Nishikawa, J <br/><br/>
Vitamin D receptor contains multiple dimerization interfaces that are functionally different.  [electronic resource] 

 -  Nucleic acids research  Feb 1995 
 - 606-11 p.  digital 
<br/><br/> Publication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>0305-1048 
<br/><br/><label>Standard No.: </label>10.1093/nar/23.4.606  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Amino Acid Sequence<br/>Animals<br/>Calcitriol--metabolism<br/>DNA--metabolism<br/>Ligands<br/>Molecular Sequence Data<br/>Polymerase Chain Reaction<br/>Protein Binding<br/>Protein Conformation<br/>Protein Multimerization<br/>Protein Structure, Tertiary<br/>Rats<br/>Receptors, Calcitriol--chemistry<br/>Receptors, Retinoic Acid--chemistry<br/>Recombinant Fusion Proteins--chemistry<br/>Retinoid X Receptors<br/>Sequence Alignment<br/>Sequence Deletion<br/>Sequence Homology, Amino Acid<br/>Transcription Factors--chemistry<br/>Zinc Fingers